ID F0XHG1_GROCL Unreviewed; 1384 AA.
AC F0XHG1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Lysine-specific histone demethylase {ECO:0000313|EMBL:EFX03272.1};
GN ORFNames=CMQ_3201 {ECO:0000313|EMBL:EFX03272.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX03272.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; GL629769; EFX03272.1; -; Genomic_DNA.
DR RefSeq; XP_014172754.1; XM_014317279.1.
DR STRING; 655863.F0XHG1; -.
DR GeneID; 25976276; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_1_1; -.
DR InParanoid; F0XHG1; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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; PF04433; SWIRM; 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; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000313|EMBL:EFX03272.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Transferase {ECO:0000313|EMBL:EFX03272.1}.
FT DOMAIN 354..449
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1271..1305
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1384 AA; 149912 MW; 3E7FDCF2C0160828 CRC64;
MEGYEDDGHH GGDVSDDSTL SELSSPSDMP DDFKYFALSP EYNSIEAAPG AVPNAGLQPI
GPIESLIESA ETATGNLFET PASRASSEDS CLSTANSMYS LGEEESHTDM EASIEDSVES
FIEVYAEEPP SGDDDERDEP SAEPEEGLPD EELPEEHIPE EQTLEDHADR LAIEPAGTCP
DEATEQPGDK PTKLEPEKAR PLGHVVPSLP PLRESVHKSL ASSVSAITDR SELYSIPSLA
SSSSKATTPI DSDIPLDVSN PSPQLSSAPA SMQAPLPQSL RKLSLSLLPD LQPPQSAVVH
LQHTISSLAS VSQLPASPVP TSPKPSLPIR IVHKVRPKSS IPADLSAREY ARQCVAAAES
SRLNPYALDE EERMILRQHI SHAQVTTYLN IRNGILRLWV RRPQVAVTRQ EAIGCAKDNR
WFDAANVCFH WLVRRGFINF GCAQIRGIQA SVADKVKDNA GGSSSMPSGK QQRRKRIIVI
GAGLAGLGCA RQLDSLFKQY TNRFLELGKQ PPPDVVVLEG RSRIGGRVYS RPFQQQQQPQ
QGEAKEEGNE SGERPVFRCT AEMGGMIITG FDRGNPLNVL VRGQLGLPYH ALWSETTIHD
TDGKPVDSRR DGLAENLFNE CLDRVSEYKF KTPVQAPVEG NRDLMDEGRD SSSSAEGHRM
IAQVEDAQAA TAQAARTVQA VATTAKMAQE AVALAATQLE TLAAKPSAQK ATILPQNGLS
VLPARGTPGV PGVLPAAYKV QKMGWDLRPG VVESRDLHLD AAAKAPGATL GFVIDEAIRQ
YQEMVDFGAK DFRLLNWHIA NLEYSTAINH SRLSLQGWDI DAGNEWEGKH SRVIGGYQSV
PRGLMLCPTP LNLRRNMIVT KISYSLDTGG SNATGHNGWE EGSAPVIIEC EGGYSFEADY
VVNTIPLGVL KHGNVEFEPP LPEWKTDVIR RLGYGVLNKV ILTFPRVFWD PKYDIFGVLR
EPSNGSSLDQ QDYSRRRGSM FQGFNVTTTT GLPCLLALMA GDAAYDTETS SNDELVAEAM
AVLRSVFGAE KVPAPAEAVV TRWASDPFAR GSYSSAGPEM RIDDYDVMAR SVGRHLLFAG
EHTTGAHPAT VHGAYLSGLR AASELIEELL GPIDVPVPLV IPREMAASLK RKAVREEEES
AGGGATGDES GSGSAAGKGG ASLGSSHRAV KARLRRRMEE REQQMEKYVQ AHIGERPLQP
ARVVDTSYLL FSKANYERAR KKCEETMMSR RKGGSGNGSG LSSARALPND VRVLTSKMWR
SASADERRPY AERASAEKQA YVAALEQHRQ EAAEWDRQAT VLRSTFAAEN SDPTATVASA
VIAASSSNSN SNSNSRSSSS MEQIARSPSA MTLDKPEPPA VPRRLRRLTS QAMDADNSDV
DMTG
//
