ID A0A167A706_9PEZI Unreviewed; 1732 AA.
AC A0A167A706;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Histone demethylase jarid1 {ECO:0000313|EMBL:KZL79790.1};
DE Flags: Fragment;
GN ORFNames=CI238_02040 {ECO:0000313|EMBL:KZL79790.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL79790.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL79790.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL79790.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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:KZL79790.1}.
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DR EMBL; LFIW01002023; KZL79790.1; -; Genomic_DNA.
DR STRING; 1573173.A0A167A706; -.
DR Proteomes; UP000076584; 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 GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
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; IPR001841; Znf_RING.
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; 2.
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; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KZL79790.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KZL79790.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 100..141
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 165..258
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 464..514
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 467..511
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 606..772
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1327..1376
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL79790.1"
SQ SEQUENCE 1732 AA; 194684 MW; B38C95A2528FBA5C CRC64;
LITTMVSAPT TGGTAAANGN GSANASSRAS PAVGAPNTAS AKSKAAQVNS NGYHPTNPQV
PLSSMRSTPL DLTSVERRGQ ATAIKEPVKK KSRPHGLEDA PTYCPTEEEW KDPMEYIKKI
SPEAKNYGLC KIIPPDSWNP DFAIDTERFH FRTRKQELNS VEGSTRANIS YLDALAKFHR
QQGNNLHRLP YVDKKPLDLY RLKKAVEARG GFDKVCKLKK WAEIGRDLGY SGKIMSSLST
SLKNSYQRWL CPYEEYLRLA KPGVHQQLEY ENGGPYTPSP AVTPMKRSNV NTPSSARADS
PARNASDALQ ASINGLKKEG DRDTPMADAP PAPAPVTSGF RAINTGGFTA VNSGFKSVNR
PTPQDDVTST PPPKSFSPVN SAKNTPEYRP SNLGPAALKR QMSCESLDSA KKDNAADKDD
GDAGSSRRSK RLKKDTVPTV AGSHMSLFRP SVPRIPRDEA STPGEKCEQC GKGDESSPLI
VCESCDHAYH GTCLDPPLKH KPDSEWNCPR CLVGDGQYGF EEGGLYSLKQ FQQKAADFKQ
GYFEKKMPFD PVLNCHRPVT EEDVETEFWR LVADIEETVE VEYGADIHCT THGSGFPTVE
RHPNNHYSTD PWNLNLLPLH PESLFRHIKS DISGMTVPWV YVGMIFSTFC WHNEDHYAYS
ANYQHFGATK TWYGIPGEDA EKFEAAMREA VPELFETQPD LLFQLVTLLT PEQLKKAGVR
VYALDQRAGQ FVITFPQAYH AGFNHGFNFN EAVNFAPCDW EPFGLSGVER LQVFRRQPCF
SHDELLWTAA EGTTNNGLTI QTAKWLAPAL DRIKKRESAH RGDFVAKHLE SQWHDCGLAG
KEGTSCPLKF EIDDTDVPEE EYQCSYCKAF TYLSRFKCLK SGKVLCLAHA GHQPCCDMPE
QHRLNGEGHA VIYRQSEEDI EATYAKVLEK ARTPEAWEEK YEKLLEEEAT PSLKTLRNLL
HEGEKIPHDL PSLPLLREFV ERCNDWVEEA TNYTIRKQQN RRKSEKSILN RKNSLDQKER
DARNVSNVYR LLSEAEQIGF DCPEITQLRE RAEAIEAFQK NAAKALEQIH LAELSEIEDL
LEEGRTFNVD MPEVDRLSRV LEQLKWNEKA RNNRGVLLSL NEVRELIEEG KRLDIPPYND
HLSYYIDQMS LGQQWEKKAR ELIVAEVVHY PQLEALSMQV TANFLPVSAD TLAAVDQILY
KQREAHRQIV DLTERSRDPD IRNRPKYAEV AEIMRRLDDL NSKPNGTLDL EREQKRHEDW
MREGKKLFGK TNAPLHILKS HMDYVFERNQ DCFDIVNDKP RMPAEPASRE ASPDQKVHRW
EDPRFREVFC ICRKVEAGMM IECELCHEWY HGKCLKIARG KVKDEDKYTC PICDWRVKIP
RDAARPKLEE LITWSEKIPN LPFQPEEEEV LTKIIDNAQD FRNHIAGYCN PLVSTESEAD
TQRFYLRKIE GAEILLAYET NFFRQELHKW CPVAPNAPPV LEVSKSTRKP RPTKLQKLLA
QFGVDDPEDL PENMKAKAAS LKRKAQNAEA AAAAAAAAAA ASATGATVPP GMSGNSRKSE
QSSATPPSTS HGNVGRQSIG SNHDPMDIDN GPTLHPGLFM SNGAPGPQLV VGNSSLSLEE
RLLQGQEDGL NLHTEAGKSK ALEILRRTEV GRKRAVEMFG PDVFKGDVGM LNGREDVPRS
QEEERAVNKM FDDLTNQDDD DVKRKQESFD GPITAESLES ERNGMDALLD GD
//
