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Database: UniProt
Entry: B8BYU3_THAPS
LinkDB: B8BYU3_THAPS
Original site: B8BYU3_THAPS 
ID   B8BYU3_THAPS            Unreviewed;       464 AA.
AC   B8BYU3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   22-NOV-2017, entry version 45.
DE   SubName: Full=Probable aspartyl aminopeptidase {ECO:0000313|EMBL:EED94436.1};
DE            EC=3.4.11.21 {ECO:0000313|EMBL:EED94436.1};
DE   Flags: Fragment;
GN   ORFNames=THAPSDRAFT_32859 {ECO:0000313|EMBL:EED94436.1};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Stramenopiles; Bacillariophyta; Coscinodiscophyceae;
OC   Thalassiosirophycidae; Thalassiosirales; Thalassiosiraceae;
OC   Thalassiosira.
OX   NCBI_TaxID=35128 {ECO:0000313|Proteomes:UP000001449};
RN   [1] {ECO:0000313|EMBL:EED94436.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED94436.1,
RC   ECO:0000313|Proteomes:UP000001449};
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M.,
RA   Brzezinski M.A., Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S.,
RA   Detter J.C., Glavina T., Goodstein D., Hadi M.Z., Hellsten U.,
RA   Hildebrand M., Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N.,
RA   Lau W.W., Lane T.W., Larimer F.W., Lippmeier J.C., Lucas S.,
RA   Medina M., Montsant A., Obornik M., Parker M.S., Palenik B.,
RA   Pazour G.J., Richardson P.M., Rynearson T.A., Saito M.A.,
RA   Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A., Wilkerson F.P.,
RA   Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology,
RT   evolution, and metabolism.";
RL   Science 306:79-86(2004).
RN   [2] {ECO:0000313|EMBL:EED94436.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED94436.1,
RC   ECO:0000313|Proteomes:UP000001449};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E.,
RA   Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M.,
RA   Katinka M., Mock T., Valentin K., Verret F., Berges J.A., Brownlee C.,
RA   Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A.,
RA   Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M.,
RA   Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y.,
RA   Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E.,
RA   Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M.,
RA   McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C.,
RA   Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N.,
RA   Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H.,
RA   Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A.,
RA   von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S.,
RA   Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CM000640; EED94436.1; -; Genomic_DNA.
DR   RefSeq; XP_002289000.1; XM_002288964.1.
DR   ProteinModelPortal; B8BYU3; -.
DR   STRING; 35128.Thaps32859; -.
DR   MEROPS; M18.002; -.
DR   EnsemblProtists; EED94436; EED94436; THAPSDRAFT_32859.
DR   GeneID; 7449571; -.
DR   KEGG; tps:THAPSDRAFT_32859; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   InParanoid; B8BYU3; -.
DR   KO; K01267; -.
DR   Proteomes; UP000001449; Chromosome 3.
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   PANTHER; PTHR28570; PTHR28570; 1.
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   ECO:0000313|EMBL:EED94436.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001449};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EED94436.1};
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:UP000001449};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:EED94436.1}.
SQ   SEQUENCE   464 AA;  50925 MW;  E0F734CB0E0425FA CRC64;
     EFLTQATDPF LAVKTCTEEL DAAGFVKLSK REPFGGVLKP GGSYYYTINH STLVAFTVGA
     KYKAGNGFKI IGGHTDSPYL KVKPISKRAG SGCVQLGVEC YGGGLWHTWF DRDLGISGRV
     LVRTSCPESE QHIVRIPKPV ARISTLCIHL QTAEERGSFK VNKEEHLSPI LGTQSVLERE
     AKLQLNKMGD DDDHWKKNQE PELLKLIASE IGIDTKQIAN FELGLFDCQP ASLGGIKNEF
     LNSARLDNLA TCFVALESIV DYSKSDNVSE DDAISLIALF DHEEIGSQST HGAGSPVMSE
     AVSRITSAFA ENTHSRDPEL HASAVRRSFI FSVDMAHAVH PNYANKHERN HGPRMNAGVV
     IKTNQNQRYA TNGVTGFIAR EVARKTEKNI PLQEFVVRSD CPCGTTIGPI LSANTGIRTV
     DLGMPQLSMH SCREVMGIAD LTNGYNLFKS FFDNFNEIDE CLEG
//
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