ID A0A7K4U6V7_9SYLV Unreviewed; 906 AA.
AC A0A7K4U6V7;
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:NWR05959.1};
GN ORFNames=SINWEB_R05607 {ECO:0000313|EMBL:NWR05959.1};
OS Sinosuthora webbiana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Sylviidae; Sinosuthora.
OX NCBI_TaxID=337173 {ECO:0000313|EMBL:NWR05959.1, ECO:0000313|Proteomes:UP000580691};
RN [1] {ECO:0000313|EMBL:NWR05959.1, ECO:0000313|Proteomes:UP000580691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-08 {ECO:0000313|EMBL:NWR05959.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWR05959.1};
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:NWR05959.1}.
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DR EMBL; VXBN01009620; NWR05959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K4U6V7; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000580691; 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; 4.
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:NWR05959.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000580691};
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 316..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..335
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..359
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWR05959.1"
FT NON_TER 906
FT /evidence="ECO:0000313|EMBL:NWR05959.1"
SQ SEQUENCE 906 AA; 101191 MW; DA5F2DFFFABCEA94 CRC64;
AEAAMAAMAG AGPGPAEGPC VLCCGELDVV ALGRCEHPIC YRCSVRMRAL CGVRYCAVCR
EELRQVVFGR KLPSFSSIAL HQLQHEKKYD IYFMDSEVYG LYRKLLQHEC PLCPDAKPFN
TFADLEQHMR KQHELFCCKL CVKHLKIFTY ERKWYSRKDL ARHRIHGDPD DTSHRGHPLC
KFCDERYLDN DELLKHLRRD HYFCHFCDSE GAQEYYRQAD CSHGSFLCLH DYEYLREHFR
EKHFLCEEGR CSSEQFTHAF RTEIDYKAHK SACHSKSRAE ARQNRHIDLQ FTYAPRHPRR
TEGVVGAEDY EEVDRFNRQG RASRLSSRGS QQNRRGSWRY KREEEDRDVA AAVRASVAAK
RQEEKKRVED KEEGSSSRGR KEDLRDPDVL GSKRVPKSSS DVTGECWTGP AGYLSIWRVP
SETAANGVLS HEDFPAIGSA AGPLQGCAQP ALVKLKEEDF PSLSSSAAPT MSSGMSLTYT
ATARRAAFQE EDFPALVSKV KPANKTLTHI TSAWNNSSSK NVVKAMSGPC VNQPAKKPSL
NTSKGSKKSN KPCESDEEDG GGGLTTQEIR SAPTMFDVSS LLAASTSQTF TKVGKKKKMG
GEKQSPSSPR PPQETPLPRA APEKAPEAEQ PCRVFPAAHG PDRAVVNGHS EKPSAACATP
KEPPGLKKPP VTNKCPLPQE DFPALGSSGS ARMPPPPGFN SVVLLKNPPP PPGLSVPVSK
PPPGFAVIPS STISEPVTTA LKEPKSCHGS YLIPENFQQR NIQLIQSIKE FLQSDESKFN
KFKTHSGQFR QGLISAAQYY KSCRELLGEN FKKIFKELLV LLPDTAKQQE LLSAHNDFRL
KEKQSSNKPK KNKKNVWQTE SPADLDCYIC PTCRQVLTQQ DVVTHKALHL EDEEFPSLQA
ISRIIS
//
