ID A7B9Z0_9ACTO Unreviewed; 434 AA.
AC A7B9Z0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=ACTODO_00446 {ECO:0000313|EMBL:EDN80014.1};
OS Schaalia odontolytica ATCC 17982.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=411466 {ECO:0000313|EMBL:EDN80014.1, ECO:0000313|Proteomes:UP000003553};
RN [1] {ECO:0000313|EMBL:EDN80014.1, ECO:0000313|Proteomes:UP000003553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN80014.1,
RC ECO:0000313|Proteomes:UP000003553};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN80014.1, ECO:0000313|Proteomes:UP000003553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17982 {ECO:0000313|EMBL:EDN80014.1,
RC ECO:0000313|Proteomes:UP000003553};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Actinomyces odontolyticus (ATCC 17982).";
RL Submitted (MAY-2007) 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:EDN80014.1}.
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DR EMBL; AAYI02000004; EDN80014.1; -; Genomic_DNA.
DR RefSeq; WP_003790824.1; NZ_DS264586.1.
DR AlphaFoldDB; A7B9Z0; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_11; -.
DR Proteomes; UP000003553; 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 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 434 AA; 46267 MW; 5041E031ED8D5151 CRC64;
MAQLELDEVH ANAVDYQHFL LDSPSPYHAA EVVAQRLVDA GFTRVDEKGA WDASPGGHVM
VRGGAVAAWF VPETVDDDAG FRIVGAHTDS PAFSVKPSVQ STTPDGWGQI DVEVYGGMMW
NSWLDRELTL AGRLVLNSGE VVLARTGPIA RIPQLAIHLD RDVNPGGLKL DPQKHLHPVW
TVDNPYGNVL EYVARTAGLD DASQVAAFDL ILTPSQGPGF FGDKGQFIAA SRQDNLSSVH
PGLVALERLA AQGTPAGGDV TVFMCFDHEE VGSESRTGAA GPILETVLRR TAKALGRDED
GFERMLAASS CVSADAAHSV HPNYAGHHDP DNRPMMGRGP VIKINSKQRY ATDAEGIALW
NRACAAAGVS SQNFVGNNAM PCGTTIGPIT ATRLGILTVD VGVGLLSMHS AREMSHVDDL
LDLARVLEAY WQGA
//