ID A0A0J7KUF2_LASNI Unreviewed; 879 AA.
AC A0A0J7KUF2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=RF55_5984 {ECO:0000313|EMBL:KMQ93884.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ93884.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ93884.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ93884.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMQ93884.1}.
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DR EMBL; LBMM01003157; KMQ93884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7KUF2; -.
DR STRING; 67767.A0A0J7KUF2; -.
DR PaxDb; 67767-A0A0J7KUF2; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000036403; 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:UP000036403};
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 825..864
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 413..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..258
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 529..802
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 413..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 102530 MW; 81B43AC21459DBA5 CRC64;
MSKRSADSGD TSSQPAIKKV QFEPILIGPI STLEEMDMKV LQFQNKKLAQ RLEQRHRMEA
ELRQRIEQLE KRQMQDDAVL NVVNRYWNQL NEDIRVLLQR FDAETADESE NKNENEATTS
FLMQLSSWDK EELDEKLANR VQVSKRAVSK VVQAFDRLSQ RNEKITLALK GEFDGEEAPN
IDEVVRRANA EIQMENRNLQ VINLQLHEKH HSTSLKLEDL QRELEETREL ANNRLQELDK
LHQQHRDTLK EVEKLKMDIR QLPESVIVET TEYKCLQSQF SVLYNESMQL KTQLDDARQQ
LQSSKNAHLR HIEMMESEEL MAQKKLRGEC IQLEDVLAQL RKEYEMLRIE FEQNLAANEQ
TGPINREMRH LITSLQNHNQ QLKGEVHRYK RKYKEASTEI PRLKREVEEL TAKLGQQTSQ
ENKEGNNSDG SGKEEDASNS LPGSTQIKEE SGVTIKRESG ADEEVETIEV GESEGNKGTP
DSLTLTSPTL KKEKDIKREK DIKKESVKTE HRDPAHRTKD GKMAESEIVR DLKAQLKKAV
NEMKEMKLLL DMYKGVGKEQ RDKVQLMAAE RKTRAELEDL RQQVKKIQES KREERKKLAD
EDAQIKIKKL EEQAYNLQRQ VAGQKQEEEA LLNEMEVTGQ AFEDMQEQNS RLIQQLREKD
DANFKLMTER IKSNQLHKLA REEKDVLKEQ VSTLTTQVEA ANVVVRKLEE KERLLQNSLA
TVEKELALRQ QAMEMHKRKA IESAQSAADL KLHLEKYHSQ MKEAQQVVAE KTSSLEAEAY
KTKRLQEEIA QLRRKVERMK KIELAETLDE VMAEELREYK ETLTCPSCKV KRKDAVLTKC
FHVFCWDCLR TRYETRQRKC PKCNCAFGAN DYHRLYLST
//
