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Database: UniProt
Entry: G2QD98_MYCTT
LinkDB: G2QD98_MYCTT
Original site: G2QD98_MYCTT 
ID   G2QD98_MYCTT            Unreviewed;       499 AA.
AC   G2QD98;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   22-NOV-2017, entry version 36.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEO57464.1};
GN   ORFNames=MYCTH_2303668 {ECO:0000313|EMBL:AEO57464.1};
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:AEO57464.1, ECO:0000313|Proteomes:UP000007322};
RN   [1] {ECO:0000313|EMBL:AEO57464.1, 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   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CP003004; AEO57464.1; -; Genomic_DNA.
DR   RefSeq; XP_003662709.1; XM_003662661.1.
DR   STRING; 573729.XP_003662709.1; -.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; AEO57464; AEO57464; MYCTH_2303668.
DR   GeneID; 11512785; -.
DR   KEGG; mtm:MYCTH_2303668; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   InParanoid; G2QD98; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000007322; Chromosome 3.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007322};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007322};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   499 AA;  53318 MW;  970CF063A9F04ACD CRC64;
     MASPPKSAFE FLDFVNASPT PYHAVASAAA LLDAAGFTKI QERDNWASTV KPGGKYYTTR
     NGSSVVAFAV GAQWKPGNPI GMVGAHTDSP CLRVKPVSKR TANGYLQVGV ETYGGGIWHS
     WFDRDLSVAG RVLVREGEGS FVQKLVKVDK PILRIPTLAV HLHRQSNFDP NKEDELLPIA
     GLAEAELNKT AEPDAAGEAA GGESDFEPLR ALPERHHPAF LSLVAQQAGV DVSRIVDFEL
     VLYDTQKSCL GGLRDELIFS PRLDNLNSTF CSIKGLISSV RSIPLDHDAS IRLVACFDHE
     EIGSLSAHGA DSNLLPAVLR RLSVLPGASS SSSSSSSSSP ESASQSASSD VAASTAFEQT
     LATSFLLSAD MSHAVHPNYA AKYERNHTPA LNGGPVIKIN ANQRYATNSP GIVLVQEVAR
     RARVPLQLFV VKNDSPCGST IGPMLSAKLG VRTLDLGNPQ LSMHSIRETG GSADVESAIR
     LFESFLGHYG ELERKILVD
//
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