ID   A0A2T5BDY3_MYCDI        Unreviewed;       416 AA.
AC   A0A2T5BDY3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Aminopeptidase T {ECO:0000313|EMBL:PTM97205.1};
GN   ORFNames=C7449_10273 {ECO:0000313|EMBL:PTM97205.1};
OS   Mycoplana dimorpha.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Mycoplana.
OX   NCBI_TaxID=28320 {ECO:0000313|EMBL:PTM97205.1, ECO:0000313|Proteomes:UP000241247};
RN   [1] {ECO:0000313|EMBL:PTM97205.1, ECO:0000313|Proteomes:UP000241247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7138 {ECO:0000313|EMBL:PTM97205.1,
RC   ECO:0000313|Proteomes:UP000241247};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PTM97205.1}.
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DR   EMBL; PZZZ01000002; PTM97205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T5BDY3; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000241247; Unassembled WGS sequence.
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   ECO:0000313|EMBL:PTM97205.1}; 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:UP000241247}.
SQ   SEQUENCE   416 AA;  44386 MW;  89ED1A3C3E06F4B7 CRC64;
     MNAPPASAPV DPVRLDKLAQ VAVHVGLQLQ KGQDLVMTAP IAALPLARLI TKHAYMAGAG
     LVSTFYADEE ATLARYRHAP DESFDRATDW LYEGMAKAYA NGAARLAIAG DNPMLLSGED
     PAKVARANKA NSKAYKPALE KIANFDINWN IVSYPNPSWA KQVFPNDAED VAVEKLANAI
     FAASRVDCDD PVGAWQAHNA GLHRRSAWLN GQRFAALHFK GPGTDLTVGL ADGHEWHGGA
     SVAKNGVTCN PNIPTEEVFT TPHALRVEGH VASTKPLSHL GTLIDDIRVR FEGGRIVEAH
     ASRGEAVLNK VLDTDEGARR LGEVALVPHS SPISASGLLF YNTLFDENAA CHIALGQCYS
     KCFLDGASLT PEQIKAQGGN SSLIHIDWMI GSGQIDIDGV AADGGRVPVM RAGEWA
//