ID A0A7K9SJ53_9PICI Unreviewed; 890 AA.
AC A0A7K9SJ53;
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:NXI35888.1};
GN ORFNames=GALDEA_R04917 {ECO:0000313|EMBL:NXI35888.1};
OS Galbula dea.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Coraciimorphae;
OC Piciformes; Galbulidae; Galbula.
OX NCBI_TaxID=1109041 {ECO:0000313|EMBL:NXI35888.1, ECO:0000313|Proteomes:UP000566440};
RN [1] {ECO:0000313|EMBL:NXI35888.1, ECO:0000313|Proteomes:UP000566440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-62 {ECO:0000313|EMBL:NXI35888.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXI35888.1};
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:NXI35888.1}.
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DR EMBL; VWZX01001334; NXI35888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K9SJ53; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000566440; 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:NXI35888.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000566440};
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 302..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..346
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..574
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXI35888.1"
FT NON_TER 890
FT /evidence="ECO:0000313|EMBL:NXI35888.1"
SQ SEQUENCE 890 AA; 99262 MW; 3099481BE2DD8099 CRC64;
AAMASGAVEA AAAGPADGSC VLCCGELEVV ALGRCDHPIC YRCSVRMRAL CGVRYCAVCR
EELGQVVFGR KLSSFSAVAL HQLQHEKKYD IYFTDGEVYA LYRKLLQHEC SLCPDLKPFN
TFADLEQHMR KQHELFCCKL CVKHLKIFTH ERKWYSRKDL ARHRIHGDPD DTSHRGHPLC
KFCDERYLDN DELLKHLRRD HYFCHFCDSD GAQEYYSDYE YLREHFREKH FLCEEGRCST
EQFTHAFRTE IDYKAHKTAC HSKSRAEARQ NRQIDLQFSY APRHQRRSEG VIGAEDYEEV
DRYNRQGRSG RLGGRGSQQN RRGSWRYKRE EEDRDVAAAV RASVAAKRQE EKKRVEDKEE
SSSRGRKEEL RDSEVLSSKR VPKASGDAPV DCGSKHFFAL FVNTPKEAAA NGALSQDDFP
AIGSAAGPLQ GSVQVKLKEE DFPSLSSSAA PPISSGLSLA YTATAKRAAF QEEDFPALVS
KMRPNKTVTN ITSAWNNGSS KNVVKAISNP AVSQVAKKPP SLGSTKGSRK SSKLPLSDEE
DSSSGLTSQE IRSTPTMVDV SSLLAASTSQ TSTKVSKKKK MGGEKQRPLS PHLLQETTLP
RQSAEKLLEA ERTANSSSAL HPPDRPPAVM NGHLEKSLGI CSTPKEPPGL KKPTVTNKCP
LPQEDFPALG SSGSARMPPP PGFNTVVLLK TPPPPPGLSV PVSKPPPGFA VIPSTKISEP
VTTSLKEPKP SHGSYLIPEN FQQRNIQLIQ SIKEFLQSDE SKFNKFKSHS GQFRQGLISA
AQYYRSCREL LGENFKKIFN ELLVLLPDTV KQQELLSAHN DFRIKEKQSS NKPKKNKKNV
WQTDSSTDLD CSICPTCKQV LTQQDVATHK ALHLEDEEFP SLQAISRIIS
//
