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Database: UniProt
Entry: A0A017T7R0_9DELT
LinkDB: A0A017T7R0_9DELT
Original site: A0A017T7R0_9DELT 
ID   A0A017T7R0_9DELT        Unreviewed;       498 AA.
AC   A0A017T7R0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   28-FEB-2018, entry version 13.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CAP_3449 {ECO:0000313|EMBL:EYF05308.1};
OS   Chondromyces apiculatus DSM 436.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Polyangiaceae; Chondromyces.
OX   NCBI_TaxID=1192034 {ECO:0000313|EMBL:EYF05308.1, ECO:0000313|Proteomes:UP000019678};
RN   [1] {ECO:0000313|EMBL:EYF05308.1, ECO:0000313|Proteomes:UP000019678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 436 {ECO:0000313|EMBL:EYF05308.1,
RC   ECO:0000313|Proteomes:UP000019678};
RA   Sharma G., Khatri I., Kaur C., Mayilraj S., Subramanian S.;
RT   "Genome assembly of Chondromyces apiculatus DSM 436.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:EYF05308.1}.
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DR   EMBL; ASRX01000025; EYF05308.1; -; Genomic_DNA.
DR   EnsemblBacteria; EYF05308; EYF05308; CAP_3449.
DR   Proteomes; UP000019678; 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   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;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EYF05308.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019678};
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:UP000019678};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   498 AA;  53131 MW;  A65E0EA9AE167B92 CRC64;
     MRAASVAQPP EVRGEGLCYA RRAMETKETK ATKDAGEAGA GSQGEDAGSP SKLLGERFPK
     TAEELRALRA LGVTAARDLC GFIDRSPTPW HATREVAARL AEHGFTELGE REAWTLAPGD
     KRFVIRNGSS IVAFVAGAEH PAQGGFRLIG SHTDSPNLRL KPHADFVKSG YQQVGVEVYG
     GVLYSTWLDR DLSIAGRVMV RRRDGALESR LFDVRRAVAR VPNLAIHLNR GVNSEGLVLN
     AQKHLVPVLG LGKESELSGL LARELDVGSE AIVGYDLCLY DVVPAAVGGV SDELIFAGRL
     DNLASCHAST QALIAASHAP AAATRGIVLY DHEEVGSRSA TGAVGTLLRD TLTRIVEAWR
     GREEPQGLRR ALAGSLLISA DMAHAVHPNY ADHHEPRHAP QLNRGLVIKS NANQSYATDG
     VTAAQFTEFC GEVGFAPQRF VVRSDLPCGS TIGPITAAEL GIATIDVGAP MLSMHSCREM
     AGTLDVHLAI ETYRRALG
//
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