ID A0A2Z6S0K5_9GLOM Unreviewed; 1189 AA.
AC A0A2Z6S0K5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=RclHR1_00310004 {ECO:0000313|EMBL:GBB97876.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB97876.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBB97876.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBB97876.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 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:GBB97876.1}.
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DR EMBL; BEXD01002335; GBB97876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6S0K5; -.
DR STRING; 94130.A0A2Z6S0K5; -.
DR Proteomes; UP000247702; 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 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; IPR019786; Zinc_finger_PHD-type_CS.
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; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000247702};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 256..297
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 321..417
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 446..497
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 584..750
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 991..1041
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 133..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 135914 MW; 0C070A592DCEA808 CRC64;
MVKTRAGSKP QPTNKNIISS FTKVQKANTQ SRKTLINLNS QELKFTLTSS TSHSQKKGYY
MENNSQASNS SLMNSTLYSR KQEPRMQPNL QPSSLKKVNL MVNSRMHESR MQIVSQAPSA
SSTGQTRMQC SRVQTISQVS KPTSLTSPGQ TRMQGSCVQP ISQDSKPTST TNSILLSRMQ
GSRMSTNSAQ STAVAKPSVE SGKNSGLIPD SVEKETIRLK EVEPIICEPF DFTTVRTEYQ
YKDPPKGSRK KDILEAPVLY PTPEEFRDPY AYIESIAHIG HRYGIIKIVP PEGWRPPFVL
NTEEFKFSTR KQTVNTMEGQ TRVKLNYLQQ LQMFHAQQGK KNFVKPPLVD RTPIDLHLLA
KVVEEKGGPE EISNKKQWAE VARAIRPDGY SAKCTSLSKT IKEKYQEIVE PYETYIADVK
AECREGRSIN LQTDPDSDSD HMDIDEEVCG ECENIIRSDP LICEGDCQKA FHAKCLKIKR
SQIHPGASWH CPKCLFLYGT KFGFDPSETY TLKAFQQIAD DFRQRYLKKR PVPQGVSVED
HVENEFWRLA MSADHDTEIL YGADNSSIDY GSGFPCPKAH SSDPYSRDPW NLRNFPKLPG
SLLSHIRPAI PGMMIPWLYV GMMFSAFCWH VEDHYTYSIN YMHWGETKTW YGVPAASAAK
FEAAAGRLLP ELFQNQPDLL SQLTTILNPI AIIGEGIDVF AIDQRPNQFV ITFPQAYHAG
FNHGLNFNEA VNFALPDWVE FGQKSVNYYK KIRRDPVFSH EKLLVDIGLK KINNFKVLSR
LKESLIEVCQ SELRRREEVT SRLRLPEANY DLTDPKDDET LCAVCRSWTG LSALQFNCTK
KVLCLECACV DTDTCCCENP CYYLRVRYSD RHLKSLAQRV KDLMQLRKDR YKALIKHVNK
VNTLALEQLA PIIEINRTYR FGLPLGDMES IVDDAANWEN NLTLIAYETA RNIWPNDYQD
VPLNEFDITD FLYQWDCRLR NVYRAGNDRK NYFCFCRGED YGGKMICCDK CDVWYHCECI
NMKSEDTLNY EHWYCAMCRA PRTARIKIDE NVRRIETLAN EAENLRINLP CISASFVTEI
NAELKKLLSG NDIHSVRIGV GLGFGLPLDG SVEFEEGVDD VDLSNFMEDN DLNSKFFGNI
EANSKNPEDS DISKRNVENF NLGQHIENDV ETRKRKCVLE PIERKKRRR
//
