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Database: UniProt
Entry: T0PM91_9STRA
LinkDB: T0PM91_9STRA
Original site: T0PM91_9STRA 
ID   T0PM91_9STRA            Unreviewed;       470 AA.
AC   T0PM91;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-NOV-2017, entry version 15.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EQC26479.1};
GN   ORFNames=SDRG_15657 {ECO:0000313|EMBL:EQC26479.1};
OS   Saprolegnia diclina VS20.
OC   Eukaryota; Stramenopiles; Oomycetes; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC26479.1, ECO:0000313|Proteomes:UP000030762};
RN   [1] {ECO:0000313|EMBL:EQC26479.1, ECO:0000313|Proteomes:UP000030762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VS20 {ECO:0000313|EMBL:EQC26479.1,
RC   ECO:0000313|Proteomes:UP000030762};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA   de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Saprolegnia declina VS20.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; JH767229; EQC26479.1; -; Genomic_DNA.
DR   RefSeq; XP_008620058.1; XM_008621836.1.
DR   EnsemblProtists; EQC26479; EQC26479; SDRG_15657.
DR   GeneID; 19956384; -.
DR   EuPathDB; FungiDB:SDRG_15657; -.
DR   Proteomes; UP000030762; 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   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:EQC26479.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030762};
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:UP000030762};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   470 AA;  51009 MW;  7A726A2E8B4DBAB9 CRC64;
     MSLVPNAKLS ATAKQTGQAL INFIDKAPSA FHAVYETVQS LKAHGFSQLR EDENWDDAIQ
     PNGKYYVTRN QSAVVAFAVG GNYAKGNGFH IVGAHSDSPC LKIKPVSKVE SQGSLQVGVE
     TYGGGLWNTW FDRDLGVAGR VFVKDAETSQ IAGRLVLINR PIMRIPMLAI HLQDAETRKA
     FSFNNENHLR PVLATSVMAE LTRPKTDADA GAKHHPILLD LLAKELDVTV DQIFDFELSL
     FDTQGGAIGG LLEEYVFAPR LDNLCCTWLA TQSLLKSLPT LETESNVRVA ASFDNEEVGS
     NSLMGAGSNF LQSIITRVSG GSLTGEVARK SMLISADMAH GVHPNYSEKH EVNSRIQMHS
     GPVIKYNANE RYATSGETAL LIKELGRRHG LDIQDFVSRQ DCGCGSTIGP ILATSTGIRT
     VDMGLAQFSM HSIREQCGTV DLELAIELFS AFYNDFVEID GSIATDSLLG
//
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