ID A0A3R7PTJ4_PENVA Unreviewed; 949 AA.
AC A0A3R7PTJ4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=C7M84_004733 {ECO:0000313|EMBL:ROT76669.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT76669.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT76669.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT76669.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT76669.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT76669.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) 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:ROT76669.1}.
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DR EMBL; QCYY01001623; ROT76669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7PTJ4; -.
DR STRING; 6689.A0A3R7PTJ4; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000283509; 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; 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 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; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
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:UP000283509};
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 20..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 259..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..403
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..521
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 103755 MW; 6EBB558FF8D70402 CRC64;
MSSKGRVSRV ESATEEEEVC VVCFRPVETY SIGECDHPVC FECSTRMRVL CGRNECPICR
KNMAKVVFTR NVVSFMSINT RNMLYERRYA IYFESEAVMK AYDLLMEHSC PLCKDIPPFK
NFAMLKDHMR KNHELFYCEL CVDHLKIFTG ERRSYTRSQL AQHRRKGDTD DTSHRGHPLC
EFCDARFMDN DELFRHLRRD HFFCHIYHYL CEEGGCQEEQ FTSVFRTKLD LQAHMAQNHS
SNLSKQAARQ ARTLDIEFTL NHRQQDSSRH DERGMRGGRG GRDGRGRGGR RDRDRDREYE
EQQLPDDMDS RPPVTQHSID INCVQDFPSL NGTGPGSGGE AGGGGGNRSM ASHLAKQNRF
TVRASGRGRS VLDEEFPSLG STSVTVSTAQ ATAQSPTSPT TSVHLKVNTK KAVRDGQNAG
QRSSNVSIQY NRTVPAAANG PQGSGAEGEG GNGAGPRIGV ISHSSNITLR SKANNKAKSK
GLEEDFPALS VSTKTTNAGM GSSGWGSTAA APAPSMPASA PVNISKNMKK DFPALGPSAG
APSVAPPSKP GKKLNPKDFP SLAPNPESQT HMKNYHGRSS VTIPVSNAWT HTVDQVPKAS
DGNEPSSSKS KKKKKGSNKS AADVTSNSSA NSNQSSSNST SNSVSNGPAK PSTKKKPVGL
HNIFDDDSDE DAVTMDLSMG KLGDYQSMAP VTSSNLNMIT SDMVNERKKS ELKIGTLRAP
PPKLDNDDAF PTLGGSFSPS PLATSTWSSP AKSTAPPGFS SKPKVPPGFS ATDMTFTSSS
GEKFAISPTS EAAVSTSAFT AQPTTTYTFQ LPPRFELRNK RLIKTIHDEC KGDEDKFDCF
KMLAGQLRSG DLSGHMYYEQ CREVMGKAIF HKILPELLVL LPDIKKQQEV LAAYRKVDGG
RGCSTVFAVC VVCQQVLSQD DYSEHMDNHD QNASDFPSLG KPAPHRFQK
//
