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Database: UniProt
Entry: K5V987_PHACS
LinkDB: K5V987_PHACS
Original site: K5V987_PHACS 
ID   K5V987_PHACS            Unreviewed;       469 AA.
AC   K5V987;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   07-JUN-2017, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKM59371.1};
DE   Flags: Fragment;
GN   ORFNames=PHACADRAFT_249819 {ECO:0000313|EMBL:EKM59371.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus)
OS   (Peniophora carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM59371.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM59371.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM59371.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa
RT   and P. chrysosporium, to elucidate the genetic basis of the distinct
RT   wood types they colonize.";
RL   BMC Genomics 13:444-444(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; JH930469; EKM59371.1; -; Genomic_DNA.
DR   RefSeq; XP_007391934.1; XM_007391872.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EKM59371; EKM59371; PHACADRAFT_249819.
DR   GeneID; 18914758; -.
DR   KEGG; pco:PHACADRAFT_249819; -.
DR   InParanoid; K5V987; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
DR   InterPro; IPR001948; Peptidase_M18.
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:UP000008370};
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:UP000008370};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:EKM59371.1}.
SQ   SEQUENCE   469 AA;  51315 MW;  A251643E6BF23BEA CRC64;
     MTMIAQAGPE AASRLISFVN ASPTPFHAVR TAVTRLEQAG FRKLREVDGW DDDLKPGGKY
     YFTRNQSALL AFTLPQKWEP GVGVSIIATH VDSPNLRVRP VSKKAKLGYL QVGVETYGGG
     IWHSWFDRDL SLAGRIVITD KKGGFTSKLV KIDRPLLRIP TLAIHLDRSV NDGFKFNKET
     ELVPIAGLVE EQLNTEKEKS ADKKSGASSI QDNHHSALLA VLSEELSVTP EEIHDFELHL
     YDVQPASLAG LNNEFIFASR LDNQFSSFAA VEAIVDHASI ESFPTFEGNV NCIALFNHEE
     IGSVSSSGAA SSLIPTLLER LSPTPQSWAR SIARSFLVSS DVSHAIHPNY SSKHEENHAP
     RMNGGVVIKT NEGQRYATDS ISSFVVKKLV EKTGGKIQNF EVRNDMPCGS TVGPMLSKIG
     IRTVDVGCGI LSMHSIREQA GAQDVQSLID LFSSLFEGFA ELDRELTVD
//
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