ID A0A3Q0SFP1_AMPCI Unreviewed; 964 AA.
AC A0A3Q0SFP1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000020523.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000020523.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 AlphaFoldDB; A0A3Q0SFP1; -.
DR STRING; 61819.ENSACIP00000020523; -.
DR Ensembl; ENSACIT00000021059.1; ENSACIP00000020523.1; ENSACIG00000015907.1.
DR GeneTree; ENSGT00390000002866; -.
DR OMA; CEQITRD; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261340; Unplaced.
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-UniPathway.
DR CDD; cd16814; RING-HC_RNF20; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
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 911..950
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..88
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 191..354
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 655..887
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 129..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 112042 MW; 32B16C8694DBB656 CRC64;
MCFRSLRMSG QKRPADPSGP SSSGAPPEKR RERSTAVETV IKLGGVSNSE EQDIKALQAK
NRKLGEALDQ RQVIEDELRE RIERLETRQA TDDASLLILN RYWNQFDENI RLIIRRYDQA
SSEPEKSPTG EGRSLKPETP EPDGDSNQER AKDRGHQGET TNSFLATLAS SSSEEMEAEL
QERVESSQKQ ATRVLEIYEC LKNTVDQLKA ELDSGAGEIK MFEASKLNSL LTNENERLQQ
LTEDLKQKHT HMTSESRLLA RAANKADQRV SEVQALIEEL QWDMEKIRRR ENRLNAHLSE
ILERVRMMPA VYFEEMNSEL EENRELAENR LIELQKLEQD LQNVQQENSS MKTELQSRAE
SLVKETSEYR CLQSQFSVLY NESLILKAQL DETRARLNTT RTARLRQLEH MENDEVALQR
KVRTEVFQLE DTLAQVRKEY EMLRIEFEQT LAANEQAGPI NREMRHLIST LQTHNQQMKG
EVVKYKLRLR EAQAELHQVR ASKGNATLQS QSSTEMDVKE ETTSPSTPAV SGEPLVKTEP
DNGSSTPSST EKEEKKEKEE KKEKDIIKKE EKEREREKEK EKERERPTRT SKQRLLTEVS
ERSFVLDDGD SFVKDSYCDF CRKAQESQRE MKLLLDMYRS APKEQRDKVQ LMAAEKKSKS
EGEELRQRLR ELEERERREG KKMADEEALR KIRSVEEQID ILNKKLSIAK QEEDALLSEM
DVTGQAFEDM QEQNIRLMQQ LREKDDANFK LMSERIKSNQ IHKLLKEEKE ELADQLLTLK
TQVDAQLQVV RKLEEKERLL QGTISTAERE LALRTQALDM NKRKAQDSAL LSEEMRTQLE
QVQQRLNLVR EEVVENSISR EKESFNARRA QEDISKLRRK IEKAKKPAEK ISNGDEILNE
EINDYKARLT CPCCNSRVKD AVLTKCFHVF CFECVKTRYD TRQRKCPKCN AAFGANDFHR
IYIG
//