ID A0A162QPZ1_9CLOT Unreviewed; 464 AA.
AC A0A162QPZ1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN Name=apeA {ECO:0000313|EMBL:KZL88807.1};
GN ORFNames=CLMAG_59000 {ECO:0000313|EMBL:KZL88807.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL88807.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL88807.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL88807.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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:KZL88807.1}.
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DR EMBL; LWAE01000014; KZL88807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162QPZ1; -.
DR STRING; 1121326.CLMAG_59000; -.
DR PATRIC; fig|1121326.3.peg.5966; -.
DR Proteomes; UP000076603; 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05659; M18_API; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000076603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 464 AA; 52063 MW; B2F61EF4747A99E0 CRC64;
MDLTKKYEYA WNKYSKDDLK GLFDLSERYK DFMSKCKTER ECVLELITRA EKAGYKNIDQ
IIKEKGNLKS GDKVYANNMD KNLALFIIGS KDFEEGLRIL GAHVDSPRLD LKQNPLYEDT
DLALFETHYY GGIKKYQWVT LPLAIHGVIV KKDGKKVNVV IGEDDSDPVV GVSDLLIHLS
GEQMDKKANK VIEGENLNVL IGSMPIEDKD AKDRVRQNIL RLLNDKYGII EEDFISAELQ
VVPAGKARDF GLDRSMIMAY GHDDRICSYT SFEAMMNIEN PDKTCVTLLV DKEEIGSVGA
TGMHSKFFEN VLAELMNLCG NYSELKLRRT LKNSKMLSSD VTAAFDPNFP SVMEKKNSAY
FGKGVVFNKY TGARGKSGSN DANPEYIAEL RRIMDKNNVT WQTSELGKVD QGGGGTIAYI
LAEYGMQVID FGIALHNMHA PWEVASKADI YEAVKGYNAF LSEA
//