ID A0A7K9JP11_9PASE Unreviewed; 879 AA.
AC A0A7K9JP11;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN Name=Znf598 {ECO:0000313|EMBL:NXH40007.1};
GN ORFNames=DICEXI_R09128 {ECO:0000313|EMBL:NXH40007.1};
OS Dicaeum eximium.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Dicaeidae; Dicaeum.
OX NCBI_TaxID=667154 {ECO:0000313|EMBL:NXH40007.1, ECO:0000313|Proteomes:UP000523279};
RN [1] {ECO:0000313|EMBL:NXH40007.1, ECO:0000313|Proteomes:UP000523279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-34 {ECO:0000313|EMBL:NXH40007.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXH40007.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-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:NXH40007.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VWZP01002203; NXH40007.1; -; Genomic_DNA.
DR Proteomes; UP000523279; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:NXH40007.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000523279};
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 3..43
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 289..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..308
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXH40007.1"
FT NON_TER 879
FT /evidence="ECO:0000313|EMBL:NXH40007.1"
SQ SEQUENCE 879 AA; 98576 MW; 9A24A16BF4C93132 CRC64;
GPCVLCCGEL DVVALGRCEH PICYRCSVRM RALCGVRYCA VCRXGRGVVF GRKLPSFSSI
ALQQLQHEKK YDIYFMDAEV YALYRKLLQH ECSLCPDAKP FNTFADLEQH MRKQHELFCC
KLCVKHLKIF TYERKWYSRK DLARHRIHGD PDDTSHRGHP LCKFCDERYL DNDELLKHLR
RDHYFCHFCD SEGAQEYYRQ AHYDYEYLRE HFREKHFLCE EGRCSSEQFT HAFRTEIDYK
AHKSACHSKS RAEARQNRHI DLQFTYTPRH PRRNDGVIGA EDYEEVDRFN RQGRAGRLSS
RGSQQNRRGS WRYKREEEDR DVAAAVRASM AAKRQEEKKR VEDKEEGSSS RGRKEDLRDP
DVLGSKRVPK SSNDVTGECW TGPAAAGHLS VWKVPSETAA NGALSQDDFP AIGSAAGPLQ
GSAQPALVKL KEEDFPSLSS SAAPTISSGM SLMYTATARK AAFQEEDFPA LVSKVKPTNR
TVTHITSAWN NSSSKNVVKA MSNPCVNQPA KKPSLNTSKG NKKSNKLCDS DNEDSGGGLT
TQEIRNTPTM FDVSSLLAAS TSQTFTKVGK KKKMGVEKQS PLSPRPPQET PRPATEKPPE
AEQPCKVFPA AHGPDRAAAV VNGHSEKASA GCAAPKEPPG LKKPPVTNKC PLPQEDFPAL
GSSGSARMPP PPGFNSVVLL KNPPPGLSVP VSKPPPGFAV IPSSTIPEPV TTALKEPKSC
HGSYLIPENF QQRNIQLIQS IKEFLQSDES KFNKFKTHSG QFRQGLISAA QYYKSCRELL
GENFKKIFKE LLVLLPDTAK QQELLSAHND FRIKEKQSSN KPKKNKKNVW QSEPPADLDC
YICPTCRQVL TQQDVVTHKA LHIEDEEFPS LQAISRIIS
//
