UniProt: A0A158P3N7

Database: UniProt
Entry: A0A158P3N7_ATTCE

LinkDB:  A0A158P3N7_ATTCE 
Original site:  A0A158P3N7_ATTCE

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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ID   A0A158P3N7_ATTCE        Unreviewed;       964 AA.
AC   A0A158P3N7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   Name=105627726 {ECO:0000313|EnsemblMetazoa:XP_012064395.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012064395.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012064395.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) 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   EMBL; ADTU01008291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADTU01008292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADTU01008293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012064395.1; XM_012209005.1.
DR   AlphaFoldDB; A0A158P3N7; -.
DR   STRING; 12957.A0A158P3N7; -.
DR   EnsemblMetazoa; XM_012209005.1; XP_012064395.1; LOC105627726.
DR   GeneID; 105627726; -.
DR   KEGG; acep:105627726; -.
DR   eggNOG; KOG0978; Eukaryota.
DR   InParanoid; A0A158P3N7; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000005205; 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:UP000005205};
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          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..603
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   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  112267 MW;  51AA6F199CF2A84F CRC64;
     MSKRPPDNGD SSSQPPIKKV QFEPILIGPI STLEEMDMKV LQFQNKKLAQ RLEQRHRMEA
     ELRQRIEQLE KRQMQDDAVL NVVNRYWNQL NEDIRVLLQR FDAETADESE NKNESEATTS
     FLMQLSSWDK EELDDKLANR VQVSKRAVSK VVQAFDRLSQ RNEKITLALK GEFDGEEAPN
     IDEVVRRANA EIQMENRNLQ AINIQLHEKY HTISLKMSEL QDTITGKDTL AAELRNQVDD
     LQYELNKVRA RNDKLEHHLG EAVEKLKAFQ QIHGTDEKGS NKPNTLVASS VSQTKLDDLQ
     RELEETRELA NNRLQELDKL HQQHRETLKE VEKLKMDIRQ LPESVIVETT EYKCLQSQFS
     VLYNESMQLK TQLDDARQQL QSSKNAHLRH IEMMESEELM AQKKLRGECI QLEDVLAQLR
     KEYEMLRIEF EQNLAANEQT GPINREMRHL ITSLQNHNQQ LKGEVHRYKR KYKETSTEIP
     RLKKEVEELT TKLGQQTSQE NKEGNNSDGS GKEEDASNSL PGSTQIKEES GVTIKRESGA
     DEEVETIEVG EGEGNKNTPD SLTLTSPTLK KEKDIKREKD IKKESVKTEH RDPAHRTKDA
     KMAESELVRD LKAQLKKAVN EMKEMKLLLD MYKGVGKEQR DKVQLMAAER KTRAELEDLR
     QQVKKIQESK REERKKLADE DAQIKIKKLE EQAYTLQRQV ACQKQNCIWL QEEEALLNEM
     EVTGQAFEDM QEQNSRLIQQ LREKDDANFK LMTERIKSNQ LHKLAREEKD VLKEQVSTLT
     TQVEAANVVV RKLEEKERLL QNSLATVEKE LALRQQAMEM HKRKAIESAQ SAADLKLHLE
     KYHSQMKEAQ QVVAEKTSSL EAEAYKTKRL QEEIAQLRRK VERMKKIELA ETLDEVMAEE
     LREYKETLTC PSCKVKRKDA VLTKCFHVFC WDCLRTRYET RQRKCPKCNC AFGANDYHRL
     YLST
//

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