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Database: UniProt
Entry: M1WCM9_CLAP2
LinkDB: M1WCM9_CLAP2
Original site: M1WCM9_CLAP2 
ID   M1WCM9_CLAP2            Unreviewed;       487 AA.
AC   M1WCM9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   28-FEB-2018, entry version 19.
DE   SubName: Full=Probable aspartyl aminopeptidase {ECO:0000313|EMBL:CCE31713.1};
GN   ORFNames=CPUR_05567 {ECO:0000313|EMBL:CCE31713.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE31713.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE31713.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE31713.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K.,
RA   Calie P.J., Fleetwood D.J., Haws D.C., Moore N., Oeser B.,
RA   Panaccione D.G., Schweri K.K., Voisey C.R., Farman M.L.,
RA   Jaromczyk J.W., Roe B.A., O'Sullivan D.M., Scott B., Tudzynski P.,
RA   An Z., Arnaoudova E.G., Bullock C.T., Charlton N.D., Chen L., Cox M.,
RA   Dinkins R.D., Florea S., Glenn A.E., Gordon A., Gueldener U.,
RA   Harris D.R., Hollin W., Jaromczyk J., Johnson R.D., Khan A.K.,
RA   Leistner E., Leuchtmann A., Li C., Liu J., Liu J., Liu M., Mace W.,
RA   Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K., Steiner U.,
RA   Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of
RT   the Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCE31713.1}.
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DR   EMBL; CAGA01000033; CCE31713.1; -; Genomic_DNA.
DR   EnsemblFungi; CCE31713; CCE31713; CPUR_05567.
DR   OrthoDB; EOG092C3JCE; -.
DR   PhylomeDB; M1WCM9; -.
DR   Proteomes; UP000016801; 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:CCE31713.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016801};
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:UP000016801};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   487 AA;  53103 MW;  35F9D2CCBE7FC42E CRC64;
     MAPPKAALDF VDFVNDSPTP YHATQTAAHR LENAGFQRIK ERDSWTSTLQ PGGKYYLTRN
     GSSIVAFAIG RKWCPGNAIG IVGAHTDSCC LRLKPVSKKT NAGYLQVGVE AYGGGIWHSW
     FDRDLSIAGR VLVTEGDKVV QKLVKIEKPL LRIPTLAIHL HRQTNFDPNK ESELFPIIGL
     ATAELNKSAD QDAAAAEKKT EEEVSEPLEK MSERHHPAVL DVIAEELHVK VADIMDFELV
     LYDTQKSVVG GLKDELIFSA RLDNLGMTYC SVEGLIASVQ NDNTSSLDQD STIRMIACFD
     HEEIGSTSAQ GAESNLLPSV IHRLASIPAS SSSDSQHNNE SSTAYEQTLS RSFLISADMA
     HAVHPNYTGK YESSHQPALN KGTVIKVNAN QRYATNSPGI VLIQQCASIA RVPLQLFVVR
     NDSPCGSTIG PGLAAKLGMR TLDLGNPQLS MHSIRETSGS ADVEFATKLF EAFFRHYGEL
     ESKIVVD
//
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