ID A0A3B4U3K4_SERDU Unreviewed; 1109 AA.
AC A0A3B4U3K4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000013174.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000013174.1}
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|ARBA:ARBA00000900};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B4U3K4; -.
DR STRING; 41447.ENSSDUP00000013174; -.
DR Ensembl; ENSSDUT00000013415.1; ENSSDUP00000013174.1; ENSSDUG00000009571.1.
DR GeneTree; ENSGT00940000165144; -.
DR OMA; AIKQWQV; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19829; Bbox2_TIF1b_C-VI; 1.
DR CDD; cd15541; PHD_TIF1_like; 1.
DR CDD; cd16585; RING-HC_TIF1_C-VI; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR047058; TIF1b_Bbox2_Znf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR PANTHER; PTHR45915:SF4; TRANSCRIPTION INTERMEDIARY FACTOR 1-ALPHA; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:PRU00024}.
FT DOMAIN 76..134
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 161..214
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 221..262
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 768..815
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 851..926
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 431..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 259..318
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 453..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1109 AA; 123603 MW; 0FE9E7E2AE43AAF9 CRC64;
MVCVLSYEST DVRLSYGHKS FKILYREAAV KKKMDETAEN VDNDDIVIIV ENEAESLPAE
EERLKQQGTF GLMDTCPICK LSFHNREPKL LPCLHSFCKR CLPAPFRSAD PRRDSQGQVD
NNKPLGAIRC PVCRQECWEM DVLDNFFVKD SAEVPSSTVE KTSQVCMSCD DNTEATGYCV
ECVEFLCVTC IEAHQRVKFT RDHTIRQKEE MSPEAVGVST QRPVFCDIHK QEPLKLFCET
CDRLTCRDCQ LLKHKDHNYQ FLEDAYRNHR QYLENMTQQL QEKRKAIEDV SGCISTGLQQ
VEENRKAVTN EIKKSICNLI MEINRKGKIL VNQLEALTKD HELGLKKQQE DVNSLSRHLD
HVISFTKWAT ASHSGTALLY CKRLILFQIH YLMRASCNPS IVPQSSVRFQ CRSGFWATNV
DLGSLVVERG PGRPPITNHQ AAPRAEAPAG GLSVSAQQRQ STLAQLQMQV DKLSQQPHRQ
PPPNHWSWYQ NVRLPGPPGP PPPTRPIHGG SSPSQGPPNL TQPGRRYGTS HPNPRSPTSS
MLHNTGFPPP QSLRDLIHSS SFPPKPMDVL QGTSRYPQPL PAGAATQTSL HQRGLPESSF
LKRSEASGSV PSITISIPKP SYAPSVASAT TDKTSTLNHI TVQGRQNSPM AKPSSTDRST
GTSSWRQTSE PPSAPSAKRR RRSSPGPIIV IKDEPEDEDE VHFVQSTVGS SLPDSSTGAQ
SKPRQQQKVS VQVPVPGSES KAGKEQRPQT AAQPESEKRA EPEEDPNEDW CAVCQNGGEL
LCCDKCPKVF HLSCHIPTLI ESPSGEWFCS FCRDLAAPEM EYNCDSKDDP ISEGFPPVDR
RRCERLLLRL FCNDFSTDFQ QPASPSETRR YKELIKTPMD LSIVKRKLES KSKEGECYSR
PEEFVADIRL IFFNCAKYYK ATSEVGSAGL YLEDYFEEQL KLVYPDKVFP GGREEQMIPP
LEDEIEEEEE MMEEGLAPIE HDKPQSPAGK GIPPVEEDLA PLEEAPAPAE EEKSEMEEKT
TDTSEKETEK TVSATGEGSP PAAEVKQDEK SPVKEVESSP AADSETKDGV APSSPKEENL
ELPTDKTVDP PEIQEKEAAP ADTAKEEEG
//
