ID A0A0L6CH65_9MICO Unreviewed; 442 AA.
AC A0A0L6CH65;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=VV01_08350 {ECO:0000313|EMBL:KNX37151.1};
OS Luteipulveratus halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=1631356 {ECO:0000313|EMBL:KNX37151.1, ECO:0000313|Proteomes:UP000037397};
RN [1] {ECO:0000313|Proteomes:UP000037397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C296001 {ECO:0000313|Proteomes:UP000037397};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-2015) 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:KNX37151.1}.
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DR EMBL; LAIR01000002; KNX37151.1; -; Genomic_DNA.
DR RefSeq; WP_050669480.1; NZ_LAIR01000002.1.
DR AlphaFoldDB; A0A0L6CH65; -.
DR STRING; 1631356.VV01_08350; -.
DR PATRIC; fig|1631356.3.peg.1621; -.
DR Proteomes; UP000037397; 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:UP000037397};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 442 AA; 46924 MW; 82FD82FE667DD91A CRC64;
MADRSTLSFS EHGFTTDDSA DGLCDYLNAS PSPFHACETS AAMLEAAGFV RLLETEVWPS
RRGRYFVVRG GSLIAWSTEY AADAASPLRV VGAHTDSPSL RVKPQPDVAR GGWQLLGVEV
YGGTLDASWL DRDLGLSGRV AVRSGDEVEG RLLRVDEPVL RVSQLAPHLD RSVRSEGLKL
NAQQHMMPHW GLGETPGDFR AYVGEQLGVA PADVLGWDVM THDLNPAART GRSRETVAGA
RQDNLATSYA ATRALIAAVE VDPVRPVVPV IALFDHEEVG SVSERGAASS YLITTLERVA
ISLGGSREHL FRAIAGGVVA SGDMAHATHP NYSERHEPSH TIAMNGGPVL KTNTNLRYAT
DAMGAAAFRL ACEQAGVPCQ EFVSRSDLPC GSTVGPITSA LTGATTVDFG APTLSMHSTR
ELTGSQDQAM YAAALACFLS PA
//
