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Database: UniProt
Entry: C6HJD4_AJECH
LinkDB: C6HJD4_AJECH
Original site: C6HJD4_AJECH 
ID   C6HJD4_AJECH            Unreviewed;      1502 AA.
AC   C6HJD4;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
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=HCDG_06315 {ECO:0000313|EMBL:EER39210.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER39210.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; GG692429; EER39210.1; -; Genomic_DNA.
DR   STRING; 544712.C6HJD4; -.
DR   VEuPathDB; FungiDB:HCDG_06315; -.
DR   eggNOG; KOG1633; Eukaryota.
DR   HOGENOM; CLU_002979_0_1_1; -.
DR   OMA; KFGIWVA; -.
DR   Proteomes; UP000002624; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:UP000002624};
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          357..417
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          612..770
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1115..1140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1268..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1330..1502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1173..1192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1268..1282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1355..1418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1419..1433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1439..1455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1461..1502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1502 AA;  166320 MW;  DE534CBF40A303C1 CRC64;
     MANTLSFRNP SSVRPSRYRT PSPPRHAIES ISPRAPAHIS SFSTRNVHPN DAPQQPRYDT
     FREKESSLKN GWSNASQDGR ASLDHSSHHY FSGGSSSNDA NTNPASRVGH KRTGSNIDTL
     ATIALATSPT FAPLAYDEHP TAISPTTHHA PAPDQSERPS KRARSEKAPS PTWLMGASRP
     ATSHVSTFDS MKTDAELLLN FARPSNFPPL QEGSGPQQLA AHELANGQQL GVKWATDTAN
     LWAKRWDITA ENKPSSAFFR NNNNGTPSRI RSRSDGSAFT GRPLMNGFSG PSLPPLMGPA
     LEDDLIDPHH IPDQHHNSAQ ANRPNGQETP SAQLQRPKSV PTSDLKEEDS DNDGSNQATC
     AACNLDRIAS DSEDEEAVTW INCDGCMRWF HIVCAGFKSD RDTRIVDKFI CRGCRPRHGP
     TTFVRKSSRA RTAIDYASLN QGFVMSSTET PEHHYIQPIK EGKITFLPDH FARIRPELVT
     AEYFERGIGM TEPVIIPASL NTRSSVPGSA DYYAPEASTQ EEFDELADNM PDDDVYFNEV
     LDCGQDLLDM VIPQGLTVRH VAELYGPEER VEVIDVKSQQ GEDKRWNMQR WADYYYDDSA
     SKTVRNVISL EVSNSPLGRL IRRPKIVRDL DLQDHVWPAE LQAIGEFPKV QFYVLMSVAD
     CYTDFHIDFG GSSVYYHILK GRKTFFFIPP KDKYLKKYEE WCNSAAQDTT FLGNQTKECY
     RVDLSAGDTM LIPSGWIHAV WTPEDSLVIG GNFLTMMNYG MQIKVAKIEK DTKVPKKFRY
     PYFQKIMWYA AIKYLEDDPI PQTVLESFSR DENYRFYREY PIYYEFGENG NGAEPGSLYY
     NARFYSQAEL DGLPELAKYL LRTALIAGGY QVDGVTTETR NAVKKSIPKG PTDPVNTVIK
     FGVWVAWKRG NEHAASWTRP GAISLDTKVD MSGRKPAGRP SRRSQRNIVA ESSQLNNNLE
     LRTGRRPSYQ LSEFNTSGTS STSFASTNAP STSGTPAPPK RKASLIDMKS EITHATKPRL
     MSKSTGLGPK RVACDACRKR RIRCRHKDEQ GLDAVTSVAV KQQHLNGRDM ATAGSLNLAS
     ATYMDGIEEH RSGKRDAMLP SSVDDSSALF MTHQANSGRM KGFIPNSSNP GKKGRSKACD
     ECRKSKRRCI HDENGRIDPV KAQERSKPRA TSSTKRPRSS DGNISPTLSK RQRPESEYSE
     EELPQTKLNF ETVQLQGRMN GQNEKLVSSE NAGIPTHSEL ATNQTSYASP PTLKADLVTA
     SEVTASLSAT TGPASSLVSP PTSLADDMEV DPNQTDGEAK PAVKNEQQQQ EHYGGRSVVN
     DALTTLCRNA SRHQRHAPEA TVPAAEVGSR KMTTATRAPP ATVTAPSDLS VAISSPSAST
     SILKKSSSSS LSSPSPRPSS SYHRTNVHPF PSSTSSLKHE METKQHNPVV DKNRLEGSHP
     PPQPNSNSNN RHTSPTSPHR RSKLTGRDRG SFSDPDADPD TLRLIREMQE QDFGLRKRPS
     RT
//
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