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Database: UniProt
Entry: F9VIK9_ARTSS
LinkDB: F9VIK9_ARTSS
Original site: F9VIK9_ARTSS 
ID   F9VIK9_ARTSS            Unreviewed;       465 AA.
AC   F9VIK9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   22-NOV-2017, entry version 32.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=SFBM_0342 {ECO:0000313|EMBL:BAK56121.1};
OS   Arthromitus sp. (strain SFB-mouse-Japan).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Candidatus Arthromitus.
OX   NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK56121.1, ECO:0000313|Proteomes:UP000001636};
RN   [1] {ECO:0000313|EMBL:BAK56121.1, ECO:0000313|Proteomes:UP000001636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX   PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA   Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA   Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA   Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT   "The lifestyle of the segmented filamentous bacterium: a non-
RT   culturable gut-associated immunostimulating microbe inferred by whole-
RT   genome sequencing.";
RL   DNA Res. 18:291-303(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}.
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DR   EMBL; AP012202; BAK56121.1; -; Genomic_DNA.
DR   RefSeq; WP_005807041.1; NC_015913.1.
DR   STRING; 1029718.SFBM_0342; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; BAK56121; BAK56121; SFBM_0342.
DR   KEGG; asf:SFBM_0342; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000001636; Chromosome.
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:BAK56121.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001636};
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:UP000001636};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   465 AA;  52289 MW;  6306AD959B45DCA8 CRC64;
     MGDKTLSKIA WENYSEENLL ELEDLCSKYK DFLSKNKTER ECVNYFINEA VKHNFKDLRE
     VIKNREKLNK GDRVYYSKMD KTLILAVIGD ESLENGFNII GSHIDAPRID IKQSPVYESD
     GLCYFDTHYY GGIKKYHWVA RPMCLKGVVI KSNGDKVVIN IGDDDNDPYL GFSDLLPHLW
     KDQAMKKGVD VIEGEQLNLL VGSRSLDGKK DKVKKLILSI LSEKYGICEE DLISAELEVV
     PAGPAKDYGL DRSMIIGYGQ DDRVCAFTSF MSMLKMDGIP KRTSICMLVD KEEIGSTGAT
     GMESKLFENF SAELLNSCRD NYSEIVLKRS LDRSYMLSAD VTCAYDPNFP NETPKQSTAF
     FGKGVTISKY TGSRGKSGCN DANPEFLAKL RDIFNREGIC YQVGELGKVD QGGGGTIAYF
     LSRYGMEVVD IGVPLQNMHA PFEVSSKADI YETYKAYGTF YKYLV
//
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