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Database: UniProt
Entry: A0A3Q0SFP1_AMPCI
LinkDB: A0A3Q0SFP1_AMPCI
Original site: A0A3Q0SFP1_AMPCI 
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
//
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