ID A0A0L6USB8_9BASI Unreviewed; 694 AA.
AC A0A0L6USB8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=[histone H3]-dimethyl-L-lysine(36) demethylase {ECO:0000256|ARBA:ARBA00013246};
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=VP01_395g9 {ECO:0000313|EMBL:KNZ51433.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ51433.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ51433.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ51433.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KNZ51433.1}.
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DR EMBL; LAVV01009012; KNZ51433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6USB8; -.
DR STRING; 27349.A0A0L6USB8; -.
DR VEuPathDB; FungiDB:VP01_395g9; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000037035; 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; 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
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 SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 213..374
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 76948 MW; EE914191F67F1183 CRC64;
MGTTAPSQAA SAATTAAGPS LTKSDHRCRK CLLNQPSLPS PWIQCSFCTK KDPSLQPIYK
EPPRKSSRAK SKKVNYSDAS NDPLTDPDRF IKIANSKKNV VDGFDVPPTG PHKGFRKMKP
TELSLDWLLN DPEAMSEPIV INDAEGLRAL GMRMPAASLS ISQIAELVGP DTPVEVIDVA
SQAELSRWTL GQWALYYEDP RRERVRNVIS LEVSESPLGS PVQLPAIVKD FDWVHTIWPS
HLRAPGSGKY PQVQKYCLMS VARCWTDWHI DFAGSSVFYH ILRGAKTFYF IRPTVANLAK
YERWSGSSEL QESTWLGDEV NVVYKVSLTA GQTMMIPTGW IHAVYTPVDS LVFGGNFLHS
LNIPLQLRIH QIENNTKVPK KFRFPFFIPM LWFVACHYLR KLEQGLIQQS HLAPGSSSTA
LPPNLDSFPT IPDRILSGLS TLAQFLLLQT DASSAHPPLT STQLFSVVES HLDTDRIPNL
GQTVVKFQHL LQLLNPSPIK PAESLPQLSS IQPSEKEGEE SKTFRSPLQI TLKRKISGPS
SVSPVKEEGQ HKPMTVKLKS KLLTSQNGGT PPPKERQDVA KKSGKPTCKK AKTVQQTRAA
SGDAPPESRK REPGEILKIS NPAPTNDVRR ELRARPSIAE PDDSSSLEQL DVEVRTTRAE
NSVLRRSIDP STGFVVFETR TVKTIIEKAF FPPA
//
