ID   F6FTJ8_ISOV2            Unreviewed;       435 AA.
AC   F6FTJ8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Isova_0394 {ECO:0000313|EMBL:AEG43191.1};
OS   Isoptericola variabilis (strain 225).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN   [1] {ECO:0000313|EMBL:AEG43191.1, ECO:0000313|Proteomes:UP000009236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Isoptericola variabilis 225.";
RL   Submitted (MAY-2011) 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}.
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DR   EMBL; CP002810; AEG43191.1; -; Genomic_DNA.
DR   RefSeq; WP_013837586.1; NC_015588.1.
DR   AlphaFoldDB; F6FTJ8; -.
DR   STRING; 743718.Isova_0394; -.
DR   KEGG; iva:Isova_0394; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_11; -.
DR   Proteomes; UP000009236; Chromosome.
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   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:UP000009236};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   435 AA;  44839 MW;  14B3A266A8BE1636 CRC64;
     MPENVAPAPV PDAALAHAED LGAFVTASPS SYHAAAEVAR RAEAAGFTRL DETAAWDVAP
     GGRYVVVRDG AAIAVVVPPS AGPTTPFTVL GTHTDSPGFK LKPRPTTTNG GWVQAGVEVY
     GGPLLNSWLD RELELAGRVV TRDGAEHLVR TGPFARIPQL AIHLDRQVND GLTLDKQRHT
     QPVVGLAESS ADVLEALAAS AEAPVRAADV VGHDVMVADT QPPRAFGAGG TLWASGRLDN
     LLSTHAALVA LLGAAPEDLT GVAVLAAFDH EELGSESRSG AAGPFLEDVL GRVSAALGAG
     DEDRRRAFAS SLCVSSDVGH AVHPNYGERH DPVNRPVAGG GPILKLNANQ RYASDAHGAA
     RWHAACAAAG VPSQEFVSNN AIPCGSTIGP ITATRLGIRV VDVGAAILSM HSARELTAVV
     DPWYLSRAMG AVLVG
//