ID A0A7K6HC49_9PASS Unreviewed; 897 AA.
AC A0A7K6HC49;
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:NWV73176.1};
GN ORFNames=DASBRO_R14618 {ECO:0000313|EMBL:NWV73176.1};
OS Dasyornis broadbenti (rufous bristle-bird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Meliphagoidea; Dasyornithidae; Dasyornis.
OX NCBI_TaxID=243059 {ECO:0000313|EMBL:NWV73176.1, ECO:0000313|Proteomes:UP000521322};
RN [1] {ECO:0000313|EMBL:NWV73176.1, ECO:0000313|Proteomes:UP000521322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-029-49 {ECO:0000313|EMBL:NWV73176.1};
RC TISSUE=Liver {ECO:0000313|EMBL:NWV73176.1};
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:NWV73176.1}.
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DR EMBL; VZRN01000275; NWV73176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K6HC49; -.
DR Proteomes; UP000521322; 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:NWV73176.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000521322};
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 309..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..353
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWV73176.1"
FT NON_TER 897
FT /evidence="ECO:0000313|EMBL:NWV73176.1"
SQ SEQUENCE 897 AA; 100331 MW; 32C7388F152691D5 CRC64;
AEAAMAAMAG AGPGSAEGPC VLCCGELDVV ALGRCEHPIC YRCSVRMRAL CGVRYCAVCR
EELRQVVFGR KLPSFSSIAL HQLQHEKKYE IYFMDAEVYA LYRKLLQHEC SLCPDAKPFN
TFADLEQHMR KQHELFCCKL CVKHLKIFTY ERKWYSRKDL ARHRIHGDPD DTSHRGHPLC
KFCDERYLDN DELLKHLRRD HYFCHFCDSE GAQEYYRQAD YLQDDYEYLR EHFREKHFLC
EEGRCSSEQF THAFRTEIDY KAHKSACHSK SRAEARQNRH IDLQFTYTPR HPRRTDGVVG
AEDYEEVDRF NRQGRASRLS SRGNQQNRRG SWRYKREEED RDVAAAVRAS VAAKRQEEKK
RVEDKEDGSS SRGKKEDLRD SDVLGSKRVP KSSNDVTGKH DFALSVSVPK EAAANGVLSQ
DDFPAIGSAA GPLQGSAQPA LVKLKEEDFP SLSSSAAPTI SSGMSLTYTA TAKKVAFQEE
DFPALVSKVK PTNKTVTHIT SAWNNCSSKN VVKAMSSPCV NQPAKKPSLN TSKGIKKSNK
LCELDDEDSS GGLTTQEIRN APTMFDVSSL LAASTSQTFT KVGKKKKMGV EKQNLSSPRP
SQETSFPRPA TEKPPEAEQP SKVFPAAHGP DRATAVVNGH SEKPSAACGT PKEPPGLKKP
PVTNKCPLPQ EDFPALGSSG SARMPPPPGF NSVVLLKSPA PPPGLSVPVS KPPPGFAVIP
SSTISEPVTA ALKEPKSCHG SYLIPENFQQ RNIQLIQSIK EFLQSDESKF NKFKTHSGQF
RQGLISAAQY YKSCRELLGE NFKKIFKELL VLLPDTAKQQ ELLSAHNDFR IKEKQSSNKP
KKNKKNVWQT DSPTDLDCYI CPTCRQVLTQ QDVVTHKALH IEDEEFPSLQ AISRIIS
//
