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Database: UniProt
Entry: A9T427_PHYPA
LinkDB: A9T427_PHYPA
Original site: A9T427_PHYPA 
ID   A9T427_PHYPA            Unreviewed;       486 AA.
AC   A9T427;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   25-OCT-2017, entry version 49.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ61735.1};
GN   ORFNames=PHYPADRAFT_191408 {ECO:0000313|EMBL:EDQ61735.1};
OS   Physcomitrella patens subsp. patens (Moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727};
RN   [1] {ECO:0000313|EMBL:EDQ61735.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y.,
RA   Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T.,
RA   Kuroki Y., Toyoda A., Suzuki Y., Hashimoto S.-I., Yamaguchi K.,
RA   Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N.,
RA   Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H.,
RA   Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K.,
RA   Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A.,
RA   Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T.,
RA   Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H.,
RA   Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J.,
RA   Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the
RT   conquest of land by plants.";
RL   Science 319:64-69(2008).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; DS545051; EDQ61735.1; -; Genomic_DNA.
DR   RefSeq; XP_001773362.1; XM_001773310.1.
DR   UniGene; Ppa.11999; -.
DR   ProteinModelPortal; A9T427; -.
DR   STRING; 3218.PP1S162_1V6.1; -.
DR   GeneID; 5936570; -.
DR   KEGG; ppp:PHYPADRAFT_191408; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   InParanoid; A9T427; -.
DR   KO; K01267; -.
DR   Proteomes; UP000006727; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
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:UP000006727};
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:UP000006727};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   486 AA;  53396 MW;  4CF8885400F547FC CRC64;
     MCREAQSNII PHLLEYVDNS CTPFHATAEA RKFLLTAGFQ EISECEEWAL QPGGRYFFTR
     NMCSIYAFAI GHKYKPGSGF HVIAAHTDSP CPKLKPVSYS AKGGFVHVRV QPYGAGVWQT
     WFDRDLSVAG RVLLRRKDGD LVNELVRVGR PILRIPTVAN PVDRGLAADG SKVDAEVNLA
     PVLAMQIESE LAMSCDSESS MPVEHNDHGS HIYPQPATAH HPLLIQVLAD ALKCDVSEVA
     DFDLSVYDTQ PACVGGARDD FVFAGRLDNL TSTFCALWAL LHTCADPSSL VDESCVRMIA
     LFDSGEVGGP DSAQAAGPQI MLQAMTRIAR WLARGSDSEG VVERAMRRSL IVSADMVEGM
     YPIQVSSPGQ EESFHHPKLR DGLVLRQDAS NANDIVTSFL FREVAKRSSI PVQNFPVSRE
     TGCCSTVSSI LAAGYGLRLI DCGVPLLSMH SVREMCSTDD IETTFRHFRE FFQHFTAIDE
     QLRVDV
//
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