ID W9YJL0_9EURO Unreviewed; 1396 AA.
AC W9YJL0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=A1O3_01653 {ECO:0000313|EMBL:EXJ93097.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ93097.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ93097.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ93097.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ93097.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMGY01000001; EXJ93097.1; -; Genomic_DNA.
DR RefSeq; XP_007729987.1; XM_007731797.1.
DR STRING; 1182542.W9YJL0; -.
DR GeneID; 19165787; -.
DR eggNOG; KOG1633; Eukaryota.
DR HOGENOM; CLU_002979_0_1_1; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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:UP000019478};
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 370..430
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 633..792
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 104..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 154666 MW; 3BD81EED519D1699 CRC64;
MPTSTLWRRS EDLARLRAIS PIRPSAELIE RLSPEPTLEA SAPLEPSLLS HTFQENGNSL
SGLGLSHAGL SESVPVTVQP DHLFYAQDGS AHVGARLVGG AAPQNRRWLQ DSRDWSSRNS
KFSHDARNPR GKGHTRSGST IDDLASAAIA HSPDLVHASP TALSKASPYP AARPSTSYIH
RYEQIDASDG PPTKRVKSER IPNLEWSPRA DRPKTSGYDT NTDITYEDAL LLLELKNEVN
FKDGTPQIPS DTLHDRSYSS HTTRRQSNGW TAKAGQVAQH KHVEDGQPED SRMQGIHFVA
DVSRTSYSDM LPQRIETSAA QNLDATDERT TAVDPTATSS QQEIKQGPEA NPPSNVPTKK
QRRVKPEVQA EVCAACQRLQ VNAADDENSV MFWISCDACN RWFHAECAGF KTKAEARSVD
KYLCKDCEPV HGKTTYVRKS SRPRTAIDYA GLHQGVVKSS AETSTHHYIQ PIKEGKIALL
PDDFARVRPE LLTAQFMESF DGMKRPFVVP ACWNPRFGVK RPSSEAHSDM DKNDGAPLTL
IDSTGALVGP DILVSNHVEE EEVIDCDQDL LDMVIPRDLT VRKVAELYGP DEHVPVIDVK
SQETKGQFTL QQWADYYELA GEKPILNVIS LEVSQSPLGK LIRRPKVVRD LDLEDHVWDG
DAETRTKKRP VQFYCLMSVA DSYTDFHIDF GGSSVYYHIL RGTKTFFFIP PEDKYLKKYE
DWCNSDTQNE TWLGDLCGGN CTRVDLHEGD TAFIPAGWIH SVWTPEDSLV IGGNFLTRLD
YELQLKVANI EKVTKVAPKF RYPYFQKVMW YSLIKYLEDD PVPDEVLNDF RDDPDYVFLR
ANPVWHEFDD LESVAEPGES AFNARYYPKS EVSGWPSLRD YLYRTARIDA GLPVADITKK
QIDAVKASIP KGHGDPLTMI KLFAIWCAWK TGNIPVPEWV HSDGALESEK TEKAKRPEVF
RMPGERSSTR KAAQSLAQVQ APQPEVSIPI PAKQNVKSGS GSKGSGLRVA CEPCRKRRIK
CRHKSGSETP TRPAPVIRPR SFSNADNTSN SAIPQNGPNG EQLTPSGARL SEPVGIHSEA
AHALSANTDQ PSSSKKSRTK ACEECRKSKR RCVHDEHGRI DPAKAAEPSK PRGSTSSRHP
ARLSDGSVQN KQWRLDGDLL DDLIDPALTN GNTFEMANEE VEDESLTPAP LNGIEIDGNM
ASLDTIMVDP ALDAMTAASI EVIKTEVDLA ENHSLKNAAD ETSPGLKSNI RVSTPATVKN
RRSVNGDFSG EPDTIPLSRH SPRQAKQMER FTPEDKRSPC KPPPKPQRMD RRASSAASAQ
TVVTSVKSRR SSSNTSGTIH QMASNMVRVS PSREGSVRPV SRGSTGGESE MDADERFARE
LQAAENGLRR RTSMRA
//
