ID   A0A255TFA0_9BACT        Unreviewed;       428 AA.
AC   A0A255TFA0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CIL02_01090 {ECO:0000313|EMBL:OYP63657.1};
OS   Prevotella sp. P3-122.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2024223 {ECO:0000313|EMBL:OYP63657.1, ECO:0000313|Proteomes:UP000215645};
RN   [1] {ECO:0000313|EMBL:OYP63657.1, ECO:0000313|Proteomes:UP000215645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P3-122 {ECO:0000313|EMBL:OYP63657.1,
RC   ECO:0000313|Proteomes:UP000215645};
RA   Accetto T., Nograsek B., Avgustin G.;
RT   "Comparative genomics of non-oral Prevotella species.";
RL   Submitted (AUG-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:OYP63657.1}.
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DR   EMBL; NPJH01000006; OYP63657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255TFA0; -.
DR   OrthoDB; 9764268at2; -.
DR   Proteomes; UP000215645; 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   Reference proteome {ECO:0000313|Proteomes:UP000215645};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   428 AA;  46601 MW;  5F01A25D96A9D8AE CRC64;
     MINRLLQFLD ASPVNFLAVR NIVAELEQSG YTRFDASESL TDIQPGSKFF VTKNDSSVYA
     FRIGSKPLAE AGFRMICAHC DSPTFRIKPN AEMLCEGGIV KLNTEVYGGP IMSTWFDRPL
     TLAGRVITRG DSPMEPRTLL MHVRRPLLQI SNLAIHFNRQ VNDGVKLSRQ KDMLPLLGMV
     TDQLEKGNML IGVICDELGI SKEEILDFDL YLADATPACL FGVHDEFISS GRLDDLSMCY
     AGLEALTGTP DGEVTSVLAI FDNEETGSQT KQGAGSPFLS SLLRRIALAQ GGGEEAYWRS
     VEKAFMVSAD NAHAWHPNYS EKYDPTNHPV LGGGPVIKFN AAQKYASDAV SAAVFSEICR
     KAGVPCQRFV NHSDVAGGST LGNILASSIP LRGVDMGNAI LAMHSCRETG SVADHEFCVK
     AFKTFLSE
//