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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}.
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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
 
 
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