ID A0A8C4UN55_FALTI Unreviewed; 874 AA.
AC A0A8C4UN55;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, 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};
OS Falco tinnunculus (Common kestrel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Falconiformes; Falconidae; Falco.
OX NCBI_TaxID=100819 {ECO:0000313|Ensembl:ENSFTIP00000015577.1, ECO:0000313|Proteomes:UP000694562};
RN [1] {ECO:0000313|Ensembl:ENSFTIP00000015577.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSFTIP00000015577.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A8C4UN55; -.
DR Ensembl; ENSFTIT00000016237.1; ENSFTIP00000015577.1; ENSFTIG00000010318.1.
DR Proteomes; UP000694562; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694562};
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 261..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..319
FT /note="Low complexity"
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"
SQ SEQUENCE 874 AA; 97906 MW; 2276E6709109DD4B CRC64;
MAASASGAAA GPADGSCVLC CGELEVVALG RCDHPICYRC SVRMRALCGV RYCAVCREEL
GQVVFGRKLT SFSTIALNQL QHEKKYDIYF TDGDVYALYR KLLQHECSLC PDLKPFNTFA
DLEQHMRKQH ELFCCKLCVK HLKIFTYERK WYSRKDLARH RIHGDPDDTS HRGHPLCKFC
DERYLDNDEL LKHLRRDHYF CHFCDSDGAQ EYYSDYEYLR EHFREKHFLC EEGRCSTEQF
THAFHTEIDY KAHKTACHSK NRAEARQNRQ IDLQFNYAPR HQRRSEGVIG GEDYEEVDRY
NRQGRSGRVS GRGSQQNRRG SWRYKREEED RDVAAAVRAS VAAKRQEEKK RVEDKEESSS
RGKKDDLRDS EVLSSKRVPK SSNDTAEAAA NGALSQDDFP AIGSAAGPLQ GSAQLAVVKL
KEEDFPSLSS SAAPTISSGM SLTYTATAKK TAFQEEDFPA LVSKMRPNNK TVTNITSAWN
NGSSKNVVKA ISNPCVNQIA KKPPSLNSTK GNKKSNKLSH SDDEDSGSGL TTQEIRNAPT
MFDVSSLLAA STSQTFTKVS KKKKMGVEKQ RPSSPRLLQE TSFPRSSTEK LPEAEQTSNA
SSALHAPDRS AAVMNGHSEK SLAICSTPKE PPGLKKPTVT NKCPLPQEDF PALGSSGSAR
MPPPPGFNTV VLLKSPPPPP GLSVPVSKPP PGFAVIPSTN ISEPVTTSLK EPKSRHGSYL
IPENFQQRNI QLIQSIKEFL QSDESKFNKF KTHSGQFRQG LISAAQYYKS CRELLGDNFK
KIFNELLVLL PDTVKQQELL SAHNDFRIKE KQSSNKPKKN KKNVWQTDSN SDLDCYICPT
CKQVLTQQDV VTHKALHIED EEFPSLQAIS RIIS
//
