(data stored in SCRATCH zone)

SWISSPROT: B4STC3_STRM5

ID   B4STC3_STRM5            Unreviewed;       455 AA.
AC   B4STC3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:ACF49966.1};
DE            EC=3.4.11.1 {ECO:0000313|EMBL:ACF49966.1};
GN   OrderedLocusNames=Smal_0261 {ECO:0000313|EMBL:ACF49966.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49966.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49966.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49966.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|SAAS:SAAS00754360}.
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DR   EMBL; CP001111; ACF49966.1; -; Genomic_DNA.
DR   RefSeq; WP_012509797.1; NC_011071.1.
DR   STRING; 391008.Smal_0261; -.
DR   MEROPS; M17.004; -.
DR   EnsemblBacteria; ACF49966; ACF49966; Smal_0261.
DR   KEGG; smt:Smal_0261; -.
DR   eggNOG; ENOG4105BZ6; Bacteria.
DR   eggNOG; COG0260; LUCA.
DR   HOGENOM; HOG000243129; -.
DR   KO; K01255; -.
DR   OMA; HFDIYGW; -.
DR   OrthoDB; 356206at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01325-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   CDD; cd00433; Peptidase_M17; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   PANTHER; PTHR11963; PTHR11963; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4STC3.
DR   SWISS-2DPAGE; B4STC3.
KW   Aminopeptidase {ECO:0000256|SAAS:SAAS00754331,
KW   ECO:0000313|EMBL:ACF49966.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00754382,
KW   ECO:0000313|EMBL:ACF49966.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00754373};
KW   Protease {ECO:0000256|SAAS:SAAS00754389}.
FT   DOMAIN      304    311       CYTOSOL_AP. {ECO:0000259|PROSITE:
FT                                PS00631}.
SQ   SEQUENCE   455 AA;  48547 MW;  5A866909C7E925E5 CRC64;
     MSEITGFTAD TAAALPLHVL GREQFAAWKD GQPAATQAWL ASQGFNAGAH SVALLPGADG
     LAGAVIGVGD RADAYSYAHA PHALPEGSVW QLATELPAEE QALLQLGWGL GSYRFDRYRK
     RNRAPAQLVA APSGEVADLI AASLRVRDWV NTPTEDMGPQ QLEDAARALA QAHGAQVEAI
     TGDELLKQNF PAIHAVGRAS HRAPRMVVLR WGKETDPALV LVGKGVCFDT GGLDIKPADG
     MRNMKKDMGG AAHALALAGL VMARRLPVHL TLLVPAVENA IGPDAFRPGE VIATRKGLSV
     EIDNTDAEGR VILCDALTFA SEQKPDLVLD FATLTGAARI ALGPDLPALF SNDDAVAQQW
     LQAGDATRDP VWRMPLWRPY LRYLSSGIAD LANAGSRMAG SVTAALYLER FLEDGQRWAH
     LDVYAWNDGE RPGRPAGGEA LALRSAWAML KARYS
//

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