ID A0A7K4ZA01_BUCAB Unreviewed; 890 AA.
AC A0A7K4ZA01;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-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:NWR68192.1};
GN ORFNames=BUCABY_R13590 {ECO:0000313|EMBL:NWR68192.1};
OS Bucorvus abyssinicus (Northern ground-hornbill) (Abyssinian
OS ground-hornbill).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Coraciimorphae;
OC Bucerotiformes; Bucorvidae; Bucorvus.
OX NCBI_TaxID=153643 {ECO:0000313|EMBL:NWR68192.1, ECO:0000313|Proteomes:UP000551127};
RN [1] {ECO:0000313|EMBL:NWR68192.1, ECO:0000313|Proteomes:UP000551127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-012-80 {ECO:0000313|EMBL:NWR68192.1};
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:NWR68192.1}.
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DR EMBL; VYZL01013415; NWR68192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K4ZA01; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000551127; 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:NWR68192.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000551127};
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 17..57
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 282..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..343
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWR68192.1"
FT NON_TER 890
FT /evidence="ECO:0000313|EMBL:NWR68192.1"
SQ SEQUENCE 890 AA; 99536 MW; C06C4EB126B5605E CRC64;
MAASASGAVA GSADGSCVLC CGELEVVALG RCDHPICYRC SVRMRALCGV RYCAVCREEL
GQVVFGRKLT SFAAIALNQL QHEKKYDIYF TDGDVYVLYR KLLQHECSLC PELKPFNTFA
DLEQHMRKQH ELFCCKLCVK HLKIFTYERK WYSRKDLARH RIHGDPDDTS HRGHPLCKFC
DERYLDNDEL LKHLRRDHYF CHFCDSDGAQ EYYSDYEYLR EHFREKHFLC EEGRCSSEQF
THAFRTEIDY KAHKTACHSK SRAEARQNRQ IDLQFNYAPR HQRRNEGVIG GEDYEEVDRY
NRQGRSGRLG GRGSQQNRRG SWRYKREEED RDIAAAVRAS VAAKRQEEKK RVEDREENSG
RGRKEDLRDC EALSSKRVPK PSNDAAASPL KRVFALFVGA PKEAAANGAL SQDDFPAIGL
AAAPLQGSAQ PTAVKLKEED FPSLSSSAAP IIPAGMSMMY MATAKKTAFQ EEDFPALVSK
MRPNSKTVTN ITSAWNNGSS KSVVKAISNP CVNQIAKKPA SLNSTKGSKK SNKLSQSDEE
DSNSGLTTQE IRNTPTMFDV SSLLAASTSQ TFTKVSKKKK MGVEKQQLSS PHLLQETSFP
RASAEKLPEA EQTSTVSSAS HAPDRAAVVM NGHVEKPLAT CSTPKEPPGL KKPPATHKCP
LPQEDFPALG SSGPARMPPP PGFNTVVLLK SPPPPPGLSV PVSKPPPGFA VIPSTKIADP
VTTSLKEPKS RHGSYLIPEN FQQRNIQLIQ SIKEFLQSDE SKFNKFKTHS GQFRQGLISA
VQYYKSCREL LGENFKKIFS ELLVLLPDTV KQQELLSAHN DFRLKEKQSS NKPKKNKKTV
WQTDPSSDLD CCVCPTCKQV LTPQDVVTHK ALHIEDEEFP SLQAISRLIS
//
