ID A0A7K7GDB3_ERIRU Unreviewed; 906 AA.
AC A0A7K7GDB3;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 15.
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:NWY67560.1};
GN ORFNames=ERIRUB_R02771 {ECO:0000313|EMBL:NWY67560.1};
OS Erithacus rubecula (European robin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Turdidae; Erithacus.
OX NCBI_TaxID=37610 {ECO:0000313|EMBL:NWY67560.1, ECO:0000313|Proteomes:UP000529965};
RN [1] {ECO:0000313|EMBL:NWY67560.1, ECO:0000313|Proteomes:UP000529965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0015 {ECO:0000313|EMBL:NWY67560.1};
RC TISSUE=Blood {ECO:0000313|EMBL:NWY67560.1};
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:NWY67560.1}.
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DR EMBL; VZSK01000720; NWY67560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K7GDB3; -.
DR Proteomes; UP000529965; 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:NWY67560.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000529965};
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 308..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..352
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWY67560.1"
FT NON_TER 906
FT /evidence="ECO:0000313|EMBL:NWY67560.1"
SQ SEQUENCE 906 AA; 101003 MW; CA5610C658BF358D CRC64;
AEAAMAAMAG AGPGPAEGPC VLCCGELDVV ALGRCEHPIC YRCSVRMRAL CGVRYCAVCR
EELRQVVFGR KLPSFSSIAL QQLQHEKKYD IYFMDAEVYA LYRKLLQHEC FLCPDAKPFN
TFADLEQHMR KQHELFCCKL CVKHLKIFTY ERKWYSRKDL ARHRIHGDPD DTSHRGHPLC
KFCDERYLDN DELLKHLRRD HYFCHFCDSE GAQELISVLS LPSDYEYLRE HFREKHFLCE
EGRCSSEQFT HAFRTEIDYK AHKSACHSKS RAEARQNRHI DLQFTYAPRH PRRGDGVVGA
EDYEEVDRFN RQGRAGRLSS RGNQQNRRGS WRYKREEEDR DVAAAVRASV AAKRQEEKKR
VEDKEEGSRG RKEDLRDPDV LGSKRVPKCS NDVTGDPCSG MNGFGLKTMS FFLSVPVPKE
AAANGVLSQD DFPAIGSAAG PLQGPAQPTL VKLKEEDFPS LSSSAAPTIS SGMSLTYTAT
ARRAAFQEED FPALVSKVKP TNKTVTHITS AWNNSSNKNV VKAMSNPCVN QPAKKPSLNT
SKGSKKSNKL CESDDEDGAG GLTTQEIRSA PTMFDVSSLL AASTSQTFTK VGKKKKMGVE
KQSPSSPRPS QETPLPRPAT EKPPEAEQPC KVFPAAHGPD RATAVVNGHS EKPTAGCAAP
KEPPGLKKPP VTNKCPLPQE DFPALGSSGS ARMPPPPGFN SVVLLKNPPP PPGLSVPVSK
PPPGFAVIPS STISEPVTTA LKEPKSCHGS YLIPENFQQR NIQLIQSIKE FLQSDESKFN
KFKTHSGQFR QGLISAAQYY KSCRELLGEN FKKIFKELLV LLPDTAKQQE LLSAHNDFRI
REKQSSNKPK KNKKNVWQTD SPAELDCYIC PTCRQVLTQQ DVVTHKALHI EDEEFPSLQA
ISRIIS
//
