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Database: UniProt
Entry: F3LDD5_9GAMM
LinkDB: F3LDD5_9GAMM
Original site: F3LDD5_9GAMM 
ID   F3LDD5_9GAMM            Unreviewed;       443 AA.
AC   F3LDD5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   22-NOV-2017, entry version 30.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=IMCC1989_1828 {ECO:0000313|EMBL:EGG95091.1};
OS   gamma proteobacterium IMCC1989.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales.
OX   NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG95091.1, ECO:0000313|Proteomes:UP000010300};
RN   [1] {ECO:0000313|EMBL:EGG95091.1, ECO:0000313|Proteomes:UP000010300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG95091.1,
RC   ECO:0000313|Proteomes:UP000010300};
RX   PubMed=21602334; DOI=10.1128/JB.05202-11;
RA   Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT   "Genome sequence of strain IMCC1989, a novel member of the marine
RT   gammaproteobacteria.";
RL   J. Bacteriol. 193:3672-3673(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGG95091.1}.
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DR   EMBL; AEVK01000035; EGG95091.1; -; Genomic_DNA.
DR   RefSeq; WP_009668853.1; NZ_AEVK01000035.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EGG95091; EGG95091; IMCC1989_1828.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000010300; 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:EGG95091.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010300};
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:UP000010300};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   443 AA;  49120 MW;  0E66C05465CCCF5C CRC64;
     MVETTQVVNE GTSKELSDQE VFNQGLLDFI DASPTPFHAT QTMAQQLLAA GFVELLEGEQ
     WALENGKKYF VTRNFSSLIA FVYSPDLFVN EGIRMMGAHT DSPCLRVKPN PEKTAQGYFQ
     LGVEVYGGAL LSTWFDRDLS LAGRVNYLDK QQQLRSSLVN FKDPIAVIPS LAIHLNREAN
     EANNINKQKH LPPILMQVKD KKNIDFKDWL HAQLELQGET DVAKVMDYEL SFYDTQPSAI
     IGLQKEFIAA SRLDNLLSCY VGLQSLINAD SDKPALLICT DHEEVGSASA CGAQGPMLEH
     CLQRMIPDTE QRLRAIDRSL MISVDNAHGI HPNYADKHDE NHGPLLNKGA VIKINSNQRY
     ATNSETSSFF RQLCDSNNVT PQVFVTRSDM GCGSTIGPIT ASEVGVKTID VGVPTFAMHS
     IRELAGTQDA FDLSRVLTSF FQQ
//
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