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Database: UniProt
Entry: A0A0C9ZMA3_9HOMO
LinkDB: A0A0C9ZMA3_9HOMO
Original site: A0A0C9ZMA3_9HOMO 
ID   A0A0C9ZMA3_9HOMO        Unreviewed;       459 AA.
AC   A0A0C9ZMA3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   23-MAY-2018, entry version 13.
DE   SubName: Full=Unplaced genomic scaffold scaffold_2, whole genome shotgun sequence {ECO:0000313|EMBL:KIK30586.1};
GN   ORFNames=PISMIDRAFT_301057 {ECO:0000313|EMBL:KIK30586.1};
OS   Pisolithus microcarpus 441.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Sclerodermatineae;
OC   Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK30586.1, ECO:0000313|Proteomes:UP000054018};
RN   [1] {ECO:0000313|EMBL:KIK30586.1, ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|EMBL:KIK30586.1,
RC   ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KN833686; KIK30586.1; -; Genomic_DNA.
DR   EnsemblFungi; KIK30586; KIK30586; PISMIDRAFT_301057.
DR   Proteomes; UP000054018; 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   Complete proteome {ECO:0000313|Proteomes:UP000054018};
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:UP000054018};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   459 AA;  50774 MW;  2562A5261126D719 CRC64;
     MSIYPEAAKR LLAFINASPT PFHAVQNAAI RLEAAGFSKI RETDDWDLQP RSKYYYTRNQ
     TCLIAFTTPS NWRPGTGVSI VATHVDSPNL RVRPVSKKSN LGYLQVGIET YGGGIWHSWF
     DRDLSLAGRV IVVQRDGTFR SKLVKIDRPL LRIPSLAIHL DRNVNDSFKF NQESEFTPIF
     GLVESELNDV KVQGASAPSG QMKHHPALLL VLSEELSVAP EEIRDFELHL YDTQPSVLGG
     VNNEFIFSPR LDNQFSSYCA VEAIATYAEN PSFMEFVGNV NCVALFNHEE IGSVSTTGAE
     SSLIPSLLQR LSPEPASYSQ SVSRSFLVSA DMGHAVHPNY SSKHEENHRP IINGGMVIKT
     NAKQRYASDA ISTFLFRKLV EQRGGKVQEF EVRNDMACGS TVGPMLSKIG LRTVDVGNAM
     LSMHSIRETG GSHDVQHAVD AFSSFFDGFS KLDGDLLID
//
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