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Database: UniProt
Entry: A0A0D7BT95_9AGAR
LinkDB: A0A0D7BT95_9AGAR
Original site: A0A0D7BT95_9AGAR 
ID   A0A0D7BT95_9AGAR        Unreviewed;       469 AA.
AC   A0A0D7BT95;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   23-MAY-2018, entry version 13.
DE   SubName: Full=Peptidase M18, aminopeptidase I {ECO:0000313|EMBL:KIY73647.1};
GN   ORFNames=CYLTODRAFT_439643 {ECO:0000313|EMBL:KIY73647.1};
OS   Cylindrobasidium torrendii FP15055 ss-10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Physalacriaceae;
OC   Cylindrobasidium.
OX   NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY73647.1, ECO:0000313|Proteomes:UP000054007};
RN   [1] {ECO:0000313|EMBL:KIY73647.1, ECO:0000313|Proteomes:UP000054007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY73647.1,
RC   ECO:0000313|Proteomes:UP000054007};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H.,
RA   Haridas S., LaButti K., Ohm R.A., Kues U., Blanchette R.A.,
RA   Grigoriev I.V., Minto R.E., Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by
RT   the genome sequences of Fistulina hepatica and Cylindrobasidium
RT   torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KN880434; KIY73647.1; -; Genomic_DNA.
DR   EnsemblFungi; KIY73647; KIY73647; CYLTODRAFT_439643.
DR   Proteomes; UP000054007; Unassembled WGS sequence.
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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KIY73647.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054007};
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:UP000054007};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   469 AA;  50836 MW;  AAB807E277F41F59 CRC64;
     MTMMLYPNTP EAAKRLLTFL NASPTPFHAV HNASVRLESA GFRKLREAEN WEPILKGGGK
     YYFVRNQAAL IAFTLPQRWK QGAGLSIVAT HVDSPNLRVR PVSKKSKAGY LQVGVETYGG
     GIWHSWLDRD LSLAGRVIVG NNASNFTSKL VKIDRPILRI PTLAIHLDRN VNESFKFNQE
     SEFVPVLGLA AASLNKPAAS NTDEGTKASS IQKNHHSELL ALVAGELSVA PEEIHDFELA
     LYDTQPSVLG GINNEFVFSP RLDNLYSSFC AVDALASLGE TENALPLEGN VNVISLFNHE
     EIGSVSMSGA ESNLIPSLLS RLSPTSETLA ESIAKSFLVS CDMGHAIHPN YASKHEENHA
     PVINGGVIIK TNAKQRYTSD AVTTFLLKQL IEKKGGKVQE FEVRNDMACG STVGPHLSTI
     GLRVVDIGMG MLSMHSIRET AGSDDVQSAI DLFTSLFEGF APLDAQLSA
//
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