ID C1G982_PARBD Unreviewed; 1572 AA.
AC C1G982;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=JmjC domain-containing histone demethylation protein 1 {ECO:0000256|ARBA:ARBA00015153};
DE EC=1.14.11.27 {ECO:0000256|ARBA:ARBA00013246};
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1 {ECO:0000256|ARBA:ARBA00031083};
GN ORFNames=PADG_03818 {ECO:0000313|EMBL:EEH47734.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47734.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH47734.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH47734.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36'
CC of histone H3, thereby playing a central role in histone code.
CC {ECO:0000256|ARBA:ARBA00003909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000256|ARBA:ARBA00001574};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00008037}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN275960; EEH47734.2; -; Genomic_DNA.
DR RefSeq; XP_010759194.1; XM_010760892.1.
DR STRING; 502780.C1G982; -.
DR GeneID; 22583059; -.
DR KEGG; pbn:PADG_03818; -.
DR VEuPathDB; FungiDB:PADG_03818; -.
DR eggNOG; KOG1633; Eukaryota.
DR HOGENOM; CLU_002979_0_1_1; -.
DR InParanoid; C1G982; -.
DR OMA; KFGIWVA; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 2.
DR CDD; cd15517; PHD_TCF19_like; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR PANTHER; PTHR23123:SF21; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 1; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_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:UP000001628};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 378..438
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 635..793
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1572 AA; 173526 MW; 844FF18562E47C9E CRC64;
MANCSSFRNH CMMRPSDYHT PSPPRDAVEL ISPARTPAHS PTSPSSIIRN VPSRDGQQPS
YEPFFGVQES SIKHEWNNPF QDGNRTGSQH PHNPQPQPHQ QEYHHYRGSS TSHPTANPAN
KIGQRSGSNI DALATIALAT SPTFAPLTYD EPASAGLATT TTTKHHQPST TDQSERPSKR
ARSEKASSPS WLTRPVTSHI SAFDSMKTDA ELLLNFARPS NFPRYQDGPK PQLQLQSANQ
PARPNRRTAA VQWATDPADL WVKKWDITAE NKPSSAFFGS NPGGAPSRIR SKSDGSAFMG
RPVMNGFVSG SSPLPPLMGH ALEDDQVDPR ETVEKPHGTM QANHLDVQQK PPTPFQRRNS
VPASDLKAED SDNDSSSQAT CASCNLDRIG SDGEDEDSVT WISCDGCNKW FHIVCAGFKS
DRDTRTVDKF ICRTCRPLHG PTTFVRKSSR ARTAIDYAGL NQGFIMSSTE TPEHHYIQPI
KDGKITFLPD NFARIRPELV TAEYFEKGIG MTEPIVIPAS FNTRASVPGS SDYIPPEVAT
EEELDEIIDN MPEDDDDGNY TEVIDCGQDL LDMVIPQGLT VRHVAELYGP EERVEVIDVK
SQQGEDKRWN MQKWADYYYD DSASKIVRNV ISLEVSNSPL GRLIRRPKIV RDLDLQDHVW
PAELQAIGDF PKVQFYVLMS VADCYTDFHI DFGGSSVYYH ILKGSKTFFF IPPKDKYLKK
YEEWCNSAAQ DTTFLGNQTK ECYRVDLSAG DTMLIPSGWI HAVWTPEDSL VIGGNFLTRM
NYGMQIKVAK IEKDTKVPKK FRYPFFQKIL WYAAIKYLED DPIPQSVLES FSRDENYLFY
REYPIYYEFG ERGNTAKPGT EYYNARYYSQ AELDGLPELA KYLLRTALIA GGYQVDGVTT
ETRNAVRRSI PKGQGDPVDT IMKFGMWVAW KRGNEPAAKW TRPGAISFDT KVDMSDRKPA
GRPSRRSQRN IAAESPQLNA NEAKNMTDSQ TSGRRLSDLS SENTNNGVIS STSSSSTTAP
SMSGTPGPPK RKASLSNVKD DISQLASSYS TNNSNNNINK PRLMQKPTGL GPKRVACDAC
RKRRIRCRHK DEQMLVESFV PVTASMSSKQ PINGRVITTV AAAAAGTFSA VNVDGIKERH
AAAVGDAGAT VGEDAYAAAA SSTSGSLLMT SQPNAGKVKG FSSNSSGAGK KRRSKACDEC
RKSKRRCIHD ENGRIDPVKA QERSKPRATA STKRPPFSED NLSPSLTKRQ KPEFYISGEE
PPQAQLDFES VRTEFPMNRM NGENEKPVAV IPMQQEIGPS QTSYASPPTL KADLVPAAEL
TSIPTTAAPA SSLVSPPTSL ADDLEVDPNQ TDGEEKAPNV KSEQEQQKQN GERSVIAYTS
TTASRNPTHQ RCAVSDAEAG SCKTATTRTL PTVTVTTEPS DLSVTLPSSS ATSISTALKM
PSFTTSSPST SRWPSSHNRT TTTPPSSSSF KHEREQKQHT PVVDKKRGVA VDEGSNNPPP
SPRSHPNQKQ DQGQSQNRSQ RTSPASPQRH RSKLTSRDRG SFSDADADPD TLRLIREMQE
QDFGLRKRPA RT
//
