ID D1Y7Z8_9BACT Unreviewed; 438 AA.
AC D1Y7Z8;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=HMPREF7215_0269 {ECO:0000313|EMBL:EFB89575.1};
OS Pyramidobacter piscolens W5455.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Pyramidobacter.
OX NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB89575.1, ECO:0000313|Proteomes:UP000006462};
RN [1] {ECO:0000313|EMBL:EFB89575.1, ECO:0000313|Proteomes:UP000006462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W5455 {ECO:0000313|EMBL:EFB89575.1,
RC ECO:0000313|Proteomes:UP000006462};
RA Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (DEC-2009) 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:EFB89575.1}.
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DR EMBL; ADFP01000127; EFB89575.1; -; Genomic_DNA.
DR RefSeq; WP_009165979.1; NZ_ADFP01000127.1.
DR AlphaFoldDB; D1Y7Z8; -.
DR STRING; 352165.HMPREF7215_0269; -.
DR eggNOG; COG1362; Bacteria.
DR OrthoDB; 9764268at2; -.
DR Proteomes; UP000006462; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 438 AA; 47117 MW; E1A2DE649B84E67F CRC64;
MKNDVSRRLI DFLDGSPTCY QAIENLSSRL REKGYAPLRE SERWSLERGG KYFTTRGESS
LIAFRLPAGE LRGFMLTASH SDSPTFKLRQ NAEVPSAGST VRLSVEGYGG AIMRSWLDKP
LSVAGRVFVK KGAGLASKLI DIDRDLLVIP SLAIHMNREM NKGVELKANV DMLPLFSMQG
EEGAFRRLVA EAAGVGADDV VSTELFLYPR TPGTLVGLNG EFIVSPRLDD LECVFCCYTG
FVESESAPSA SAPLFCVFNN EEVGSGSRQG ANSTFLEDTV GRICGALDMS ADERGAAVAD
SFMISADNAH AIHPAHSEYA DGNEFPVLNG GVVIKYNAAQ KYTTDGLSGA VFSRLCELAG
VPVQRYSNRA DLPGGSTLGN ISGSHLSVPT VDIGLPQLAM HSCYEIAGVK DAEYLIEAVR
AFYGKSFRHG ADGRIALE
//
