ID A0A5N5KKV7_PANHP Unreviewed; 908 AA.
AC A0A5N5KKV7;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=PHYPO_G00135950 {ECO:0000313|EMBL:KAB5531009.1};
OS Pangasianodon hypophthalmus (Striped catfish) (Helicophagus hypophthalmus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Pangasiidae; Pangasianodon.
OX NCBI_TaxID=310915 {ECO:0000313|EMBL:KAB5531009.1, ECO:0000313|Proteomes:UP000327468};
RN [1] {ECO:0000313|EMBL:KAB5531009.1, ECO:0000313|Proteomes:UP000327468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indonesia {ECO:0000313|EMBL:KAB5531009.1,
RC ECO:0000313|Proteomes:UP000327468};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB5531009.1};
RA Wen M., Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Avarre J.-C., Campet M., Ha T.T.T., Dugue R., Lampietro C., Louis A.,
RA Herpin A., Echchiki A., Berthelot C., Parey E., Roest-Crollius H.,
RA Braasch I., Postlethwait J., Bobe J., Montfort J., Bouchez O., Begum T.,
RA Schartl M., Guiguen Y.;
RT "A chromosome-scale genome assembly of the striped catfish, Pangasianodon
RT hypophthalmus.";
RL Submitted (JUN-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:KAB5531009.1}.
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DR EMBL; VFJC01000024; KAB5531009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5KKV7; -.
DR Proteomes; UP000327468; Chromosome 23.
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; 1.
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:UP000327468};
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 13..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 270..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 102270 MW; FC7E6975BEAB9D2A CRC64;
MESGMKKEAE NVCVLCCQDI DIFAVGKCDH PVCYRCSTKM RVLCEQKYCA VCRVELDKVI
FVRKLQPFAA LTQHEYQAEK KYDIYFGEGR IFAQFRKILL SECPQCPEPK VFSRFDELEQ
HMRKQHELFC CKLCAKHLKI FSYERKWYNR KELARHRMQG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DADGAQEYYS DYRYLSEHFR ESHFLCEEGR CSTEQFTHAF
RTEIDYKAHK ASAHSKNRAE ARQNRQIDLQ FNYAPRQQRR NDGLVGADDY EEADRFNRQG
RSGRGRPQGL HQNVRSWRYN REEEDRDLAA AIQASQAARR QAERGQVHER VGQKPRKEET
ADGEELRGNR GAVKPPSDMQ GRSTKNNVPL KGEDFPVLGA GAPPPPIHSM VKPTPVSLKE
DDFPSLGHSG TMGSAPMTPA YMAQARKPSS FQEEDFPALV SKIRPHKPHE TTTSAWSQVG
SKSGVLNNKP VVLPTKTHSH NAPVFSANDP PPSSTIPQAN TSRRKKKLTS SQTAKATSKV
KSPVSSDDEN PQPGKMIQEI CAVPTMLDIS SLLTVKTGSS QPNNKNSKKK RQPSATPSGT
STNIVELVTT AAHKENVPET KPPDGSVPKG TVVPKSNMFI NGYKEKPKEI KDTVLPEEPP
APKKQPISEP SAVPEEEDFP ALISKKPPPG FKNTFSSKNI QTVMPPPPPG LGPVISKPPP
GFTGVPLNSN VAECTVPVFN RPASSLGTYH MPENFKQRNM DLIQSIQNFL QNDESKFNEF
KNYSGQFRQG LISAAQYHKS CHELLGENFS RVFNELLVLL PDTHKQQELL TAHADFKAME
KQQPGSKGKK SKKKAWQTCT SNNNLDLDCQ VCPTCMQVLA PKDFSAHKTL HIGDDDFPSL
QAISKIIS
//
