ID A0A3N0YTA9_ANAGA Unreviewed; 974 AA.
AC A0A3N0YTA9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, 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};
GN ORFNames=DPX16_15763 {ECO:0000313|EMBL:ROL49437.1};
OS Anabarilius grahami (Kanglang fish) (Barilius grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Xenocypridinae incertae sedis; Anabarilius.
OX NCBI_TaxID=495550 {ECO:0000313|EMBL:ROL49437.1, ECO:0000313|Proteomes:UP000281406};
RN [1] {ECO:0000313|EMBL:ROL49437.1, ECO:0000313|Proteomes:UP000281406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-KIZ {ECO:0000313|EMBL:ROL49437.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:ROL49437.1};
RA Jiang W.;
RT "Genome assembly for a Yunnan-Guizhou Plateau 3E fish, Anabarilius grahami
RT (Regan), and its evolutionary and genetic applications.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROL49437.1}.
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DR EMBL; RJVU01026577; ROL49437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0YTA9; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000281406; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 2.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000281406};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 61..101
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 361..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..767
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 109214 MW; D654669E378150E4 CRC64;
MHCSERLRTQ ERASPGLTAR TVVYNKPFKS IRSIPRKLQH TQPVPSSRME STPKKDAEST
CVLCCQDIDM FAVGKCDHPV CYRCSTKMRV LCEQKYCAVC REQLDKVPPP LLQQRAQASA
AGRTVVFIKK PEPFAALKIH QYQCEKKYDI YFGDGKIYAQ FRKILLHECP HCPEPKVFSK
FEELEQHMRK QHELFCCKLC AKHLKIFSYE RKWYNRKDLA RHRTQGDPDD TSHRGHPLCK
FCDDRYLDND ELLKHLRRDH YFCHFCDADG AQEYYSDYQY LSEHFRESHY LCEEGRCSTE
QFTHAFRTEI DYKAHKAAAH SKSRAEARQN RQIDIQFNYA PRQQRRNDGL VIGGDDFEEA
DRFNRQGRPG RGRGPGGQQN VRSWRYNREE EDREMAAALR ASMVSRQEER NHVQDRSSQK
PRKEEKMEPD EMRNNRGTAK PTIEMQARTM KSNASLAGQD FPVLGAAAPP APIQSTIKQT
SVSLKEDDFP SLSGSLVSTP MTPAYTNQPK KLSSFQEEDF PALVSKIKPL KPQSNTTSAW
SQAGSKPVVV PNKPVVLPTK TVHVVSSSIL SASDPPPSGS MPQPLTAASS RRKKKLTSAE
THKAPPKVKC PSSSDDEDPQ SGKTAQEIRT VPTMLDISTL LTVKGGSSQP NPKASKKKKP
VTASSLGSPS HTPESVSKMA HKENVPEMKP PDTSIAKAPV APKTNSFING LMEKPAEALS
CTSFPENIPS PVTDQAPPSN EEEFPALISK KPPPGFKGAF PLKSTPSTLP PPPPPGLGPV
VSKPPPGFTG IPLNSNVVES SVSAVNRPTP AIGSYLVPEN FQQRNMDLIQ SIKNFLQNDE
TKFNEFKTFS GQFRQGIIPA VQYYKSCQEL LGENFNRVFN ELLVLLPDTR KQQELLTAHG
DFKALEKQQQ GLKPKKNKKK AWQTGTTSNS LELDCQVCPT CKQVLALKDF NTHNTLHTGD
DDFPSLQAIS KIIS
//
