JHD1_ASPFU
ID JHD1_ASPFU Reviewed; 1418 AA.
AC Q4WHB7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=JmjC domain-containing histone demethylation protein 1;
DE EC=1.14.11.27 {ECO:0000250|UniProtKB:P40034};
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1;
GN Name=jhd1; ORFNames=AFUA_2G05970;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36'
CC of histone H3, thereby playing a central role in histone code.
CC {ECO:0000250|UniProtKB:P40034}.
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:0000250|UniProtKB:P40034};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The JmjC domain mediates the demethylation activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000305}.
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; AAHF01000008; EAL87688.1; -; Genomic_DNA.
DR RefSeq; XP_749726.1; XM_744633.1.
DR AlphaFoldDB; Q4WHB7; -.
DR SMR; Q4WHB7; -.
DR STRING; 746128.CADAFUBP00002247; -.
DR PRIDE; Q4WHB7; -.
DR EnsemblFungi; EAL87688; EAL87688; AFUA_2G05970.
DR GeneID; 3506876; -.
DR KEGG; afm:AFUA_2G05970; -.
DR VEuPathDB; FungiDB:Afu2g05970; -.
DR eggNOG; KOG1633; Eukaryota.
DR HOGENOM; CLU_002979_0_1_1; -.
DR InParanoid; Q4WHB7; -.
DR OMA; FGIWVAW; -.
DR OrthoDB; 181449at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
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:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
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 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; SSF57903; SSF57903; 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 Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1418
FT /note="JmjC domain-containing histone demethylation protein
FT 1"
FT /id="PRO_0000226792"
FT DOMAIN 588..746
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 331..391
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 639
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 642
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 644
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 659
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 714
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 1418 AA; 157353 MW; 5575A6C161A1C82C CRC64;
MIGATSFLNH SGPRPPRYRT PSPPRRAVEP ISPFTTTTDF RASWIDRGDS QAASYDRDRV
TSNNDVYSST NRGSHGRTSH GRSSSTIDTL ATIALATSPT FAPLSYRPPS QDPTPAMPLF
PSQSIESTER PAKRPRSEKS PSPLHQPQTT VAPDANPSST FDSMKTDAEL LLNFARPSNF
QPAAFYPSKR VSIDESYHPH YGEEPKSHFR AGLGSTYILP DGEKSAYHTS ANTAFPASRM
RSQSDGSAFI SRPVIQGVRP NTSSSTLPPI VWQEEEGNAK TGPGPPSTKF PGAETRYENS
VFTGIDTGAD RASLDVPPRG DDDTESDENN QANCAACNLV RIPVDSEEQG DVTWISCDGC
KQWFHIVCAG FKNDREIRTV DKFICRRCRP IHGQTTFVRK SSRARTAIDY AGLNQGLVKA
ASDSLEHHYI EPIREGKIRF LPDNFPRMRP ELVTAEYFER GSGMTEPIVI PAHLNTRDSI
PIVDPEFDSL VQEATSQEMF DELLEHLPEE GKDFETVIDC GQDQLDMVVP QGLTVRAVAE
LYGPEERVEV IDVKSQQGED KRWNMQKWAD YYESTGSKVV RNVISLEVSQ SKLGKLIRRP
KIVRDLDLQD AVWPEELKAI GDYPKVQFYC LMSVADCYTD FHIDFGGSSV YYHILKGKKT
FFFIPPKDKH LKKYEDWCNS PAQDSTFLGD QTKECYRVDL SEGDTMLIPS GWIHAVWTPT
NSLVIGGNFL TRLNYGMQIK VAKIEKDTKV PRKFRYPFFQ RIQWYTALKY LEDDPIPQSV
LNAFAEDENY RFHRAYPIYY EFGERENKAP AGDPYHNSRF YSQAELEGLP DLAKYLLRTA
LIASGYMVEG VTMDARNAVK RSIPKGQGDP IDTVRKFGIW VAWKRGNEKA PQWTRPGVVE
SNAKLSLTEK KPAGRPSRRS ERNAEGQRMY AERQAVQRPL EQPPDLTNGL SSEESSSAPS
TVEIPQSTVI STLPGTETKE LKEEIAQKPR SIHRSSGLGP KRVACDACRK RRIRCRHKDE
HNDTISAKQT TFGTFPAGVQ SSLAHDAASA LNSLAAIASE AGFQDAANGH GLERLEGSGN
YSTAILSTPN AATSKVHDGS PEGLNTGKKG RSKACDDCRK SKRRCIHDEY GRIDPIKAQE
RSKPRATASA KRPRPPQEED AAFTLNKRPK QESTSPVARP ASLFRAEGDM SHTQRPVDLE
ASSYFGTAHD HNGIAQTKLT SAVGQTSYAS PPAFQSDTVV MEVAGQGVSK PTASLVSPPT
SQADETDVPP EQDAEKDNHV VYYTPTTSSR HSSRQPRHVD RYVPESQPAK AVKTTHTPSK
RRASCSGPTT ARRVTPGAQG SSKKPASRPS SSHAKKGVSP VTEKKFDRMT TTSTSPGHKG
AKRERTAIAD DEPDAESLRL IRELQEQEFG LRKRTTRV
