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Database: UniProt
Entry: A0A3Q1CMZ3_AMPOC
LinkDB: A0A3Q1CMZ3_AMPOC
Original site: A0A3Q1CMZ3_AMPOC 
ID   A0A3Q1CMZ3_AMPOC        Unreviewed;       481 AA.
AC   A0A3Q1CMZ3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000027163.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000027163.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   AlphaFoldDB; A0A3Q1CMZ3; -.
DR   STRING; 80972.ENSAOCP00000027163; -.
DR   Ensembl; ENSAOCT00000030294.1; ENSAOCP00000027163.1; ENSAOCG00000015889.1.
DR   GeneTree; ENSGT00940000156206; -.
DR   OMA; FYCCETV; -.
DR   OrthoDB; 5406876at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007369; P:gastrulation; IEA:Ensembl.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13195; FERM_C_MYLIP_IDOL; 1.
DR   CDD; cd17104; FERM_F1_MYLIP; 1.
DR   CDD; cd16523; RING-HC_MYLIP; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR041790; MYLIP_FERM_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF13; E3 UBIQUITIN-PROTEIN LIGASE MYLIP; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   PRINTS; PR00935; BAND41.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1..279
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          388..423
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          339..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  54458 MW;  6C2C99B9F3D04AB9 CRC64;
     MLCHVTRPDS VVMEVEVDAK ANGEDCLNKV CRKLGVIEVD YFGLQFTGSK GENLWLNLRN
     RICQQMDNVA PCRLRLRVKF FVEPHLILQE QTRHIFFMHV KEDLHNGHLR MGSEQAEELS
     ALLAQAEFGD YNQNTAQYWY SELCGEEPST ATINSIISRH RALEGLSQGS VEYQALQLVS
     SLEHYGVEWH WARDANGQRL AIGVGPEGIA ICKEDFSLVN RISYPIIQIA TQSGKSVYLT
     VTKDTNDSVV LLFKLISNRA ANGLYRAITE THAFYRCDTV TNAVMMQYSR DFKGHLASLF
     LNENINLGKK YVFDIRRTSK EVYDHARRAL YNSGVVDLVS PSESGERSSP SRSPNRDEQQ
     DEGLDCGSCQ QSRALQERLQ KLREALLCML CCEEEIDAAF CPCGHMVCCQ TCANQLQLCP
     VCRSEVEHVQ HVYLPTCTSL LSLTLSDNHH QRSSIPAPIH RDMASPHTCS TTEYEHKLYH
     T
//
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