ID A0A087QNK2_APTFO Unreviewed; 984 AA.
AC A0A087QNK2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=AS27_10769 {ECO:0000313|EMBL:KFM02806.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM02806.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM02806.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM02806.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KL225763; KFM02806.1; -; Genomic_DNA.
DR RefSeq; XP_009289228.1; XM_009290953.1.
DR RefSeq; XP_019330581.1; XM_019475036.1.
DR RefSeq; XP_019330582.1; XM_019475037.1.
DR AlphaFoldDB; A0A087QNK2; -.
DR STRING; 9233.A0A087QNK2; -.
DR GeneID; 103908560; -.
DR KEGG; afor:103908560; -.
DR CTD; 56254; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053286; 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; cd16814; RING-HC_RNF20; 1.
DR Gene3D; 1.20.1170.10; -; 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:SF2; E3 UBIQUITIN-PROTEIN LIGASE BRE1A; 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:UP000053286};
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 931..970
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..85
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 236..298
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 322..373
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 846..901
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 510..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 114926 MW; 08B629917F53B767 CRC64;
MSGIGNKRTA GEPGPSAPPE KKAGVEDSGT TVETIKLGGV SSTEEMDIRT LQTKNRKLAE
MLDQRQAIED ELREHIEKLE RRQATDDASL LIINRYWNQF DENIRIILKR FDLDQGLGDL
LSERKALVVP EPEPDSDSNQ ERKDERERGE GLEPAFSFLA TLASSTSEEI ESQLQERVES
SRRAVAQIVT MYDKLQEKVD VLSHKLNSGD ISLMEEAVLE LNTYLSHENG RLQELADVLQ
EKHRIMSQEF SKLQERVETA ESRVSVLETM IDDLQWDIDK IRKREQRLNR HLADVLERVN
SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAG NRLSELEELR QDLEEVTTQN
EKLKVELRRA VEEAVKETPE YRCMQSQFSV LYNESLQLKA HLDEARTLLH GTRTTHQRQV
ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI
SSLQNHNHQL KGEVLRYKRK LREAQSDLSK IRSRSGSALL QSQSSTEDTK EEPPEVKQEP
DDPSAQVSVP KAASEDVNEM KARRDEEERE RERRERERER EKEKEKERER EKEKEKEKER
EREKQKQKES EKERESKEKE KGKHEDGRKK EAEVIKQLKA ELKKAQESQK EMKLLLDMYR
SAPKEQRDKV QLMAAEKKAK AELEELRQRV KELEDKEKKE SKKMADEDAL RKIRAVEEQI
EYLQKKLAMA KQEEEALLSE MDVTGQAFED MQEQNIRLMQ QLREKDDANF KLMSERIKSN
QIHKLLKEEK EELADQVLTL KTQVDAQLQV VRKLEEKEHL LQSSIGTGEK ELGLRTQALE
MNKRKAMDAA QLADDLKAQL ELAQKKLHDF QDEIVENRVT REKEMFNFKR AEEDISRLRR
KLETTKKPDM VPNCDEILME EIKDYKARLT CPCCNMRKKD AVLTKCFHVF CFECVKTRYD
TRQRKCPKCN AAFGANDFHR IYIG
//
