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Database: UniProt
Entry: A9RD26_PHYPA
LinkDB: A9RD26_PHYPA
Original site: A9RD26_PHYPA 
ID   A9RD26_PHYPA            Unreviewed;       471 AA.
AC   A9RD26;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ83200.1};
DE   Flags: Fragment;
GN   ORFNames=PHYPADRAFT_111408 {ECO:0000313|EMBL:EDQ83200.1};
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:EDQ83200.1, 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; DS544891; EDQ83200.1; -; Genomic_DNA.
DR   RefSeq; XP_001751765.1; XM_001751713.1.
DR   UniGene; Ppa.488; -.
DR   ProteinModelPortal; A9RD26; -.
DR   STRING; 3218.PP1S2_377V6.1; -.
DR   MEROPS; M18.A02; -.
DR   GeneID; 5914949; -.
DR   KEGG; ppp:PHYPADRAFT_111408; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   InParanoid; A9RD26; -.
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   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: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}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:EDQ83200.1}.
SQ   SEQUENCE   471 AA;  51674 MW;  9E27D865DD137849 CRC64;
     SIVTDMLNFL NESWTPFHAT AEAKRQLLKA GFQQLNEEQE WTVQPGGRYF FTRNMSSIFA
     FAIGQKYEAG NGFNIVAAHT DSPCPKLKPV SAASKAGFLN VGVQTYGGGL WHTWFDRDLS
     VAGRVLLRKK NGTIVQGLIK VDRPIMRIPT LAIHLDRTVN TDGFKPNLET HLAPVLATQI
     KAELLGKSET GGQSEGGNGA INSSKKPHHS LLLEVLAEQL NCSVEEIVDF ELNVCDTQPS
     CVGGARKEFI FSGRLDNLAS SYCALRALLD TCPDSASLAD ESCIRAIALF DNEEVGSDSA
     QGAGSPVMFQ AMSRITKWLT RDTPTEGIEE RTIRKSFLVS ADMAHALHPN YADRHEENHQ
     PKLHEGLVIK YNANQRYATN TVTAFLFKEV AKVAGVPTQN FVVRNDMGCG STIGPILASG
     IGIRTVDVGM PQLSMHSVRE MCGTEDVDLS YRHFKAFYEL FTTIDKLTVD S
//
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