(data stored in ACNUC7421 zone)

SWISSPROT: C7QJB8_CATAD

ID   C7QJB8_CATAD            Unreviewed;       431 AA.
AC   C7QJB8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Caci_0307 {ECO:0000313|EMBL:ACU69260.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69260.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69260.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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; CP001700; ACU69260.1; -; Genomic_DNA.
DR   RefSeq; WP_012784555.1; NC_013131.1.
DR   STRING; 479433.Caci_0307; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ACU69260; ACU69260; Caci_0307.
DR   KEGG; cai:Caci_0307; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; GHAVHPN; -.
DR   OrthoDB; 304020at2; -.
DR   BioCyc; CACI479433:G1GFP-311-MONOMER; -.
DR   Proteomes; UP000000851; 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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
DR   PRODOM; C7QJB8.
DR   SWISS-2DPAGE; C7QJB8.
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACU69260.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACU69260.1};
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:UP000000851};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   431 AA;  44934 MW;  8221827D9F432D67 CRC64;
     MPIFDRAHTD DLLAFLAASP TPYHAVTNAA ARLEAAGFRQ LRQSAGWESA DGGGFYAIRG
     AAIIAWYLPE GAAAPTGFRV VGAHTDSPNL RVKPLPDTGS AGFRQVAVEL YGGPLLNSWL
     DRDLGLAGRL VLRGGEAALV HVDRALMRVP QLAVHLDRGV NDSGLLLDKQ QHLTPAWGLG
     PVEDGALIEF AAKEAGVSAS DVMGFDLMLH DVTPPTYLGR DQEMIAAPRM DNLVSVHAGV
     QALIAAASGA GGPLTAIPVL AAFDHEETGS ESDTGAGGPL LGTILSRVTQ AQLGGSADDY
     ARALAATVVM SSDMSHAVHP NYPERHEPGH RPRLNGGPAL KTNVNQRYAT DGLGRAIWTD
     VCERAGIPTQ YFVGKNSLPC GTTIGPITAA KLGVTTFDVG ITSLSMHSAR EMGGADDPFL
     LASAAASFFA G
//

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