ID A0A7L0UFY2_CHOAC Unreviewed; 877 AA.
AC A0A7L0UFY2;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
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:NXL65719.1};
GN ORFNames=CHOACU_R01004 {ECO:0000313|EMBL:NXL65719.1};
OS Chordeiles acutipennis (Lesser nighthawk) (Caprimulgus acutipennis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Strisores; Caprimulgiformes;
OC Caprimulgidae; Chordeilinae; Chordeiles.
OX NCBI_TaxID=118183 {ECO:0000313|EMBL:NXL65719.1, ECO:0000313|Proteomes:UP000568556};
RN [1] {ECO:0000313|EMBL:NXL65719.1, ECO:0000313|Proteomes:UP000568556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-008-62 {ECO:0000313|EMBL:NXL65719.1};
RC TISSUE=Mixed tissue sample {ECO:0000313|EMBL:NXL65719.1};
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:NXL65719.1}.
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DR EMBL; VXAQ01001350; NXL65719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0UFY2; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000568556; 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:NXL65719.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000568556};
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 280..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..346
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXL65719.1"
FT NON_TER 877
FT /evidence="ECO:0000313|EMBL:NXL65719.1"
SQ SEQUENCE 877 AA; 97914 MW; FA75D44FC6CC838A CRC64;
RGVGAAMAAS ASAGPADGPC VLCCGELEVV ALGRCDHPIC YRCSVRMRAL CGVRYCAVCR
EELGQVVFGR KLTSFSTIAL NKLQHEKKYD IYFTDGEVYA LYRKLLQHEC SLCPDAKPFN
TFADLEQHMR KQHELFCCKL CVKHLKIFTH ERKWYSRKDL ARHRIHGDPD DTSHRGHPLC
KFCDERYLDN DELLKHLRRD HYFCHFCDSD GAQEYYSDYE YLREHFREKH FLCEEGRCST
EQFTHAFRTE IDYKAHKTAC HSKSRAEARQ NRQIDLQFNY APRHQRRNEG VIGGEDYEEV
DRYNRQGRSG RLGGRGSQQN RRGSWRYKRE EEDRDVAAAV RASVAAKRQE EKKRVEDKED
NSSRGKKEDL RDSEVLGSKR VPKSSADAAE AAANGALSQD DFPAIGSAAG PLPGSAQQAA
VKLKEEDFPS LSSSAAPTIS SGMSLTYTAT AKKTAFQEED FPALVSKMRP NNKTVANITS
AWNNGSSKNV VKAMSNPCVS QAAKKPSSLH STKGSKKSNK LSQSDDEDSS SGLTTQEIRN
TPTMFDVSSL LAASTSQTFT KVSKKKRMGV EKQRPSSPHL SQETSFPKSS TEKPLETERT
SNASSALHAP DRSTAVTNGH LEKSLAVCTT PKEPPGLKKP TVTNKCPLPQ EDFPALGSSG
SARMPPPPGF NTVVLLKSPP PPPGLSVPVS KPPPGFAVIP SPTISEPVTT SLKEPKSCPG
SYLIPENFQQ RNMQLIQSIK EFLQSDESKF NKFKTHSGQF RQGLISAAQY YKSCRELLGE
NFKKIFNELL VLLPDTVKQQ ELLSAHNDFR IKEKQSSNKP KKNKKNVWQT DSNSDLDCCI
CPTCKQVLTQ QDVVTHKALH IEDEEFPSLQ AISRIIS
//
