ID A0A3Q1F7N7_9TELE Unreviewed; 644 AA.
AC A0A3Q1F7N7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Checkpoint with forkhead and RING finger domains protein {ECO:0000256|ARBA:ARBA00031332};
DE AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000256|ARBA:ARBA00029800};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000012289.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000012289.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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: Nucleus, PML body
CC {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the CHFR family.
CC {ECO:0000256|ARBA:ARBA00005797}.
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DR AlphaFoldDB; A0A3Q1F7N7; -.
DR Ensembl; ENSAPOT00000031951.1; ENSAPOP00000012289.1; ENSAPOG00000000419.1.
DR GeneTree; ENSGT00400000022306; -.
DR OrthoDB; 450556at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd22672; FHA_CHFR; 1.
DR CDD; cd16503; RING-HC_CHFR; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.40.140; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR040909; CHFR_Znf-CRD.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF17979; zf-CRD; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 29..80
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 266..305
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 120..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 71780 MW; 575D55D0D2F9CE49 CRC64;
MDSNRRGRPW GKLVKVDSSE TIMLFSRECT VGRKKGCYLS FPASKLVSGE HCKIVKDESS
GLVWLEDMST NGTVINMSKL VKKQTHMLQS GDVIYFVYRK SEPEQNIAYV YHSIKPEQAA
SPHSFDTERS AHSPSPVPAS EMSLSVEPVM LAKPPRDPTQ EEPQPSTSAS HFCIESPSSS
GPMATAASPA SGHTKDASTA AEKDTDNLEP ESKKRKTDDG KDYDLGLPHT SRIEAVGSTK
GSLGNLLSKP PVEGTKTDKM EESLTCVICQ DLLHDCVSLQ PCMHVFCAAC YSGWMERSSL
CPTCRCPVER IRKNHILNNL VEAYLIQHPE KCRSEEDLKS MDSRNKITQD MLQPKVERSF
SDEEGSSDYL FELSDNDSDS SDNSQPLVMC RQCPGYRRDV SQMLFSTTSN YWFPGLPSLP
PVPPPPKAAT DEGAVKPAGE QPSTSSDIPS APQEYRCSPQ GFHLICTCCL QPMPDRRAEL
NNQQVIAQQC VLCQRPFCHM YWGCQRIGCQ GCLVRFSELN LTDKCLDGVL NNNNYESEVL
QNYLSSKGKS WKDLLKESLQ GLQQGSYFLT DRRISANTIL CFCCGLGAFK ELAYKYRQNI
PASELPAGVT SRPDCYWGRN CRTQVKAHHA VKFNHICEQT RFKS
//
