ID C5M237_CANTT Unreviewed; 740 AA.
AC C5M237;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Histone demethylase JHD2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CTRG_00126 {ECO:0000313|EMBL:EER35387.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER35387.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER35387.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; GG692395; EER35387.1; -; Genomic_DNA.
DR RefSeq; XP_002545345.1; XM_002545299.1.
DR AlphaFoldDB; C5M237; -.
DR STRING; 294747.C5M237; -.
DR EnsemblFungi; CTRG_00126-t43_1; CTRG_00126-t43_1-p1; CTRG_00126.
DR GeneID; 8296216; -.
DR KEGG; ctp:CTRG_00126; -.
DR VEuPathDB; FungiDB:CTRG_00126; -.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000991_4_0_1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF33; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 13..56
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 79..170
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 179..229
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 325..491
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 672..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 637..664
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 740 AA; 85575 MW; 859AD4133C9B52FE CRC64;
MTMPFNKNLL TPCPVLTPNE EEFRDPVGYL SNEENLKLGA TYGIVKIVPP PHWKPSFHIN
PDFKFHVRKQ VISDLGITTR SRDFFRENIN RFLKMRRKRQ LKLYFEVDGT KVYYYDLYRD
VEEMSGAMNE EKWHTLGSKF GVDYKRIKQE YESNIKYYAN YLHHNAKYEF PDSDSEDEFD
NCLICGQHDD PSETLLCDNC DNPFHMKCLN PPLTAVPATN WYCDKCLIGT GEYGFDEDVD
VKYTIPQFIK MCQEFDSKFI KDYNNGQPLT VDAIEQKFWS FVDIEKSDLE VMYGADIHNL
KPGEISGFPM ENTPNLDTTN PVVQYYINHP CNLNKLPLAK GSLLNFINTS ISGMTIPWIY
VGSLLSTFCW HVEDHYTLSA NYCHFGATKK WYGIPSSFAD KFEKLMKDAA PDLFKRQPDL
LHQLVSLMSP MQLVANGIPC VYADQNPNEF VVTYPRVYHA GFNCGFNFNE AVNFATDQWL
EFGEKSIDDY RPIKKENVFN HNELMENILV KFNKDRGVSI DLVRRSLAGF EKFVNHQNGL
LSKLKGKFDV EFVKQELSDD ESLCDHCKTH LSYQYCIILP ESKRKKPMAI SHLLTPQASP
QDVILKQEVE QEKVDELANS QASHNLSQLN KEPVAESDKF QSLIENAKKE ISEENNDAPT
TRRRSKRILT LKQKEEPPKK KARMGKMTKK RDQTAVPSEP KLCLQCVCSL DEKLQHGKLV
YIKQMPALEE LISETKNNLK
//