##gff-version 3 
Transcript_1	rpstblastn	match_part	204	257	2.00e-06	-	0	Target=pfam00415 204 257;hin=1;hsn=1;hs=0;hf=0;hsl=54;hil=50;ql=257;pi=66.67;qc=21.01;hc=36.00;d=pfam00415  RCC1  Regulator of chromosome condensation (RCC1) repeat.
Transcript_2	rpstblastn	match_part	67	300	2.00e-10	-	0	Target=pfam12776 67 300;hin=1;hsn=1;hs=0;hf=0;hsl=234;hil=95;ql=303;pi=32.91;qc=77.23;hc=82.11;d=pfam12776  Myb_DNA-bind_3  Myb/SANT-like DNA-binding domain. This presumed domain appears to be related to other Myb/SANT like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.
Transcript_4	rpstblastn	match_part	1	126	5.00e-23	-	0	Target=pfam04640 1 126;hin=1;hsn=1;hs=0;hf=0;hsl=126;hil=73;ql=446;pi=64.29;qc=28.25;hc=57.53;d=pfam04640  PLATZ  PLATZ transcription factor. Plant AT-rich sequence and zinc-binding proteins (PLATZ) are zinc dependant DNA binding proteins. They bind to AT rich sequences and functions in transcriptional repression.
Transcript_6	rpstblastn	match_part	38	166	1.00e-12	-	0	Target=COG2217 38 166;hin=1;hsn=1;hs=0;hf=0;hsl=129;hil=713;ql=395;pi=58.14;qc=32.66;hc=5.89;d=COG2217  ZntA  Cation transport ATPase  Inorganic ion transport and metabolism .
Transcript_6	rpstblastn	match_part	38	166	3.00e-12	-	0	Target=cd00371 38 166;hin=2;hsn=1;hs=0;hf=0;hsl=129;hil=63;ql=395;pi=51.16;qc=32.66;hc=68.25;d=cd00371  HMA  Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals for example  the CPx-type heavy metal ATPases and copper chaperones.HMA domain contains two cysteine residues that are important in binding and transfer of metal ions  such as copper cadmium  cobalt and zinc. In the case of copper  stoichiometry of binding is one Cu  ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.
Transcript_6	rpstblastn	match_part	38	166	4.00e-11	-	0	Target=pfam00403 38 166;hin=3;hsn=1;hs=0;hf=0;hsl=129;hil=58;ql=395;pi=44.19;qc=32.66;hc=74.14;go=GO:0046872,GO:0030001,;d=pfam00403  HMA  Heavy-metal-associated domain. 
Transcript_6	rpstblastn	match_part	2	166	4.00e-09	-	0	Target=COG2608 2 166;hin=4;hsn=1;hs=0;hf=0;hsl=165;hil=71;ql=395;pi=36.36;qc=41.77;hc=76.06;d=COG2608  CopZ  Copper chaperone  Inorganic ion transport and metabolism .
Transcript_6	rpstblastn	match_part	2	166	2.00e-07	-	0	Target=PRK10671 2 166;hin=5;hsn=1;hs=0;hf=0;hsl=165;hil=834;ql=395;pi=37.50;qc=41.77;hc=6.12;d=PRK10671  copA  copper exporting ATPase  Provisional.
Transcript_9	rpstblastn	match_part	198	290	4.00e-07	-	0	Target=COG5191 198 290;hin=1;hsn=1;hs=0;hf=0;hsl=93;hil=435;ql=290;pi=48.39;qc=32.07;hc=7.13;d=COG5191  COG5191  Uncharacterized conserved protein  contains HAT (Half-A-TPR) repeat  General function prediction only .
Transcript_10	rpstblastn	match_part	9	80	2.00e-09	-	0	Target=pfam17123 9 80;hin=1;hsn=1;hs=0;hf=0;hsl=72;hil=29;ql=240;pi=45.83;qc=30.00;hc=82.76;d=pfam17123  zf-RING_11  RING-like zinc finger. 
Transcript_10	rpstblastn	match_part	3	80	3.00e-08	-	0	Target=cd16468 3 80;hin=2;hsn=1;hs=0;hf=0;hsl=78;hil=43;ql=240;pi=57.69;qc=32.50;hc=60.47;d=cd16468  RING-H2_RNF11  RING finger  H2 subclass  found in RING finger protein 11 (RNF11) and similar proteins. RNF11 is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It is the downstream of an enzymatic cascade for the ubiquitination of specific substrates.It is also a molecular adaptor of homologous to E6-associated protein C-terminus (HECT)-type ligases. RNF11 has been implicated in the regulation of several signaling pathways.It enhances the transforming growth factor receptor (TGFR)signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM) a de-ubiquitinating enzyme that enhances transforming growth factor-beta (TGF-beta) signaling and epidermal growth factor receptor (EGFR) endosomal recycling. It also acts directly on Smad4 to enhance Smad4 function  and plays a role in prolonged TGF-beta signaling. Moreover  RNF11 functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation. It also interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex thus participating in the regulation of lysosomal degradation of EGFR. Furthermore  RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family. In addition  RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi  and further restricts antiviral signaling and type I interferon (IFN)-beta production. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch  Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2)  and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13.
Transcript_10	rpstblastn	match_part	3	83	2.00e-07	-	0	Target=pfam13639 3 83;hin=3;hsn=1;hs=0;hf=0;hsl=81;hil=44;ql=240;pi=44.44;qc=33.75;hc=61.36;d=pfam13639  zf-RING_2  Ring finger domain. 
Transcript_10	rpstblastn	match_part	9	80	2.00e-07	-	0	Target=cd16486 9 80;hin=4;hsn=1;hs=0;hf=0;hsl=72;hil=44;ql=240;pi=50.00;qc=30.00;hc=54.55;d=cd16486  mRING-H2-C3H2C2D_ZSWM2  Modified RING finger  H2 subclass (C3H2C2D-type)  found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins. ZSWIM2  also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2  is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas  death receptor (DR) 3 and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It also acts as an E3 ubiquitin ligase  through the E2  Ub-conjugating enzymes UbcH5a  UbcH5c  or UbcH6.ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination  and two modified RING-H2 fingers separated by a ZZ zinc finger domain  which was required for interaction with UbcH5a and its self-association. This family corresponds to the second RING-H2 finger  which is not a canonical C3H2C3-type  but a modified C3H2C2D-type.
Transcript_10	rpstblastn	match_part	9	80	6.00e-07	-	0	Target=cd16473 9 80;hin=5;hsn=1;hs=0;hf=0;hsl=72;hil=46;ql=240;pi=37.50;qc=30.00;hc=52.17;d=cd16473  RING-H2_RNF103  RING finger  H2 subclass  found in RING finger protein 103 (RNF103) and similar proteins. RNF103 also known as KF-1  or zinc finger protein 103 homolog (Zfp-103) is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs  including brain  heart  kidney  spleen  and lung.It is involved in the ER-associated degradation (ERAD) pathway through interacting with components of the ERAD pathway including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions  as well as a C-terminal C3H2C3-type RING-H2 finger.
Transcript_10	rpstblastn	match_part	9	80	7.00e-07	-	0	Target=cd16454 9 80;hin=6;hsn=1;hs=0;hf=0;hsl=72;hil=43;ql=240;pi=50.00;qc=30.00;hc=55.81;d=cd16454  RING-H2_PA-TM-RING  RING finger  H2 subclass  found in the PA-TM-RING ubiquitin ligase family. The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases  which has been characterized by an N-terminal transient signal peptide  a PA (protease-associated) domain  a TM(transmembrane) domain  as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13  RNF167  ZNRF4 (zinc and RING finger 4)  GRAIL (gene related to anergy in lymphocytes)/RNF128 RNF130  RNF133  RNF148  RNF149 and RNF150 (which are more closely related)  as well as RNF43 and ZNRF3 which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species  but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting  suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer.
Transcript_10	rpstblastn	match_part	9	80	8.00e-07	-	0	Target=cd16667 9 80;hin=7;hsn=1;hs=0;hf=0;hsl=72;hil=43;ql=240;pi=50.00;qc=30.00;hc=55.81;d=cd16667  RING-H2_RNF126_like  RING finger  H2 subclass  found in RING finger proteins RNF126  RNF115  and similar proteins. The family includes RING finger proteins RNF126  RNF115 and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP)pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor(CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase(AID)  a poorly soluble protein that is essential for antibody diversification. RNF115  also known as Rab7-interacting ring finger protein (Rabring 7)  or zinc finger protein 364 (ZNF364)  or breast cancer-associated gene 2 (BCA2) is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK)activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1  and targets HIV-1 Gag for lysosomal degradation  impairing virus assembly and release  in a tetherin-independent manner. Moreover RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. RNF115 and RNF126 associate with the epidermal growth factor receptor(EGFR) and promote ubiquitylation of EGFR  suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF)  the AKT-phosphorylation sites  and the C-terminal C3H2C3-type RING-H2 finger.
Transcript_10	rpstblastn	match_part	9	86	9.00e-07	-	0	Target=COG5540 9 86;hin=8;hsn=1;hs=0;hf=0;hsl=78;hil=374;ql=240;pi=50.00;qc=32.50;hc=6.95;d=COG5540  COG5540  RING-finger-containing ubiquitin ligase  Posttranslational modification  protein turnover  chaperones .
Transcript_10	rpstblastn	match_part	9	77	5.00e-06	-	0	Target=cd16665 9 77;hin=9;hsn=1;hs=0;hf=0;hsl=69;hil=46;ql=240;pi=52.17;qc=28.75;hc=50.00;d=cd16665  RING-H2_RNF13_like  RING finger  H2 subclass  found in RING finger protein 13 (RNF13)  RING finger protein 167 (RNF167) and similar proteins. This subfamily includes RING finger protein 13 (RNF13)  RING finger protein 167 (RNF167) Zinc/RING finger protein 4 (ZNRF4)  and similar proteins which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide  a protease-associated (PA) domain  a transmembrane domain (TM)  and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development  muscle cell growth  and neuronal development.Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167 also known as RING105  is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination.It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover  RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA  also known as ORCTL2/IMPT1/BWR1A/SLC22A1L) which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4  also known as RING finger protein 204 (RNF204)  or Nixin  is an endoplasmic reticulum(ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner  induces calnexin ubiquitination and p97-dependent degradation  indicating an ER-associated degradation-like mechanism of calnexin turnover. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and involved in spermatogenesis.
Transcript_10	rpstblastn	match_part	9	77	9.00e-06	-	0	Target=cd16448 9 77;hin=10;hsn=1;hs=0;hf=0;hsl=69;hil=44;ql=240;pi=54.17;qc=28.75;hc=54.55;d=cd16448  RING-H2  H2 subclass of RING (RING-H2) finger and its variants. RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the  cross-brace  motif that chelates zinc atoms by eight amino acid residues  typically Cys or His  arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses  RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type)  according to their Cys/His content.There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially  the fourth or eighth zinc ligand is prevalently exchanged for an Asp  which can indeed chelate Zn in a RING finger as well. This family corresponds to H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants  including C4HC3- (RING-CH alias RINGv)  C3H3C2-  C3H2C2D-  C3DHC3- and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique  cross-brace  arrangement  which distinguishes it from tandem zinc fingers and other similar motifs.RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions  including oncogenesis development  viral replication  signal transduction  the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s  also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins  which enables efficient transfer of ubiquitin from E2 to the substrates.
Transcript_10	rpstblastn	match_part	9	80	1.00e-05	-	0	Target=cd16461 9 80;hin=11;hsn=1;hs=0;hf=0;hsl=72;hil=43;ql=240;pi=41.67;qc=30.00;hc=55.81;d=cd16461  RING-H2_EL5_like  RING finger  H2 subclass  found in rice E3 ubiquitin-protein ligase EL5 and similar proteins. EL5  also known as protein ELICITOR 5  is an E3 ubiquitin-protein ligase containing an N-terminal transmembrane domain and a C3H2C3-type RING-H2 finger that is a binding site for ubiquitin-conjugating enzyme (E2). It can be rapidly induced by N-acetylchitooligosaccharide elicitor. EL5 catalyzes polyubiquitination via the Lys48 residue of ubiquitin  and thus plays a crucial role as a membrane-anchored E3 in the maintenance of cell viability after the initiation of root primordial formation in rice. It also acts as an anti-cell death enzyme that might be responsible for mediating the degradation of cytotoxic proteins produced in root cells after the actions of phytohormones. Moreover  EL5 interacts with UBC5b  a rice ubiquitin carrier protein  through its RING-H2 finger.EL5 is an unstable protein  and its degradation is regulated by the C3H2C3-type RING-H2 finger in a proteasome-independent manner.
Transcript_12	rpstblastn	match_part	2	202	7.00e-15	-	0	Target=PTZ00368 2 202;hin=1;hsn=1;hs=0;hf=0;hsl=201;hil=148;ql=212;pi=32.84;qc=94.81;hc=45.27;d=PTZ00368  PTZ00368  universal minicircle sequence binding protein (UMSBP)  Provisional.
Transcript_12	rpstblastn	match_part	2	208	1.00e-13	-	0	Target=PTZ00368 2 208;hin=1;hsn=2;hs=0;hf=0;hsl=207;hil=148;ql=212;pi=30.43;qc=97.64;hc=45.95;d=PTZ00368  PTZ00368  universal minicircle sequence binding protein (UMSBP)  Provisional.
Transcript_12	rpstblastn	match_part	2	208	3.00e-13	-	0	Target=PTZ00368 2 208;hin=1;hsn=3;hs=0;hf=0;hsl=207;hil=148;ql=212;pi=35.71;qc=97.64;hc=46.62;d=PTZ00368  PTZ00368  universal minicircle sequence binding protein (UMSBP)  Provisional.
Transcript_12	rpstblastn	match_part	2	178	2.00e-08	-	0	Target=PTZ00368 2 178;hin=1;hsn=4;hs=0;hf=0;hsl=177;hil=148;ql=212;pi=31.15;qc=83.49;hc=40.54;d=PTZ00368  PTZ00368  universal minicircle sequence binding protein (UMSBP)  Provisional.
Transcript_12	rpstblastn	match_part	62	208	4.00e-06	-	0	Target=PTZ00368 62 208;hin=1;hsn=5;hs=0;hf=0;hsl=147;hil=148;ql=212;pi=34.00;qc=69.34;hc=33.78;d=PTZ00368  PTZ00368  universal minicircle sequence binding protein (UMSBP)  Provisional.
Transcript_12	rpstblastn	match_part	2	196	1.00e-10	-	0	Target=COG5082 2 196;hin=2;hsn=1;hs=0;hf=0;hsl=195;hil=190;ql=212;pi=32.31;qc=91.98;hc=26.84;d=COG5082  AIR1  Arginine methyltransferase-interacting protein  contains RING Zn-finger  Posttranslational modification  protein turnover  chaperones / Intracellular trafficking and secretion .
Transcript_12	rpstblastn	match_part	11	178	2.00e-06	-	0	Target=COG5082 11 178;hin=2;hsn=2;hs=0;hf=0;hsl=168;hil=190;ql=212;pi=28.12;qc=79.25;hc=32.63;d=COG5082  AIR1  Arginine methyltransferase-interacting protein  contains RING Zn-finger  Posttranslational modification  protein turnover  chaperones / Intracellular trafficking and secretion .
Transcript_16	rpstblastn	match_part	3	104	2.00e-08	-	0	Target=pfam01391 3 104;hin=1;hsn=1;hs=0;hf=0;hsl=102;hil=60;ql=249;pi=52.94;qc=40.96;hc=53.33;d=pfam01391  Collagen  Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily.Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine  the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Transcript_16	rpstblastn	match_part	12	104	3.00e-08	-	0	Target=pfam01391 12 104;hin=1;hsn=2;hs=0;hf=0;hsl=93;hil=60;ql=249;pi=54.84;qc=37.35;hc=48.33;d=pfam01391  Collagen  Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily.Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine  the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Transcript_16	rpstblastn	match_part	3	104	3.00e-08	-	0	Target=pfam01391 3 104;hin=1;hsn=3;hs=0;hf=0;hsl=102;hil=60;ql=249;pi=52.94;qc=40.96;hc=53.33;d=pfam01391  Collagen  Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily.Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine  the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Transcript_16	rpstblastn	match_part	3	107	1.00e-07	-	0	Target=pfam01391 3 107;hin=1;hsn=4;hs=0;hf=0;hsl=105;hil=60;ql=249;pi=50.00;qc=42.17;hc=60.00;d=pfam01391  Collagen  Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily.Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine  the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Transcript_16	rpstblastn	match_part	3	104	1.00e-06	-	0	Target=pfam01391 3 104;hin=1;hsn=5;hs=0;hf=0;hsl=102;hil=60;ql=249;pi=51.43;qc=40.96;hc=58.33;d=pfam01391  Collagen  Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily.Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine  the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Transcript_16	rpstblastn	match_part	3	101	5.00e-06	-	0	Target=pfam01391 3 101;hin=1;hsn=6;hs=0;hf=0;hsl=99;hil=60;ql=249;pi=51.52;qc=39.76;hc=51.67;d=pfam01391  Collagen  Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily.Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine  the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Transcript_21	rpstblastn	match_part	112	465	2.00e-22	-	0	Target=pfam01151 112 465;hin=1;hsn=1;hs=0;hf=0;hsl=354;hil=244;ql=468;pi=29.37;qc=75.64;hc=49.18;go=GO:0016021,;d=pfam01151  ELO  GNS1/SUR4 family. Members of this family are involved in long chain fatty acid elongation systems that produce the 26-carbon precursors for ceramide and sphingolipid synthesis. Predicted to be integral membrane proteins  in eukaryotes they are probably located on the endoplasmic reticulum.Yeast ELO3 affects plasma membrane H -ATPase activity and may act on a glucose-signaling pathway that controls the expression of several genes that are transcriptionally regulated by glucose such as PMA1.
Transcript_22	rpstblastn	match_part	79	171	2.00e-07	-	0	Target=smart00066 79 171;hin=1;hsn=1;hs=0;hf=0;hsl=93;hil=43;ql=292;pi=34.38;qc=31.85;hc=74.42;d=smart00066  GAL4  GAL4-like Zn(II)2Cys6 (or C6 zinc) binuclear cluster DNA-binding domain. Gal4 is a positive regulator for the gene expression of the galactose- induced genes of S.cerevisiae. Is present only in fungi.
Transcript_22	rpstblastn	match_part	79	171	2.00e-07	-	0	Target=cd00067 79 171;hin=2;hsn=1;hs=0;hf=0;hsl=93;hil=36;ql=292;pi=40.62;qc=31.85;hc=88.89;d=cd00067  GAL4  GAL4-like Zn2Cys6 binuclear cluster DNA-binding domain  found in transcription regulators like GAL4. Domain consists of two helices organized around a Zn(2)Cys(6 )motif Binds to sequences containing 2 DNA half sites comprised of 3-5 C/G combinations.
Transcript_24	rpstblastn	match_part	20	343	1.00e-52	-	0	Target=cd07481 20 343;hin=1;hsn=1;hs=0;hf=0;hsl=324;hil=264;ql=343;pi=51.67;qc=94.46;hc=45.45;d=cd07481  Peptidases_S8_BacillopeptidaseF-like  Peptidase S8 family domain in BacillopeptidaseF-like proteins. Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F encoded by bpr  a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases  but do not share their three-dimensional structure and are not homologous to trypsin. The stability of these enzymes may be enhanced by calcium  some members have been shown to bind up to 4 ions via binding sites with different affinity.