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Database: UniProt
Entry: A0A139DQM8_9DELT
LinkDB: A0A139DQM8_9DELT
Original site: A0A139DQM8_9DELT 
ID   A0A139DQM8_9DELT        Unreviewed;       477 AA.
AC   A0A139DQM8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   12-APR-2017, entry version 4.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=AMR96_06650 {ECO:0000313|EMBL:KXS55730.1};
OS   Candidatus Adiutrix intracellularis.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Candidatus Adiutrix.
OX   NCBI_TaxID=1705730 {ECO:0000313|EMBL:KXS55730.1, ECO:0000313|Proteomes:UP000070156};
RN   [1] {ECO:0000313|EMBL:KXS55730.1, ECO:0000313|Proteomes:UP000070156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Adiu1 {ECO:0000313|EMBL:KXS55730.1};
RX   PubMed=26914459;
RA   Ikeda-Ohtsubo W., Strassert J.F., Kohler T., Mikaelyan A., Gregor I.,
RA   McHardy A.C., Tringe S.G., Hugenholtz P., Radek R., Brune A.;
RT   "'Candidatus Adiutrix intracellularis', an endosymbiont of termite gut
RT   flagellates, is the first representative of a deep-branching clade of
RT   Deltaproteobacteria and a putative homoacetogen.";
RL   Environ. Microbiol. 0:0-0(2016).
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:KXS55730.1}.
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DR   EMBL; LQAA01000145; KXS55730.1; -; Genomic_DNA.
DR   Proteomes; UP000070156; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070156};
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:UP000070156};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   477 AA;  52279 MW;  009763D0E48A4EF7 CRC64;
     MALSRKEERD DLKKLANKLV IKSNLIWDEM TPIDRQAAER LAADYLSFLT ASKTERAVVK
     NIRQILTGHG FVDLNQKKRA PGGGFLIHHE KLIGFFRPGR LSPEDGFNLI VAHGDSPRLD
     LKPKCVYEES GPGFGMLRTN LYGGLKKFQW LARPLALWGF CALKGGRTVE IIFGEEPDDP
     VLTIPDLLPH LDRKVQRDKK IGEAIVADKM NLLAVSIPLG RPRDKDRFKL AVLKILYDRW
     GLVEEDLVSS EIEIVPAGPA RSVGFDASLL GGYGQDDRLP VFATLAAVAE VKKPDRPTLV
     IIYDREEIGS YGSVGASGNF IEHLAARAFE AVGLDVHWSK VREALLKTQA LSADVEAGVD
     PDYKEVHEEL NSAHIGRGPC LVRYTGGTGK YGASEASAEY VSRVRSAFAK AGVLWQSAIL
     GKQEEGGGGT VALYLAAYGL NIVDCGPPVI SMHSPFEISS KADLWMTVRA YAAFLKM
//
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