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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