ID A0A3P8NM37_ASTCA Unreviewed; 972 AA.
AC A0A3P8NM37;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000005809.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000005809.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000005809.1}
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};
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DR AlphaFoldDB; A0A3P8NM37; -.
DR Ensembl; ENSACLT00000005934.1; ENSACLP00000005809.1; ENSACLG00000003875.1.
DR GeneTree; ENSGT00940000165144; -.
DR Proteomes; UP000265100; Chromosome 17.
DR Bgee; ENSACLG00000003875; Expressed in anal fin and 8 other cell types or tissues.
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; cd05502; Bromo_tif1_like; 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 SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
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 43..89
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 116..169
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 176..217
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 639..686
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 741..796
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 382..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..306
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 406..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 108700 MW; E183315AE878F6AE CRC64;
MDESAETAEN DDIVIIVENE AESLPAEEER LKQQATFGLM DTCPVCKLSF HNREPKLLPC
LHSFCKRCLP APFMSAEPRL VGIRCPVCRQ ECWEMDVLDN FFVKDSAEVP SSTVEKTTQV
CMSCDDNTEA TGYCVECVEF LCVTCIEAHQ RVKFTRDHTI RQKEEMSPDA VSLSTQRPVF
CDIHKQEPLK LFCETCDRLT CRDCQLLKHK DHNYQFLEDA YRNHRQCLET MTQQLQEKRK
AIEEVSSCIN GGLQQVEENR KAVTNEIKKS ICNLIMEINR KGKILVNQLE ALTKDHELGL
KKQQEEVNSL GRHLDHVISF TKWATASHSG TALLYCKRLL LYQIHYLMRA HCSPSIVPQS
SVRFQCRSGF WATNVDLGSL VVERGPSRPP ITNHQTGPRA EAPTGALSLS AQQRQSTLAQ
LQMQVDKLSQ QHPRGPPPNS WSWHQNVRLP GPPPPTRPIH GGSSPSQGVP NMVQQGRRYG
SSHPNPRSPT SSLLNNMSFP AAQSLRDLIH TSSFPPKPTD GSQGVSRFPQ PLTSGAATQM
SLHQVCRTVI IKIFSLTQHE SRKTTSWKQT AETPSAPALK RRRRTSPGPV IVIKDEPEDD
DEVRFVQSSV GSSLPDSSTG PQSQPESEKR AEPEEDPNED WCAVCQNGGE LLCCDKCPKV
FHLACHIPTL NESPSGEWFC SFCRDLVSPE MEYNCDSKDA PISEKFPPVD RRKCERLLLR
LFCNDFSTDF QQPASPSTRR YKELIKTPMD LSIVKRKLES KAKDGESYVS PEGFVADVRL
IFFNCAKYYK PTSEVGSAGL YLEDYFEEQL KLIYPDRVFP GGREEQMIPP LEDEIDEEEE
MMEDGAADVK DKPQSPAEKG IPPVEEDTSP LEDRTTPAAK EKSDAETSEK MTGKAIAATE
GDAPPADEVK QENVAAVKQA ESSPATQSDT KDGVASSSTK EVKPRITTDT TTEPPEAPQE
TSASVDTAKE KR
//
