ID E2ACV6_CAMFO Unreviewed; 964 AA.
AC E2ACV6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=EAG_14680 {ECO:0000313|EMBL:EFN68754.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN68754.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL438582; EFN68754.1; -; Genomic_DNA.
DR RefSeq; XP_011255741.1; XM_011257439.2.
DR AlphaFoldDB; E2ACV6; -.
DR STRING; 104421.E2ACV6; -.
DR EnsemblMetazoa; XM_011257439.3; XP_011255741.1; LOC105250982.
DR GeneID; 105250982; -.
DR KEGG; cfo:105250982; -.
DR InParanoid; E2ACV6; -.
DR OMA; THIEIMT; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000311; 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 GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR CDD; cd16705; RING-HC_dBre1-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 Reference proteome {ECO:0000313|Proteomes:UP000000311};
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 910..949
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 492..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 231..265
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 289..337
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 608..887
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 492..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 112244 MW; 6EF4BFB937AB64C3 CRC64;
MSKRSADSGD ISSQPAIKKV QFEPILIGPI STLEEMDMKV LQFQNKKLAQ RLEQRHRMEA
ELRQRIEQLE KRQMQDDAVL NVVNRYWNQL NEDIRVLLQR FDAETADESE NKNESEATTS
FLMQLSSWDK EELDEKLANR VQVSKRAVSK VVQAFDRLSQ RNEKITLALK GEFDGEEAPN
IDEVVRRANA EIQMENRNLQ VLNLQLHEKH HTSSLKMSRL QDTIMGKDTL VAELRNQVDD
LQYELNKVRA RNDKLEHHLG EAIEKLKAFQ QIHGTDEKGS NKPNTLVASS VSQTKLEDLQ
RELEETRELA NNRLQELDKL HQQHRDTLKE VEKLKMDIRQ LPESVIVETT EYKCLQSQFS
VLYNESMQLK TQLDDARQQL QSSKNAHLRH IEMMESEELM AQKKLRGECI QLEDVLAQLR
KEYEMLRIEF EQNLAANEQT GPINREMRHL ITSLQNHNQQ LKGEVHRYKR KYKEASTEIP
RLKREVEELT AKLGQQTSQE NKEGNNSDGS GKEEDASNSL PGSTQIKEES SVTIKRESGA
DEEVETIEVG ENEGNKGTPD SLTLTSPTLK KEKDIKREKD IKKESVKTEH RDPAHRTKDG
KMVESEIVRD LKAQLKKAVN EMKEMKLLLD MYKGVGKEQR DKVQLMAAER KTRAELEDLR
QQVKKIQESK REERKKLADE DAQIKIKKLE EQAYNLQRQV AGQKQNCVWL QEEEALLNEM
EVTGQAFEDM QEQNSRLIQQ LREKDDANFK LMTERIKSNQ LHKLAREEKD VLKEQVSTLT
TQVEAANVVV RKLEEKERLL QNSLATVEKE LAVRQQAMEM HKRKAIESAQ SAADLKLHLE
KYHSQMKEAQ QVVAEKTSSL EAEAYKTKRL QEEIAQLRRK VERMKKIELA ETLDEVMAEE
LREYKETLTC PSCKVKRKDA VLTKCFHVFC WDCLRTRYET RQRKCPKCNC AFGANDYHRL
YLST
//
