ID I4Y887_WALMC Unreviewed; 788 AA.
AC I4Y887;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=WALSEDRAFT_69954 {ECO:0000313|EMBL:EIM20179.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM20179.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM20179.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
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 EMBL; JH668241; EIM20179.1; -; Genomic_DNA.
DR RefSeq; XP_006959667.1; XM_006959605.1.
DR AlphaFoldDB; I4Y887; -.
DR STRING; 671144.I4Y887; -.
DR GeneID; 18475666; -.
DR KEGG; wse:WALSEDRAFT_69954; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_0_0_1; -.
DR InParanoid; I4Y887; -.
DR OMA; YRQMQEY; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005242; 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: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; PF08647; BRE1; 1.
DR Pfam; PF00097; zf-C3HC4; 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 Reference proteome {ECO:0000313|Proteomes:UP000005242};
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 735..774
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 198..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 342..383
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 445..472
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 557..626
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 198..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 90860 MW; C218E7FA14B0E34F CRC64;
MDQKKRKLDD DGNSDLDNDN ALLEQFRKEA IWRQMREYKR QYEHSLNRLQ DLESKSNSLQ
SSLSSVEVCW NELIDVLQLV IVPSSSIQSN DALKDFLEYS NSEDLALLNS ALSVRSGATK
ELIGSVLTTA TRNQSPDAVH LQKQAHMYQQ QSNSYKQELR LTRLQLDDCK SQWESTRDKL
LNAEKQVDRV KSSLISKIHQ ETKPISSDSP IPQPKTDSVD QIKSEPSQAP SPVRETPQPP
PPPGPTKEEL EDARKLAMQR MTESVELRAE KIKLSQEVDS LRVTLRRPND EAILESGLYR
DLQQQIGHFQ SDADTAKIKY NKLQKEFEGI FTSRREFEDR LKADANSQLD AALQKLQVKE
ADINRLRGQR EELNSELNVR RTKDSTKLQH IEQTQQLSES RLERIRCLNS EIQRLKGRIA
AGYGNENVYR AIMGDSVTEE DLNITIRLDT QLKTANEEIE ALKSQISNLQ SGGDLHVRLE
QVETKLQSYE KAFSDPADPE VQNLVNQINK KDERIKTLEL QNVESETTSN AIYGEIERLS
KAWEVLDEQN RSKIFDLQHL EEKVSRLMTE KAKSDNKYFA AMRAKDAVDI ERKTALRTHE
KQSKTIERLV DTEKQLQQQI SIHEKELMVY SSKTKALEDK VFTTERELSS ARLLADESKR
RLMEVSTKLN ERHVMYEDER AAKKRLEEDN TKLRSDLQRI PHNQPVSSGA MNGIHNAKEE
NLQRERDQLF FLLRCSTCKN ELKSHCITRC MHTLCKSCID ARIETRQRKC PICQIGFSSS
DVQKLQWA
//
