ID A0A210R6I3_MIZYE Unreviewed; 973 AA.
AC A0A210R6I3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 28-JAN-2026, 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};
GN ORFNames=KP79_PYT05832 {ECO:0000313|EMBL:OWF56534.1};
OS Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC Mizuhopecten.
OX NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF56534.1, ECO:0000313|Proteomes:UP000242188};
RN [1] {ECO:0000313|EMBL:OWF56534.1, ECO:0000313|Proteomes:UP000242188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PY_sf001 {ECO:0000313|EMBL:OWF56534.1,
RC ECO:0000313|Proteomes:UP000242188};
RX PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA Chourrout D., Li R., Bao Z.;
RT "Scallop genome provides insights into evolution of bilaterian karyotype
RT and development.";
RL Nat. Ecol. Evol. 1:120-120(2017).
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:OWF56534.1}.
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DR EMBL; NEDP02000167; OWF56534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A210R6I3; -.
DR STRING; 6573.A0A210R6I3; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000242188; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR056437; Znf-C2H2_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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
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; 1.
DR Pfam; PF23230; zf-C2H2_13; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 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:UP000242188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 14..54
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 102..126
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 277..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 110425 MW; DB4F692959DFE6A6 CRC64;
MEKRQRRESA TESCPVCHEA VEIYAIGSCD HPVCYRCALR MRALCNQFYC PICRTDLSQV
YMVHNLVKES AIPRHGYIPN RKLKIFYEDD SIKKRVDKLL EHNCPKCKQS FRLFKELQTH
MRKDHTHFYC DLCIVHLQIF PFERKYYSRQ DLATHRRVGD KDDTSYKGHP LCHFCEERYM
DNDELYRHLR KEHYYCHFCE KDGCNEYYGD YEDLKRHFRD QHYLCQDEDC VNAQFTHAFR
SEIDLKAHKA NEHNRGLTKA QVRQSRVVDV DIQLAPRKKP QRGVVSRDAY EDTGPRNRGR
NGVSGRQASY RERFRDEDVE KAIKVSLETM KEDRTKQSKS PVEEMELESP KIVHDESNFP
LLGNMPSGRP HTPTPTEELI KDRSIAHKLA KANHMSVQHG RLGMADFPSL GQSSGGAPEP
PKPSGSRKGY HEPRVGASKS VSTVSNKNRP SSMQSVENED FPGLPTAKNI SSSNTSSKVG
SWGVQPPPKP HSSVQQNKDI TQNINVTLDS KVSKSKQYNV IPSKRVLVDD KEFPSLGNKP
PLNLEWGNSS SENKKQPTSK KVDWFDVDEQ EFSIHNFKSD KDGVHTDTAG KSKKKKKKQK
GVDSTSDEKN SSSFGEHASL DNIASSLISA KSKPDPTELQ KLKENKKPVS VKDSKDIKHV
SDEEFKEYPV VTNSGKIELK ERATVAVVQN HSTFNKFDLL GSEDFPQMAN SMPKSRASEK
PRKEKATLLL DEEEYPQLGG NKKSKAPPGF SKTPLPTSPP GFSTTPAPKK PPPGFGPSVK
SESKQHEILD LHAIQESLTL KTIVPMSVNM GNFLYAPLED SQSRNHKLIS DIRSHAHDDF
DKFKTWAGDF RNGKMLAASY YDKCERLLGK KDFTSIFPEL LALLPDIDKQ QELLSIYSSV
ESAKPCDKHR GGQGRKGGWE VSSFSTCPTC RQVLLQKDYN QHIAMHDTGS DFPSLHSDSS
SRPVGLKEWV KAQ
//
