ID G3J989_CORMM Unreviewed; 1071 AA.
AC G3J989;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Lysine-specific histone demethylase 1 {ECO:0000313|EMBL:EGX94068.1};
GN ORFNames=CCM_02339 {ECO:0000313|EMBL:EGX94068.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX94068.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX94068.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX94068.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH126400; EGX94068.1; -; Genomic_DNA.
DR RefSeq; XP_006667554.1; XM_006667491.1.
DR AlphaFoldDB; G3J989; -.
DR STRING; 983644.G3J989; -.
DR GeneID; 18164366; -.
DR KEGG; cmt:CCM_02339; -.
DR VEuPathDB; FungiDB:CCM_02339; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_2_1; -.
DR InParanoid; G3J989; -.
DR OMA; WCAENPF; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR CDD; cd00084; HMG-box_SF; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR Pfam; PF01593; Amino_oxidase; 2.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Methyltransferase {ECO:0000313|EMBL:EGX94068.1};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Transferase {ECO:0000313|EMBL:EGX94068.1}.
FT DOMAIN 191..285
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 933..1009
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 933..1009
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 110..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 119121 MW; 4F7B5377EA714321 CRC64;
MEADVHSQYR PGYELGPCDT RPIDSLPVLS NVVATAPTRS NVPPVNRRVQ VSTGCHHNSS
YGPISMAEDP RGVESQVLEL DTVTPPLGHN VSSKIKIENS DCEIPIPSLN NGATESFDSE
MSDLSSRQSS FSSKATTPAD NDTPKKRIPG ISTPTMPQRS FSHDGDRLDF IVQPKSSVPK
DIPSSQYATE CIIAAENSRL NPYALHTEEY LLLRYHISHA QVTTYLNIRN SILRLWLQKP
WQGITREEAV GCANARWFDA ANVCYDWLVR RGYINFGCLD LGRVATRAKH QSQSRKRRTI
AVIGAGISGL SCARQLEGLF KQYAYRFHEL DEDIPRVLLI EGRSRVGGRV YSRQFKTQPK
SPMDGFHNKR CTAEMGGMIV TGFDRGNPIN VLVRGQLCLP YHALRAETTI YDSDGKPVDA
ERDQLIEKLY NECLDRVSEH KYKMVAAKLI AGNRDLLNEG KDSPTDGSKT IAQSEELAAS
QANESTQSQQ NAGDVEPTVP VSSNELTTEA GVPATAKAPE KAAYMGWTLK QGIDTEKDLD
LSYAVHNPNA TLGSVLDDAI SQYKSLVELN ALDHRLINWH IANLEYSNAT NLHNLSLSLW
DIDAGNEWEG SHTMVVGGYQ SVARGLLHCP TPLEITTKSP VKRIRYQADT FNGPARIECE
NGRVVEVDSV VCTVPLGVLK HGNIEFDPPV PEWKSLAVER LGFGILNKVA LVYDQVFWES
DRHIFGVLKD ASDPQSTAQH EYRGSRGRFF QWFNVTNTTG IPCLIALMAG DAGFDTEASS
NEDLIREATE TLRSIFGPDV PQPLEAVVTR WGSDPFARGS YSSAAPNMQP EDYDNMAKPL
GNLFFAGEHT IVTHPATVHG AYLSGLRAAS EVLQEILGPI EVPTPLILPR DSLLLQKRKE
AAKDPRQARV DAYETEAWRH VKSRIGERPI PPGKMAGNAY LIFSKLYFDE ARRRCEENRK
TGRTKAMPNE VRVMTSRMWK EASEDTRQPF EAQAMEQKQV YAEAMAQYTQ AAEKWDLEAI
EIRATYERNN PFMPELGDAA TGSSSRELLT PKSRRARNVS YAEDNDNGME F
//