(data stored in ACNUC7421 zone)

SWISSPROT: A8FPI5_SHESH

ID   A8FPI5_SHESH            Unreviewed;       679 AA.
AC   A8FPI5;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   SubName: Full=Oligopeptidase A {ECO:0000313|EMBL:ABV34758.1};
DE            EC=3.4.24.70 {ECO:0000313|EMBL:ABV34758.1};
GN   OrderedLocusNames=Ssed_0145 {ECO:0000313|EMBL:ABV34758.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34758.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34758.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34758.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP000821; ABV34758.1; -; Genomic_DNA.
DR   RefSeq; WP_012004284.1; NC_009831.1.
DR   STRING; 425104.Ssed_0145; -.
DR   MEROPS; M03.004; -.
DR   EnsemblBacteria; ABV34758; ABV34758; Ssed_0145.
DR   KEGG; sse:Ssed_0145; -.
DR   eggNOG; ENOG4105DGW; Bacteria.
DR   eggNOG; COG0339; LUCA.
DR   HOGENOM; HOG000245986; -.
DR   KO; K01414; -.
DR   OMA; KNFQSAM; -.
DR   OrthoDB; 1935578at2; -.
DR   BioCyc; SSED425104:G1G9Y-154-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   Pfam; PF01432; Peptidase_M3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPI5.
DR   SWISS-2DPAGE; A8FPI5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Hydrolase {ECO:0000256|RuleBase:RU003435,
KW   ECO:0000313|EMBL:ABV34758.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN      222    676       Peptidase_M3. {ECO:0000259|Pfam:PF01432}.
SQ   SEQUENCE   679 AA;  76904 MW;  1E07ABFBEEDA1EC3 CRC64;
     MSNPLLTSAV LPPFSKIKPE HIQDAVEQGI ANCRSQIEKV LAQPQPFTWN NLIAPLEEVD
     DELSKIWSPI SHMNSVVSSE EWRQAHDACL PLLSEYGTFV GQHQPLYQAY KSIKASDEFE
     QLTQAQKMVI EHSLRDFELS GIGLNDADKL RYGELVKRMS ELTSGFSNQL LDATQAWTKL
     ITDEDELAGL PESAIAAAKA MAAAKEQEGW LFTLDFPSYL PVMTYSENRN LREECYRAFV
     TRASDQGPFA GKYDNGPLMD EIVALRHELA LLLGFDSYAH KSLATKMAQT PQQVLEFLNE
     LASRSKDQGK TELAELTEFA GKEFGATDLS PWDLSFYAEK LKHHRYEISQ ELLRPYFPED
     KVLSGLFYTV NRLFGLKITE QKEFDSWHKD VRFFSIEDSE GEHRGSFYFD LYAREGKRGG
     AWMDDCRVRR QTISGMQNPV AYLTCNFNAP VDGKPALFTH DEVTTLFHEF GHGIHHMLTK
     IDVAGVSGIN GVPWDAVELP SQFMENWCFE EEALAEISGH FETGEPLPKV MLDKMLAAKN
     FQSGMGMLRQ LEFSLFDFRM HLEYSPEKGA NIQAKLDEVR SQVAVITAAD FNRFQHSFAH
     IFAGGYAAGY YSYKWAEVLS ADAFSRFEEE GIFNSETGLS FLNNILEMGG SEEPMELFKR
     FRGREPRIDA LLRHSGING
//

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