ID A0A850Z792_9PASS Unreviewed; 887 AA.
AC A0A850Z792;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
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:NWI02447.1};
GN ORFNames=TICMUR_R07281 {ECO:0000313|EMBL:NWI02447.1};
OS Tichodroma muraria.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sittidae; Tichodroma.
OX NCBI_TaxID=237442 {ECO:0000313|EMBL:NWI02447.1, ECO:0000313|Proteomes:UP000629438};
RN [1] {ECO:0000313|EMBL:NWI02447.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10K-DU-012-47 {ECO:0000313|EMBL:NWI02447.1};
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:NWI02447.1}.
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DR EMBL; WAAG01050770; NWI02447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A850Z792; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000629438; 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:NWI02447.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000629438};
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 12..52
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 301..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..342
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWI02447.1"
FT NON_TER 887
FT /evidence="ECO:0000313|EMBL:NWI02447.1"
SQ SEQUENCE 887 AA; 98690 MW; EFE4008D2A1AEF8B CRC64;
AGAGPGPAEG PCVLCCGELD VVALGRCEHP ICYRCSVRMR ALCGVRYCAV CREELRQVVF
GRKLPSFSSI ALHQLQHEKK YDIYFTDAEV YALYRKLLQH ECSLCPDAKP FNTFADLEQH
MRKQHELFCC KLCVKHLKIF TYERKWYSRK DLARHRIHGD PDDTSHRGHP LCKFCDERYL
DNDELLKHLR RDHYFCHFCD SEGAQDSAFS LPSDYEYLRE HFREKHFLCE EGRCSSEQFT
HAFRTEIDYK AHKSACHSKS RAEARQNRHI DLQFSYAPRH PRRADGVVGA EDYEEVDRFN
RQGRAGRLSS RGNQQNRRGS WRYKREEEDR DVAAAVRASV AAKRQEEKKR VEDKEEGSSS
RGRKEDLRDP DVLGSKRVPK SSNDVTGECW TGPAAPGHLS VWKVPPEKAA ANGALSQDDF
PAIGSAAGPL QGSAQPALVK LKEEDFPSLS SSAAPTISSG MSLTYTATAR KAAFQEEDFP
ALVSKVKPAN KTVTHITSAW SNGSSKNVVK AMSNPCVNQP AKKPSLNTSK GSKKSNKLCE
SDDEDGGGGL TTQEIRNTPT MFDVSSLLAA STSQTFTKVG KKKKMGVEKQ SPSSPRPSQE
TPLPRPATEK PPEAEQPCKV FPATAVVNGH SEKPAAGCAA PKEPPGLKKP PVTNKCPLPQ
EDFPALGSSG SARMPPPPGF NSVVLLKNPP PPPGLSVPVS KPPPGFAVIP SSTIPEPVTT
ALKEPKSCHG SYLIPENFQQ RNIQLIQSIK QFLQSDESKF NKFKTHSGQF RQGLISAAQY
YKSCRELLGE NFKKIFKELL VLLPDTAKQQ ELLSAHNDFR VKEKQSSNKP KKNKKNVWQT
DSPGELDCCI CPTCRQVLTQ QDVVTHKALH IEDEEFPSLQ AISRIIS
//
