ID A0A7L3RPJ2_CEPGR Unreviewed; 890 AA.
AC A0A7L3RPJ2;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
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:NXV15519.1};
GN ORFNames=CEPGRY_R02107 {ECO:0000313|EMBL:NXV15519.1};
OS Cepphus grylle (Black guillemot) (Alca grylle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Alcidae;
OC Cepphus.
OX NCBI_TaxID=28697 {ECO:0000313|EMBL:NXV15519.1, ECO:0000313|Proteomes:UP000578766};
RN [1] {ECO:0000313|EMBL:NXV15519.1, ECO:0000313|Proteomes:UP000578766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0020 {ECO:0000313|EMBL:NXV15519.1};
RC TISSUE=Liver {ECO:0000313|EMBL:NXV15519.1};
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:NXV15519.1}.
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DR EMBL; VZUD01000045; NXV15519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L3RPJ2; -.
DR Proteomes; UP000578766; 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:NXV15519.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000578766};
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..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..681
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 542..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXV15519.1"
FT NON_TER 890
FT /evidence="ECO:0000313|EMBL:NXV15519.1"
SQ SEQUENCE 890 AA; 99719 MW; E8AF5D0184A62EAF CRC64;
MAASASGAAA GPADGSCVLC CGELEVVALG RCDHPICYRC SVRMRALCGV RYCAVCREEL
GQVVFGRKLT SFSTIALNQL QHEKKYDIYF MDGEVYALYR KLLQHECFLC PDAKPFNTFA
DLEQHMRKQH ELFCCKLCVK HLKIFTYERK WYSRKDLARH RIHGDPDDTS HRGHPLCKFC
DERYLDNDEL LKHLRRDHYF CHFCDSDGAQ EYYSDYEYLR EHFREKHFLC EEGRCSTEQF
THAFRTEIDY KAHKTAFHSK NRAEARQNRQ IDLQFNYAPR HQRRNEGVIG GEDYEEVDRY
NRQGRSGRLG GRGSQQNRRG SWRYKREEED RDVAAAVRAS VAAKRQEEKK RVEDKDDSSS
RGKKEDLRDS EVLSSKRVPR SSNDVTVEKH FFALFVTTPK EAAANGALSQ DDFPAIGSAV
GPLQGSAQLA AVKLKEEDFP SLSSSAAPTI SSGMSLTYTA TAKKTAFQEE DFPALVSKMR
PNNKTVTNIT SAWNNGSSKN VVKAISNPCV NQIAKKPSSL NSTKGSKKSN KLSQSDDEDS
GSGLTTQEIR NTPTMFDVSS LLAASTSQTF TKVSKKKKVG IEKQRPSSPH LLQETSLPGS
STEKLPEAER TSNASSALTP HAPDRSTAVM NGHSEKSLAI CSTPKEPPGL KKPTVTNKCP
LPQEDFPALG SSGSARMPPP PGFNTAVLLK SPPPPPGLSV PVSKPPPGFA VIPSTNISEP
VTTPLKEPKS SHGSYLIPEN FQQRNIQLIQ SIKEFLQSDE SKFNKFKTHS GQFRQGLISA
AQYYKSCREL LGDNFKKIFN ELLVLLPDTV KQQELLSAHN DFRIKEKQSS NKSKKNKKNV
WQTDCNSDLD CYICPTCKQV LTQQDVVTHK ALHIEDEEFP SLQAISRIIS
//
