ID   JHD1_EMENI              Reviewed;        1407 AA.
AC   Q5AW75; C8VBD1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   02-SEP-2026, entry version 123.
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=AN7455;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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=N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 2-oxoglutarate
CC         + 2 O2 = L-lysyl(36)-[histone H3] + 2 formaldehyde + 2 succinate + 2
CC         CO2; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787,
CC         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}.
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DR   EMBL; AACD01000129; EAA62035.1; -; Genomic_DNA.
DR   EMBL; BN001304; CBF79416.1; -; Genomic_DNA.
DR   RefSeq; XP_680724.1; XM_675632.1.
DR   AlphaFoldDB; Q5AW75; -.
DR   SMR; Q5AW75; -.
DR   STRING; 227321.Q5AW75; -.
DR   EnsemblFungi; CBF79416; CBF79416; ANIA_07455.
DR   GeneID; 2869726; -.
DR   KEGG; ani:ANIA_07455; -.
DR   VEuPathDB; FungiDB:AN7455; -.
DR   eggNOG; KOG1633; Eukaryota.
DR   HOGENOM; CLU_002979_0_1_1; -.
DR   InParanoid; Q5AW75; -.
DR   OMA; KFGIWVA; -.
DR   OrthoDB; 5876800at2759; -.
DR   Proteomes; UP000000560; Chromosome IV.
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 H3K36me/H3K36me2 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:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00067; GAL4; 1.
DR   CDD; cd15517; PHD_TCF19_like; 1.
DR   Gene3D; 2.60.120.650; Cupin; 2.
DR   InterPro; IPR041070; JHD.
DR   InterPro; IPR050690; JHDM1_Histone_Demethylase.
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; 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   Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1407
FT                   /note="JmjC domain-containing histone demethylation protein
FT                   1"
FT                   /id="PRO_0000226797"
FT   DOMAIN          577..735
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   ZN_FING         323..382
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          98..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          893..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1122..1183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1252..1389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..914
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..938
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1254..1264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1273..1284
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1285..1296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1297..1349
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         628
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         631
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         633
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         648
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         703
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ   SEQUENCE   1407 AA;  156107 MW;  CE85B1C78A76A2D0 CRC64;
     MISATSFVTA IGSRPPRYRT PSPPRRAVEP ISPCSTADYR TYRASREISA SATSDHVRST
     PTDKRPSPAD VPASHRSGHG RSSSTIDTLA TIALATSPTF TPLTHRPPSD KSNTTLSMFP
     PETEPVERPA KRPRSERDES SYTQHRSNAF SIARPPAISD SMKTDAELLL NFARPTNLYP
     PIPSSKRANT DDSYHNHTFH TQAQIKERNA STYWVTNHEN VIFNHSAMHN IPPSRMRSQS
     DGSAAISRPV IEGLRPNTSS STLPPLAFQE EADSGDRHWD MERKPVLEES QVDFCKPDET
     VPILSQSQPL KKELDADSNG SSQASCATCN LVRIPVDNED QDVTWISCDG CKRWFHIVCA
     GFKNDRETRT VDKFICKTCR PIHGQTTFVR KSSRVRTSID YAGLNQGLVK SATDSLEHHY
     IEPIKQNKIR FLPENFPRMR PELVTAEYFE KGNGMTEPIV IPAEFNTHAT IPPTNPEFDA
     LVQDAPSQEM FDELLDHLPN VDHETVIDCG QNQLDMVIPQ GLTVRTVSEL YGPEERVEVI
     DVKSQHGEDK RWTMQKWADY YESTGDKVVR NVISLEVSQS KLGRLIRRPK IVRDLDLQDA
     VWPEELKAVG NFPKVQFYCL MSVADCYTDF HIDFGGSSVY YHILKGKKTF FFIPPKDKHL
     KKYEEWCNSP AQDYTFLGDQ TKECYRVDLS EGDTMLIPSG WIHAVWTPEN SLVIGGNFLT
     RLNYGMQIKI AKIEKETKVP MKFRYPFFQK IQWYAVLKYL EEDPVPQSVL AAFSQDENYR
     FHRKYPIYYE FGERANTEPK GSPYHNSRFY SQAELEGLPD LAKYLLRTAL IAGSYLVEGV
     TADTRNAVKR SIPAMPGEPI DVIRTFGVWI AWKRGNEKAA HWTRPGVVES NAKLSLAEKR
     PAGRPSRRSE RNADNQRTYA ERQAVQRLSE RPAVDIQKDS APGDESVAPL ANNSPPAATS
     GIPVPVMNED TSQKHKTASR GSGLGPKRVA CDACRKRRIR CHHKEENNGA SGSQMTVSTS
     SLGHHTPTAQ DAASALNSLA AIASGAGFQN GLHSIKGMDR MDASANFATS ISATPHGVTL
     KVGDGSPDGL NSAKKGRSKA CDDCRKSKRR CIHDEYGRID PIKAQERSKP RATSLAKRPR
     VHEEAAPSSA NKRLKQESTS PVAQPVHSSH MDTETPTRAQ DSVENGVLDQ YPRKSNTQHA
     DGLPAEKALL PDQSSYASPP AFQADAVATK ELPATVSKPA AVLVSPPTSL ADEMDIHDQV
     DAGGEHVSVI YTPSSGSRQS SRQPRQVERY MPEVHFAKTA KSTTTTPQTT RRSSFGSSGR
     KTTPGLSSGS KKSGSRPSSS HGKKSLSPSV EKKAERHAIS SAPFGQHGRG SKSEHGTSDV
     DPDAESLRLI REIQEQEFGL RRRAGRA
//