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Database: UniProt
Entry: A0A109QEG3_9DEIN
LinkDB: A0A109QEG3_9DEIN
Original site: A0A109QEG3_9DEIN 
ID   A0A109QEG3_9DEIN        Unreviewed;       408 AA.
AC   A0A109QEG3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Peptidase M29 {ECO:0000313|EMBL:AMA75531.1};
GN   ORFNames=AV541_05005 {ECO:0000313|EMBL:AMA75531.1};
OS   Thermus parvatiensis.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=456163 {ECO:0000313|EMBL:AMA75531.1, ECO:0000313|Proteomes:UP000061630};
RN   [1] {ECO:0000313|EMBL:AMA75531.1, ECO:0000313|Proteomes:UP000061630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RL {ECO:0000313|EMBL:AMA75531.1,
RC   ECO:0000313|Proteomes:UP000061630};
RA   Tripathi C., Lal R.;
RT   "Genome sequence of Thermus parvatiensis, a thermophile isolated from a hot
RT   water spring.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M29 family.
CC       {ECO:0000256|ARBA:ARBA00008236}.
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DR   EMBL; CP014141; AMA75531.1; -; Genomic_DNA.
DR   RefSeq; WP_060384389.1; NZ_CP014141.1.
DR   AlphaFoldDB; A0A109QEG3; -.
DR   KEGG; tpar:AV541_05005; -.
DR   Proteomes; UP000061630; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   PRINTS; PR00919; THERMOPTASE.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061630}.
SQ   SEQUENCE   408 AA;  45155 MW;  10308BD04692A2E6 CRC64;
     MDAFKRNLEK LAELAIRVGL NLEKGQEVIA TAPIEAVDFV RLLSQKAYEH GASLFTVLYS
     DNVISRQRLS LAPEEGLDRA PGWLYEGMAK AFREGAARLA VSGNDPKALE GLPPERIGRA
     QQAQSRAYKP ALDAITEFVT NWTIVPFAHP GWARAVFPGL PEEEAVRRLW EAIFQATRAD
     QEDPIAAWEA HNRALHEKVA YLNARRFHAL HFKGPGTDLV VGLAEGHLWQ GGATPTKKGL
     LCNPNLPTEE VFTAPHRERV EGVVRASRPL ALGGTLVEGI FARFERGFAV EVRAEKGEEV
     LRRLLDTDEG ARRLGEVALV PADNPIAKTG LVFFDTLFDE NAASHIAFGQ AYQENLEGRP
     SGEAFRKRGG NESLVHVDWM IGSEEMDVDG LYEDGTRVPL MRRGRWVV
//
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