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Database: UniProt
Entry: T1FM14_HELRO
LinkDB: T1FM14_HELRO
Original site: T1FM14_HELRO 
ID   T1FM14_HELRO            Unreviewed;       310 AA.
AC   T1FM14;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=20209863 {ECO:0000313|EnsemblMetazoa:HelroP184809};
GN   ORFNames=HELRODRAFT_184809 {ECO:0000313|EMBL:ESO11968.1};
OS   Helobdella robusta (Californian leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX   NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP184809, ECO:0000313|Proteomes:UP000015101};
RN   [1] {ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESO11968.1, ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:HelroP184809}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; AMQM01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB095811; ESO11968.1; -; Genomic_DNA.
DR   RefSeq; XP_009008688.1; XM_009010440.1.
DR   AlphaFoldDB; T1FM14; -.
DR   STRING; 6412.T1FM14; -.
DR   EnsemblMetazoa; HelroT184809; HelroP184809; HelroG184809.
DR   GeneID; 20209863; -.
DR   KEGG; hro:HELRODRAFT_184809; -.
DR   CTD; 20209863; -.
DR   eggNOG; KOG0311; Eukaryota.
DR   HOGENOM; CLU_056557_1_1_1; -.
DR   InParanoid; T1FM14; -.
DR   OMA; LHNELMC; -.
DR   OrthoDB; 460116at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000015101; Unassembled WGS sequence.
DR   GO; GO:0031519; C:PcG protein complex; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16740; RING-HC_RING2; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR032443; RAWUL.
DR   InterPro; IPR043540; RING1/RING2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46076:SF3; E3 UBIQUITIN-PROTEIN LIGASE RING1; 1.
DR   PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR   Pfam; PF16207; RAWUL; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          45..85
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          145..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  34805 MW;  3A7CA22ACA6AE3FE CRC64;
     MEQPPTPSKT WGLTPYELHR TPQEAVTDNT EIAVSPRSLH NELMCPICLD MLKNTMTTKE
     CLHRFCQECI ITALRSGNKE CPTCRKKLIS KRSLRPDPNF DALISKIYPC RDEYDAHQER
     VLAKLKQTMN PAALTQNIEE GLRQQALSRN QRKKVTDSES NDTPRKHHGN SDESAGENSM
     CGDVSSEGPS TGRPTNKSPP EIELVFKPHP SHSDSNSTQV RYIKTTSNAS IEHLSKYLAM
     RIALEKQQIN PGARILSNPP SDKYNIFIST SLAEGLLLLP GNLSLAQTSE KYWHSTKPMV
     LYYALDLQAC
//
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