ID A0A2T9ZBF6_9FUNG Unreviewed; 1715 AA.
AC A0A2T9ZBF6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN ORFNames=BB560_003626 {ECO:0000313|EMBL:PVV01936.1};
OS Smittium megazygosporum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133381 {ECO:0000313|EMBL:PVV01936.1, ECO:0000313|Proteomes:UP000245609};
RN [1] {ECO:0000313|EMBL:PVV01936.1, ECO:0000313|Proteomes:UP000245609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-DP-2 {ECO:0000313|EMBL:PVV01936.1,
RC ECO:0000313|Proteomes:UP000245609};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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:PVV01936.1}.
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DR EMBL; MBFS01000696; PVV01936.1; -; Genomic_DNA.
DR STRING; 133381.A0A2T9ZBF6; -.
DR Proteomes; UP000245609; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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; IPR048615; KDM5_C-hel.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
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; PF21323; KDM5_C-hel; 1.
DR Pfam; PF08429; PLU-1; 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; 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:UP000245609};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 50..91
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 115..208
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 347..489
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1581..1600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1715 AA; 196693 MW; F4B24CEECB663C89 CRC64;
MAATRPQRPK AFDLSSVDTP ASRHRLRGSK DKGSLSSIHP RDNVFKLKSA KTYFPSIAEF
NDPITYIDSI RAEAEQYGII KIVAPPSWNP SFSLDTKNFR FKTRLQQLNV LDGNNRAKKN
YSEKVLAFHE KVFNKHMKIP ILDKKTIDLH NLKTQVCQRG GVEAVIKNKL WAEVGRSLGY
DNKSCTSLSN SLKVTFLNFI KPYEDYLSTD SNEFGIHKPG ESSNPESTVP SNLPPEKNQL
VKDDDIESSS DDEDFWTNYG FEDSPNLYSL SEFQNKSDLF KKSMFQSFFQ NSSPYTTNPV
PLDVVEKRFW SLVKNQDEDF VVEYGADLAS SIYGSGFPTP ELDPLDPYTS SGWNLTNIPK
SKNSLFPFLK EEVDGMTIPW LYVGMCMSAF CWHNEDHYTY SINYMHWGEP KTWYGVPGSQ
SDLFESTVKK HLPELFESNP NILFHLVTMV SPQIFKDNGV DVFTIDQYPV NFATPDWIPF
GLSSIKYYQR HKRHPVFCHE ELIYNINQKY LDSGGTRPDW LLLSMHDLVL TEIHLREDIL
NFFSYNQKSL PMKQVMLDEF IRTNTETSFN SDSSSSYCVN CSECFKLCFF SFIYIRNQNF
GSFVCLQCFK KKYHSDTSKY KTNEISLVFR SSNTDLQSKS FQTSENSTKW INSVWKIIYP
YASDTFSTSS TSHSMKSILN TINVSPNINK FDYNPIVVPT NYSSIILAEI RSLVNYSTYL
LGTEDTPMFI QEYHLQLLEF VKKSNLLCFI SQCLLKQFGK LDKLKDCLKS TIDLAYKVKD
PLVLINDIKQ ETQSTNDPSQ KEIPSSHSEV FKELSILIDP KKDISIDNLQ GSALPPLPHL
KTTNTALKNE HSKKSAANFG SPNKDDDFTT RSHITSSGSR SSRPKRSTAQ YKNPSFSYAA
YITSPFLDES TPSESHSLEP EDVYDFCSRK SKQETLTAIE YIFSKLKINI RSKSQTKDIS
LAHIDKLLKE FSKLKVDCPE ANAIKAWYSQ NIQLQRAAQG FINSMAHFNL INRECSVCAS
DKSICEYLYF DITSFENSSL SQCNELIKWL DDSNIFYPEY SILADLVPKL EWVVSLKNEF
AARSLDMNKL VYYLEEAIKL KIPPNQYEFT RLRSERASVI NWEEEVAEIL GISVRKNAKS
KILTLRKSAT LMERANNFQF FPRYYEDLKE VNNMILKLQS SCDLLVEQAS NDYFPSRPTL
EEAQKLYSTL KDFDKKNTFE FSPNTKPELE QFILDSEKWL FEVKSAFTRP NATRSISNIL
ISVHQTTQRS LNIVSQIANS IIPSDGMKEK RLEKLDFDLN NILYFVDEDN DFRAGQVSNT
RAKLKPLREI LCVCQSTDTG SKIKCLTCPI VFHTKCLKLS KDSNNEYTQS PCPVCLQNSL
FTYSTKNPSL TSVNLLIEKG RRLNLVCPEL DLLLNIALDV RSISSTINKC IEPLEKLSGD
RTKNMKYKHL HDSICRAILL ITTGLEVNIA NENVGSISSI GTYFDITFRK KLFNMSLNNP
QISEGFLAER KRRTRYNPKQ TLPKTTSNSE MERSSLLLLG QHKKRKASGE KISVYSSDSQ
EEVPLEARLF KEEASLRGFD SSTKSFKSKP SSSAKRFTEK ESKAHLLSTS SIEKLNHEIC
VCRATPKTDP NWHRYNNFII QCDFCREYFH INCVLVPEDQ AAEILYFQNL RKNYKTAEPL
NISMSSFHKG MAFMCPICSY TKNIPYEYGE IILDD
//
