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Database: UniProt
Entry: G4TAG4_SERID
LinkDB: G4TAG4_SERID
Original site: G4TAG4_SERID 
ID   G4TAG4_SERID            Unreviewed;       785 AA.
AC   G4TAG4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   16-OCT-2019, entry version 52.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=PIIN_02180 {ECO:0000313|EMBL:CCA68316.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA68316.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA68316.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA68316.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S.,
RA   Biedenkopf D., Wong P., Samans B., Grimm C., Basiewicz M., Murat C.,
RA   Martin F., Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome
RT   Analyses of the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC         protein]-L-lysine.; EC=2.3.2.27;
CC         Evidence={ECO:0000256|RuleBase:RU365038};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|RuleBase:RU365038}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365038}.
CC   -!- SIMILARITY: Belongs to the BRE1 family.
CC       {ECO:0000256|RuleBase:RU365038}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCA68316.1}.
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DR   EMBL; CAFZ01000030; CCA68316.1; -; Genomic_DNA.
DR   STRING; 65672.G4TAG4; -.
DR   EnsemblFungi; CCA68316; CCA68316; PIIN_02180.
DR   InParanoid; G4TAG4; -.
DR   OMA; RTDVFKQ; -.
DR   OrthoDB; 782448at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007148; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010390; P:histone monoubiquitination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163; PTHR23163; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|RuleBase:RU365038};
KW   Coiled coil {ECO:0000256|RuleBase:RU365038, ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007148};
KW   Metal-binding {ECO:0000256|RuleBase:RU365038};
KW   Nucleus {ECO:0000256|RuleBase:RU365038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW   Transferase {ECO:0000256|RuleBase:RU365038};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW   Zinc {ECO:0000256|RuleBase:RU365038};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175,
KW   ECO:0000256|RuleBase:RU365038}.
FT   DOMAIN      732    771       RING-type. {ECO:0000259|PROSITE:PS50089}.
FT   REGION      190    219       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED       30     50       {ECO:0000256|SAM:Coils}.
FT   COILED      137    157       {ECO:0000256|SAM:Coils}.
FT   COILED      255    275       {ECO:0000256|SAM:Coils}.
FT   COILED      333    367       {ECO:0000256|SAM:Coils}.
FT   COILED      433    453       {ECO:0000256|SAM:Coils}.
FT   COILED      464    491       {ECO:0000256|SAM:Coils}.
FT   COILED      497    531       {ECO:0000256|SAM:Coils}.
FT   COILED      560    580       {ECO:0000256|SAM:Coils}.
FT   COILED      609    629       {ECO:0000256|SAM:Coils}.
FT   COILED      644    671       {ECO:0000256|SAM:Coils}.
FT   COILED      679    706       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    190    205       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   785 AA;  89271 MW;  5B13E6B9950336C6 CRC64;
     MTPVSPSAVA DEPQNAEIES FRKEAIYRRM QHYSRELERS QHVVSQLESK TLSYEAALVA
     IETCWDQLLQ QVRLLVKPGE LQDVEDQSAL FALAQDVDAE GKIGNAYMDA IKAKESLTVN
     TIRAVVASTP ALARPDVQDL QNMAHRLRSQ LSSISGELAL TKAKLEESVA SVETYRELLS
     TAENRLERLK STTVQKLEAK PQPKEEPEPS SQSNGNGTLI KAEPMQTTAP DMNGHVSSEE
     VEEWKYRAEE RLRTIEDFQK EHFELRQQIS KLKTQLVAPS SEVLTSLHLY KSLQSSVDTI
     RKAEESQRAE VKALRDYILR MEESRSQFQA QAQAEANAKV NDLRTLLEKK ESDLLRLREN
     RDTLSADLLD RKARESTRDG SLNQSKILAN ARGERIAMLV SENHRLKARL AAREGEETFF
     AFIMSNPQDE SFVRAQEERV DMLQRANNSL NATLKALGQG NPDVENFIQV ATEAKEQAEA
     LRTRLEKFEA LYGPDAIASS SVDLQQLSEQ LRCKEEELRK LRLELKASLE EPTALYTEIE
     RLSALWENLD KQLKSKIFDL GAMEDKLTKA QTEKSKADNK YFAAMRELDA LKAVVQHKDR
     ENKKQSLVQS KLVDSEKALK EQLAHLERET HLQAKSISER DTVIARAQIQ IDKERASLEL
     SNRRVQELNT QVLERDDLIA KHRLEVNKLN EKCESLRRQA DAKVAQARAA NATGYEAELV
     KERDSLMSIL KCSTCKLQYR KYVLTKCMHT FCKDCIDARL TTRQRKCPAC NGPFANSDVQ
     ELWFQ
//
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