ID B6Q397_TALMQ Unreviewed; 1483 AA.
AC B6Q397;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=PMAA_028800 {ECO:0000313|EMBL:EEA28061.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28061.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995899; EEA28061.1; -; Genomic_DNA.
DR RefSeq; XP_002144576.1; XM_002144540.1.
DR STRING; 441960.B6Q397; -.
DR VEuPathDB; FungiDB:PMAA_028800; -.
DR HOGENOM; CLU_002979_0_1_1; -.
DR OrthoDB; 2784357at2759; -.
DR PhylomeDB; B6Q397; -.
DR Proteomes; UP000001294; 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:UP000001294};
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 335..395
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 591..749
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1483 AA; 164735 MW; 8A6C35D1DB1C05ED CRC64;
MASTSSFLSH PGGRPRQYRT PSPPRRAIEP ISPTFKSERH SFWNDRDAFY PRGYNGNSYN
SQSDQSRRSI GASHTRPSFG SQVEHPKAGH GHHRASSSIE TLANIALATS PRFQSLSFDP
PGNPTHRESP PLFPPTDAEF ERPAKRARSE KASPVFQHVD TRPSTSHVTT VPDSMKTDAE
LLLNFARPTN FASPHQYSQS SNGFDQPFNQ FANDQRIPAG YGTSMAIPGF IASALPGSNQ
SPSRLRSHSD GSTAIAPPVI PELRPNTSSS TLPGSSWEGD TFRKYNNAQE QSSHLPDENN
IMPKPMKRRP TITGETMEAV PEAKEEEVTP DESVPANCAA CHLVRMDVNN EDQGEDTWIK
CDGCESWYHI VCAGFKNDRE VRTVDKFICR KCRPVHGQTT FVRKSSRART TIDYAGLNQG
LVKTSTDSYE HHYIQPIKDG RIQFLPESFP RMRAELVTAE FFERGVGMTE PIIIPAALNP
RTSIDTSELD STFDGLAGEA STQEMFDEVL ENQPGEPEMV LDCGQDVLDM VIPQGLTVRA
VAELYGPEER VEVIDVKSQQ GEDKRWNMQK WADYYESTGK KIVRNVISLE VSQSPLGKLI
RRPKIVRDLD LQDSVWPEEL KAIGDFPKVQ FYCLMSVADC YTDFHIDFGG SSVYYTILKG
KKTFFFIPPK EKHLKKYEEW CNSPAQDTTF LGDQTKECYR VDLQEGDTML IPAGWIHAVW
TPENSLVIGG NFLTRMNYGM QIKVAKIEKD TKVPRKFRYP FFQKIQWYTA LKYLNDDPIP
DSVFDAFSRD EHYRFYRQFP IYYEFGEREN RSALGSPYHN ARFYSQAELE GLPELLRYLL
RTALIAGGYS VDGVTAEARN AIKRSIPKMQ GDPVEIAKKF AIWIAWKRGN ENAASWTRPG
AISSTFKIDQ VEKRPAGRPS RRSERHADAQ KMYAERQSLQ LVTEPLLEPQ DAFPSSTPNP
PSDIVPIPQP QPQPVLIPVT PAATAAAAPA LSTPIISTPS VSTPATTNST VKEELPKPRT
TNKGSGLGPK RVACDACRKR RIRCRHKDEQ GDGLSLGVSP TAAPPGVMFD SVDPQRQSIL
ARDAASVLNA LASVATESTL QDGGELLPYN SDGFSRDNVS FLSSISQSAF PRPVEGSVNG
INSGKKGRSK ACDECRKSKR RCIHDEYGRI DPVKAQERSK PRATSSAKRP RPNEDGLDPA
THKKAKADAT ASVPLDNFNY TGFETDQTMP PYLPASDTLV LAEEQYQREY YKQDPDGLST
VQSPPEDRFD QSMDIEPADV SYAVLPNPKI NGDTAIPTSH TQANHQLANS LASPPTSLSG
ETEILPPKHP SEELKGGSVI VDGEHEVLHT PNSSSRHSSR QPRHVDRYIP EQQVGTKPST
ITKQAAMATS TRQPTKALST TSSHGKKSTS RPSSSHTKKS ASPSLEKKLA HSSTTSPSSS
KNVKRERTSF TADDTTDADA ESLRLIRELQ EQDFGLRRRA ARV
//
