ID   A0A0N5BP88_STREA        Unreviewed;       855 AA.
AC   A0A0N5BP88;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000771500.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000771500.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU365038};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365038}.
CC   -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC       ECO:0000256|RuleBase:RU365038}.
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DR   AlphaFoldDB; A0A0N5BP88; -.
DR   STRING; 174720.A0A0N5BP88; -.
DR   WBParaSite; SPAL_0000771500.1; SPAL_0000771500.1; SPAL_0000771500.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000046392; Unplaced.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd16499; RING-HC_Bre1-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR   PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR   Pfam; PF00097; zf-C3HC4; 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   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU365038};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW   Transferase {ECO:0000256|RuleBase:RU365038};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          802..840
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          275..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          62..89
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          222..256
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          578..630
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          662..710
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   855 AA;  100590 MW;  8E83BC362C0A4573 CRC64;
     MLKRDAGVIS EVDAGLQPVK KAKINDKEVL EFELLKIANI GVGNTIDVDA CHVQLYTLSE
     MYRSRDKEAK KLQDELAAYK KKVQEYKKRY ETVVSVTKRC YDTLDNDLMR LGQRFVSGLT
     REIDSFTDEP DTVFEYEPWE NGQMEKHLER KCANTSSIID QLINVLVQRL NKCDKMDNFL
     SRVNVSDEEI KKKLGQATRE SQRLTEISGK LQEENRDIIK KTKALQHRTK SLEEQLKQKD
     EEIQKANDEE RKTRRLYEKL KFRFAWYIKY ENKRKDDNES KSKETTEHDS SSVKQTEELE
     VLKKKYAELE NMNECRMNEI KELVERNVQL AHEISELKQN KKEVTKDDLI NSVEYIALNE
     KLKRVVVEYE ELRQHCNELT TFNLDYIKGL VQFDDAYDAE VLRSKQLIKQ LLIESEEIRL
     KAGDCTSAFM KQVELDKPHG DFLQREIDRL QEYIGALQKK MSIMKHESKR SAMEKEALLK
     RILAADKKTK EMTNRCYRCR WIESLDGTNS DTEINIDFEK INDIEQVVEK SSDDELRNYF
     KQFMKLVKGI KTMYDRVETA KDESLKEMFN SDEYLKLSKM HSDQIEKLKE ELEKAQQSVS
     SYAEQFEETD SQLEEEVANS EKLRRELSER DSLYLEQMQS VFDSKQETAR ANRKLVIMEH
     CISQLREYIE LQKLENDQLK KDSKAAVDAL KAKTEEIRML NEEFKKYEDC QGQLLDQVKH
     QDIEIQKLRK SEFSLKDSID KYTVDKETYE HKIRRAEEMG SQYKLKYEIC KNERNTLRKS
     VTGGGNDFYI RQISELQSAL SCCCCKENRK DTIITKCLHM FCSKCVTQVI ETRKRKCPSC
     ATSFGVGDYK PISLE
//