ID K6VPY2_9MICO Unreviewed; 447 AA.
AC K6VPY2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=KILIM_120_00030 {ECO:0000313|EMBL:GAB98268.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB98268.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB98268.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB98268.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-2012) 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:GAB98268.1}.
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DR EMBL; BAHD01000120; GAB98268.1; -; Genomic_DNA.
DR RefSeq; WP_006594800.1; NZ_BAHD01000120.1.
DR AlphaFoldDB; K6VPY2; -.
DR STRING; 1184609.KILIM_120_00030; -.
DR eggNOG; COG1362; Bacteria.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000008366; 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:UP000008366};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 447 AA; 47176 MW; 1A09992EF0992FDC CRC64;
MPTPTSLELD VDGHAADLCA FIDASPTPFH AVQEAARRLT DAGFTELAER DAWPREPGRY
FVRREGTIAA WSTAAAAGAS TGPATGFRVL GGHTDSPNLR IKPNADVRTL GWDQLGVEVY
GGPLITTWLD RDLGLAGRVA VRDADEPTGV RMCLVQVSEP LLRVAHLAIH LDRSIADEGV
RLNPQQHLAP IWGATGGAPT LAEYLAGLLD VEPNDVLAHD LMMFDLTPSG RLGHARDLIA
APRLDNQATC YAGVRALIDA DTAMAGGGSH IPLLVLFDHE EIGSMTNRGG FSEFLPGLLE
RVVLTQGGDR EDLHRALADS LVCSADMAHA THPNYTERHE PSHRIAVNAG PVLKVNVKGR
YASDAPGAAA FALACEQAGV PLQRFVVRSD MPCGSTIGPM TAALTGVVTV DVGAPMLSMH
SARELCGVAD PAMYVAALTA MLAPAAV
//
