ID A0A1B9H2Q4_9TREE Unreviewed; 1966 AA.
AC A0A1B9H2Q4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Histone demethylase JARID1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=I316_00679 {ECO:0000313|EMBL:OCF37553.1};
OS Kwoniella heveanensis BCC8398.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF37553.1, ECO:0000313|Proteomes:UP000092666};
RN [1] {ECO:0000313|EMBL:OCF37553.1, ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|EMBL:OCF37553.1,
RC ECO:0000313|Proteomes:UP000092666};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; KV700122; OCF37553.1; -; Genomic_DNA.
DR STRING; 1296120.A0A1B9H2Q4; -.
DR Proteomes; UP000092666; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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 PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 3.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000092666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 198..239
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 263..352
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 490..541
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 656..822
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1820..1966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1820..1842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1879..1894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1966 AA; 216968 MW; EEB210D1B0B8EB8C CRC64;
MIQPQTPPLG VTSAGVNVSA SAGASTAKPL SYPTRQRMAS SSSAKPPRTP NMSNGPNGAA
HSNTSPTKRS SPSESKRKPT FTSSLQYPDV LPAPTYFSAG TGEGGELQRS QRRSKAEANA
KLDRGGTPIQ VNTGPTATSF LPPSAQPQQP IAGPSAARNP LHRPTVINPP FSPSTVRQEA
PRYPTSRTAT RPFGLEECPV FYPTAEEFKD TMAYISSITE EARPYGICKI VPPEGWKMPF
TLESETFRFK TRLQRLNQLE AASRAKINFL EQLSMFHNQS SENEISIPRI DRQPLDVWKL
RKEVNKAGGY LELDRTKAWG KITETLGHKP IWGPHVREAY MSIVLPFDRW ALRAKSASVS
PLTPMQAPNG TRPPAFTTDT PPSPSQIKSA GRMGSVKVSP RTRMSSRMGA QTASLPANAA
PFSSVNGLQA AAEIEQATLV NGDPSTTVKI KVPGFSTRDG SESELSDADS VLSDGSPRKP
QVATPEYQKG EVCEVCRGGH AADKILLCDG CDRGFHTYCL DPPLASVPTN EEWFCTSCLL
SQGDDFGFDE GEDHSMASFQ ARDASFSYHW WNRHRPQATS SSAPPSSNGL IKDIKPNNPL
ARNFGKVSVT EDDVEREFWR LTESATDTVE VEYGADVHST THGSAGPTME THPLDPYAAD
GWNLNNMPIL PDSLLRYIRS DISGMTVPWI YLGMMFSTFC WHNEDHYTYS VNYMYWGETK
TWYGIPGSDA EKFEEAMKSE APELFEQQPG LLFQLVTMMN PGRVRDAGVK VVACDQRPNE
FVITFPKAYH CGFNHGINMN EAVNFALPDW LAEGKESVVK YQGYLKPPVF DHNELLITIT
LYSETIRTAI WLRDSLEEMV EEETRRRDHL RALYPNLNET IVEDDGPEDQ YQCAVCKAFC
YLAQITCSCT KLVTCLDHAE QLCSCSKSKR TLRKRYTEAQ LDEILAIVVA RASQPENWRN
KLYSLLEVPR PALKSMRTLL AEGEKIAYSM PETYDLRALV DRAYSWVDRV SALLTRKTAG
RRRKGKKDEE EDEDMVGRSP EVLSALLKEG ETLAFDAPEI LQLRQSLLSI QSFQSEASVI
LSTPEDQLDL EKCKTVLILG ESLNLDLPEI AAISTIINRL TWFRKVEDEV DDRTLEYKDT
VKLLQQAEEF DIPETHPTIV ELKRRRQKGA DWLEKVEELF ISPTIQIDQI STLIEGQELV
PVAVDKMRQL ENMRKTVLGW QSSARNFLSS NGSALAASRL CKNVSSASAP INRVEIPEII
ELQEELDHHA LWQEKVAEIL EVPINQVTHT VKFLLREFEH HFNPEDDEPS DDIVCFCRNP
PGAVMVTCRN CQGEYHPRCV GVTPKNASNP FQCAMCLRIL PGDGPSLNEF AALATSERWN
FKITPPDFVM AKSLVDAAVR YSVVMLKMID ARDEAEPYRD VDKIQHAIRK IYSLSLLYDA
YNFKTNERVV FVKWLFKRMQ DAIKFHAGLL KDGVAPPKER TRTRGRKPRF VLAQAYPKEL
HCICPAGQRT PDYNVLVDCM KCGQVYHASC VRAPPECIGT DGKGWRCPCC AVKEAKYYQK
GVEVRVQMKE QFGTNEYIDY RSTINEYAET PIMVHWPPSS DVILLECTKF VPPILPEDIG
RDASAFEGQG GDASKKRRKV RPSDVATSDI NGHTASVHGD LYRSTNGPVN GGSSGHATPT
SATPTQANFT DARVNGKAGP SSSHHTIYNP QPIDPFPPAL TTVDLPAYAN GDTQTHTHAY
SHSPLPVHPT PNLHLAPSAL GIHATGEDTY NIRSSSVYVH NSPPVASVNS ATPLLSRQPP
PHVLPTATTT EELVSILTRS VEPAEDSNQP PAASTTPSII EYHSPLPGTA ALPTTAGAED
VPDPDIADVV SSKSERKLSA SPPGRKRKSR SFETEGAIDL SADPGPGSAF SALNAGSASG
AGTVGSESNG YEGDVRLQRG DGGVRMERSG TGGSKGSSVD DPIEID
//
