ID   A0A1Z9AGD3_9GAMM        Unreviewed;       432 AA.
AC   A0A1Z9AGD3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   03-MAY-2023, entry version 12.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CBC55_11605 {ECO:0000313|EMBL:OUV19498.1};
OS   Gammaproteobacteria bacterium TMED95.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1986771 {ECO:0000313|EMBL:OUV19498.1, ECO:0000313|Proteomes:UP000195745};
RN   [1] {ECO:0000313|EMBL:OUV19498.1, ECO:0000313|Proteomes:UP000195745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED95 {ECO:0000313|EMBL:OUV19498.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) 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:OUV19498.1}.
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DR   EMBL; NHEW01000035; OUV19498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z9AGD3; -.
DR   Proteomes; UP000195745; 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; cd05658; M18_DAP; 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:SF3; ASPARTYL AMINOPEPTIDASE; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   432 AA;  46893 MW;  709A710B35D91BE0 CRC64;
     MTSSLLTQLL DYIKASPTPF HATQITANRL NAAGFKAIDE ASAWTLQKGR YFVTRNDSSI
     IAFNYDPDSL PDTGFKMVGA HTDSPCLKVK PNPVFECKGY QQIAVEVYGG VLLNPWFDRD
     LSLAGKVTYK CLDGQLRSAL IDFEVPVATI PSLAIHLDRE ANNARTVNPQ TDLPPIVAQV
     DFDFHHQLIE QVKRCHPDAQ IETILAFDLS FYDTQAPRLT GLHSDFIASA RLDNLLSCFL
     ALEALIASPQ APNAMIIFND HEEVGSASYA GADGSFLVDV IDRLTPSSES KIRSLAASML
     ISTDNAHGVH PNFSAKHEPR HGPKLNGGPV IKINANQRYA TNSDTHAIFK SLCEDKGIPH
     QVFVTRSDMG CGSTIGPITA SKLGIKTLDV GLPTFGMHSI RELAGAQDAQ HLVDVLTAFY
     QSPGPSIVPG ET
//