ID E1BBP0_BOVIN Unreviewed; 738 AA.
AC E1BBP0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 84.
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};
GN Name=CHFR {ECO:0000313|Ensembl:ENSBTAP00000018544.6,
GN ECO:0000313|VGNC:VGNC:27288};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000018544.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000018544.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000018544.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000018544.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000018544.6};
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; E1BBP0; -.
DR SMR; E1BBP0; -.
DR STRING; 9913.ENSBTAP00000018544; -.
DR PaxDb; 9913-ENSBTAP00000018544; -.
DR Ensembl; ENSBTAT00000018544.6; ENSBTAP00000018544.6; ENSBTAG00000013951.6.
DR VEuPathDB; HostDB:ENSBTAG00000013951; -.
DR VGNC; VGNC:27288; CHFR.
DR eggNOG; KOG0802; Eukaryota.
DR GeneTree; ENSGT00400000022306; -.
DR HOGENOM; CLU_032966_0_0_1; -.
DR InParanoid; E1BBP0; -.
DR OMA; SNYWFPG; -.
DR TreeFam; TF330957; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000013951; Expressed in spermatocyte and 107 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044779; P:meiotic spindle checkpoint signaling; IEA:Ensembl.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; 2.
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 Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
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 113..164
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 379..418
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 80726 MW; 155B8F458160C4B7 CRC64;
MSVDSSGGCA AGSGFGAGRG VSWRRARASG GTLGRLAARA AAVGRGRRGG AAGRSLCPCG
PGLTRRFRVS SDVNPMERPG EGEQPPQQQP WGRLLRLGAE EGEPHVLLRK REWTIGRRRG
CDLSFPGNKL VSGDHCKITV DEKSGQVSLE DTSANGTVIN KLKVVKKQTC PLQTGDVIYL
VYRKNEPEHN VAYLYESLNE KQGVTQDSFE ANKENVFHVT KDTSGAGRGD DPQDPQVLLS
SPATQVCFEE PQPSTSTSDL FPTASTSSME PTSAGRGPPS SSSSRGTDIS PKGCGPSVTS
DEISSFPLTL PDREGASFSL SEPQDQEDLE PVKKRVKAVG EPDLNLPILV TDPGRDPPAA
LDVRAEAMKP DKMEETLTCI ICQDLLHDCV SLQPCMHTFC AACYSGWMER SALCPTCRCP
VERICKNHIL NNLVEAYLLQ HPDKRRSEED LRSMAARNKI TQDMLQPKVR RAFSDEEGSS
EDLLELSDVD SESSDVSQPS IVCRQCPEYR RQAGQPLPYP GPGSEPGAPQ VPGDAPSTSA
SVMAAQDYVC ALQGSHAICT CCFQPMPDRR AERERDPRIA PQQCAICLQP FCHLYWGCAR
TGCLGCLAPF CELNLGDRCL DGVLSNNNYE SDVLKNYLAT RGLTWKNMLT ESLGALQRGV
FLLSDYRITG NTVLCYCCGL RSFRELTYQY RQNIPASELP AAVTSRPDCY WGRNCRTQVK
AHHAMKFNHI CEQTRFKN
//