ID C8VTU6_EMENI Unreviewed; 1405 AA.
AC C8VTU6;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN ORFNames=ANIA_01060 {ECO:0000313|EMBL:CBF88234.1};
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;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF88234.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
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., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., 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., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., 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] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR EMBL; BN001308; CBF88234.1; -; Genomic_DNA.
DR STRING; 227321.C8VTU6; -.
DR EnsemblFungi; CBF88234; CBF88234; ANIA_01060.
DR VEuPathDB; FungiDB:AN1060; -.
DR eggNOG; KOG0954; Eukaryota.
DR eggNOG; KOG0958; Eukaryota.
DR HOGENOM; CLU_001442_1_3_1; -.
DR InParanoid; C8VTU6; -.
DR OMA; NQERVNR; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IMP:AspGD.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IMP:AspGD.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd15571; ePHD; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 76..117
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 347..510
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 590..715
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1405 AA; 156910 MW; DA6F03372E65DA97 CRC64;
MAATIDRPLF EPIAGGPATD AASITPPHSI NGKKDGPDGA PSELSDLELD SKPTDAQEDI
SVEEGDQEIE PDHYYGGGKI PVFKPFRDFQ SFIKRIDKYG MRSGVVKVIP PKEWRDALPP
LDEAVKKIRV KNPIMQEFHG SHGTYTQANI EKQRSYNLPQ WKALCEDGSH QPPARRGERR
RNQERVTRAP SAPKAQTTRA DTPKRGPGRP AKRSNQAKVK EEPVKIKEEP AADEVMEKIK
PEGPPTPVSP ESIPAETKSE ALSDGESLSA PKSRGRQPKS VTARRKQNKG DTVEHVDEEA
YKNFDYRIHD NEDYTPERCE ELETAYWKSL MFNNPMYGAD MPGSLFDDRI TSWNVAKLPN
LLDVIGQKVP GVNTAYLYLG MWKATFAWHL EDVDLYSINY IHFGAPKQWY SISQEDAPRF
EQAMKSIWPS DAKTCDQFLR HKTYLVSPSL LKSQYGITVN KMVHYEGEFV ITYPYGYHSG
YNLGYNCAES VNFATEKWLD YGRVAKKCNC EADSVWIDVE EIERKLRGEL TPEYYGEYDS
DLDGYEAASD LLTPPRSVPE KTSNRGRKRK HDGDMNKAKR MRADMGIPRR LPCLLCPNDL
DYEDLLPTED GKSHAHRRCA LYTEETSILR DGSGKEVVCD IDKIPKARMG LKCLYCREVR
GACFQCNFGK CTRSYHATCA LLAGVQVEEG LVTVVADDGS QYSVPSVDLK CKYHRQKKPT
WMTSSESPEN DRKLMDTARR LVTGDILQFQ ADKEIYGAVV IENRVAERTL QVKVLPRGDV
IELPYRWMLV VRRSNFAPLA AGIKPLPAHL SRKPEGRREL ESALPVAGNP FGDGRSPYQW
AEFETVDSTN RPAAPPAVQV DLGKMEQIWY YLGQSSTECR AQYTHNPSVP IHNPRSNFLD
SVKSLGAVMA RLPSYPHHRL PSYVLTTPPP HLLSSAAATT TASAVAAAAA SRPLLPPRPP
FAPPRSSPAA PTSAAVAASA MPSAYRSLPN QIARHAPYPQ VTKAHLQSQQ QHSHQQQQQN
TNGSHSTANS HLPANNFANV RELIARRRLA QITDHANVFA GYTIVGPELV VETLLGPMGS
VPPSNGLEKL ELAMAQQRVQ PRAPDGTLLP MQPLNMRSEE VTRLLQMLRF SLISHRDRLD
VLQKKETETA KQEAANKVKG ATPKLPRKYA YLELQREQAP TVYQSPYDMP SGFTEYARTT
FGLTRHEPEL PKPSLANDYF ASLSPENQEK ILKTCGSFVQ RAIERSAPHS RQSSSSNFRL
ASALAQQTEN PTIDITTVEN MPLSGLDFPL RADSPCSNFS RSHLRFHSPN DFSHHGTEVH
HDHHDLFGDQ QANTRFWQHG PWAAGDGNTP NEENRPFFGP HERLKHDYAS SDISLGRGGP
GSLHSVDMAG FGLDNPDDLC AALSP
//
