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Database: UniProt/TrEMBL
Entry: G2Q230_MYCTT
LinkDB: G2Q230_MYCTT
Original site: G2Q230_MYCTT 
ID   G2Q230_MYCTT            Unreviewed;       783 AA.
AC   G2Q230;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   07-JUN-2017, entry version 43.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEO55063.1};
GN   ORFNames=MYCTH_2086155 {ECO:0000313|EMBL:AEO55063.1};
OS   Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS   (Sporotrichum thermophile).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Thermothelomyces.
OX   NCBI_TaxID=573729 {ECO:0000313|EMBL:AEO55063.1, ECO:0000313|Proteomes:UP000007322};
RN   [1] {ECO:0000313|EMBL:AEO55063.1, ECO:0000313|Proteomes:UP000007322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799
RC   {ECO:0000313|Proteomes:UP000007322};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J.,
RA   Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B.,
RA   Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J.,
RA   Lucas S., Harris P., Powlowski J., Bellemare A., Taylor D., Butler G.,
RA   de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R.,
RA   Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J.,
RA   LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M.,
RA   de Leon A.L., Rey M.W., Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading
RT   fungi Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000256|SAAS:SAAS00591578}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|SAAS:SAAS00563877}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00574581}.
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DR   EMBL; CP003002; AEO55063.1; -; Genomic_DNA.
DR   RefSeq; XP_003660308.1; XM_003660260.1.
DR   ProteinModelPortal; G2Q230; -.
DR   STRING; 573729.XP_003660308.1; -.
DR   EnsemblFungi; AEO55063; AEO55063; MYCTH_2086155.
DR   GeneID; 11505914; -.
DR   KEGG; mtm:MYCTH_2086155; -.
DR   eggNOG; ENOG410KJHV; Eukaryota.
DR   eggNOG; KOG0409; Eukaryota.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2084; LUCA.
DR   eggNOG; COG2940; LUCA.
DR   InParanoid; G2Q230; -.
DR   OrthoDB; EOG092C1QPC; -.
DR   Proteomes; UP000007322; Chromosome 1.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 2.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR029154; NADP-bd.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF14833; NAD_binding_11; 2.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|SAAS:SAAS00508265};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007322};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS00590675};
KW   Nucleus {ECO:0000256|SAAS:SAAS00574642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007322};
KW   S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00591079};
KW   Transferase {ECO:0000256|SAAS:SAAS00591533}.
FT   DOMAIN      525    611       Pre-SET. {ECO:0000259|PROSITE:PS50867}.
FT   DOMAIN      614    749       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN      767    783       Post-SET. {ECO:0000259|PROSITE:PS50868}.
SQ   SEQUENCE   783 AA;  85013 MW;  5202BFB4874AFDB0 CRC64;
     MAEPKPPIAF IGLGAMGFGM ATHLVKQGYP VTGFDVWAPT LERFAAAGGL TASTPSAAVA
     DKPFCVCMVA TAQQAQSVLI DGPDAAVHAL PKGAALLLCS TVPCDYVQSL DRQLRSLGRG
     DILLVDSPVS GGAARAADGT LSIMAGMSDA ALDKARPLLA EMADPAKLYI VQGGVGAGSN
     MKMVHQVLAA CHILASSEAV GFAARLGLDL AQTQKAVLGS DAWNWMFEHR TPRMLTQFQP
     VASAVNIIVK DTKIITAEAK RSGFKVPMTG RAEEGYQQAV DKGYGQDDDS SLLRLYTGAG
     SGETGESSAE ADEEKLALVL DLLRGINLCA AGESLAFASF VGLDLDQVLD LCVNAAGSST
     MLKQYGPQFI TALRQGVDSR SSKAAEGELS LDAVAERLQR VVEEAERVKV PLFLGSRALD
     VVREALKLGT SPLSVNAVVN RGRVPTANME KSIRPHFFKH GLPESDPEEE KNCHWCQIRS
     FATHKTIPIT IVNDEDDEVL NPNFRFIDHS VIADDVPVAE DSFRTGCDCA DDEDCMYNTC
     QCLDEMAPDS DEDENDGSAT RPRRKRFAYY SSGPKAGLLR SRILMSREPI YECHEGCSCS
     LNCPNRVVER GRTVPLQIFR TPDRGWGVRC PVDIKEGQFV DKYLGEIISS READRRRAEA
     TVSRRKDVYL FALDKFSDPN SLDPLLAAPP LEVDGEWMSG PTRFINHSCD PNMRIFARVG
     DHADKHIHDL ALFAIRDIPA GEELTFDYVD GLEDMDNDAH DPSKIKDMTV CKCGTKRCRG
     FLW
//
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