ID H9FX08_MACMU Unreviewed; 668 AA.
AC H9FX08;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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|EMBL:AFE79167.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE79167.1};
RN [1] {ECO:0000313|EMBL:AFE79167.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE79167.1}, and Testis
RC {ECO:0000313|EMBL:AFI37685.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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 EMBL; JU335414; AFE79167.1; -; mRNA.
DR EMBL; JV047614; AFI37685.1; -; mRNA.
DR AlphaFoldDB; H9FX08; -.
DR UniPathway; UPA00143; -.
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:0051301; P:cell division; 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 2: Evidence at transcript level;
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 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 40..91
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 308..347
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 73987 MW; 8A05D17927D4B8A3 CRC64;
MERPEEGKQP PPLPPQPWGR LLRLGAEEGE PHVLLRKREW TIGRRRGCDL SFPGNKLVSG
DHCKIVVDEK SGQVTLEDTS TNGTVINKLK VVKKQTCPLQ SGDAIYLVYR KNEPEHNVAY
LYESLNEKQG MTQESFEANK ENVFHGTKDA SGAGVGAGPG ADPRLPPLSP TAQVCFEEPQ
PSTSTSDLFP TALASSTEPP PAGREHSSSC ESGDGGISPK GCGPSVASDK ISSFASALPD
RKPASFSSLE PQDQEDLEPV KKKMKGDGDL DLNLQLLVAQ PRRNAQTVQE DVRAATGKPD
KMEETLTCII CQDLLHDCVS LQPCMHTFCA ACYSGWMERS SLCPTCRCPV ERICKNHILN
NLVEAYLTQH PDKSRSEEDV QSMDARNKIT QDMLQPKVRR SFSDEEGSSE DLLELSDVDS
ESSDISQPYV VCRQCPEYRR QVAQPPHCPA PEVEPGAPQA LGDVPSTSVS LTTAVQDYVC
PLQGSHALCT CCFQPMPDRR AEREQDPRVA PQQCAVCLQP FCHLYWGCTR TGCFGCLAPF
CELNLGDKCL DGVLNNNSYE SDILKNYLAT RGLTWKNMLT ESLVALQRGV FLLSDYRVTG
NTVLCYCCGL RSFRELTYQY RRNIPASELP VAVTSRPDCY WGRNCRTQVK AHHAMKFNHI
CEQTRFKN
//
