ID A0A134AHL2_9FIRM Unreviewed; 449 AA.
AC A0A134AHL2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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=HMPREF1863_00675 {ECO:0000313|EMBL:KXB67202.1};
OS Peptoniphilus coxii.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=755172 {ECO:0000313|EMBL:KXB67202.1, ECO:0000313|Proteomes:UP000070442};
RN [1] {ECO:0000313|Proteomes:UP000070442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00729 {ECO:0000313|Proteomes:UP000070442};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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:KXB67202.1}.
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DR EMBL; LSDG01000022; KXB67202.1; -; Genomic_DNA.
DR RefSeq; WP_068367264.1; NZ_KQ960172.1.
DR AlphaFoldDB; A0A134AHL2; -.
DR PATRIC; fig|755172.3.peg.647; -.
DR OrthoDB; 89722at2; -.
DR Proteomes; UP000070442; 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:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 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:UP000070442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 449 AA; 49258 MW; 3C7E00291010C62F CRC64;
MEKIKSYWKL PDVQKDIAAF SEDYKTFLDR SKTERMAVAE IMRIAEKAGY NNLDDVEKLG
RGDRVYVNNK GKSIMLFDIG ENPEKGMAII ASHIDSPRLD VKPNPLYEEN NVALLKTHYY
GGIKKYQWTA IPLAIHGVMF RKDGTKVDVH VGSDPEDPIF TITDLLPHLS KSQNSKTLAE
GIIGEKLNVL VGHKPGEVNV KEALLALLKE KYGIEEDDFT VSELEVVPAF SARDLGFDRS
MIAGYGQDDR VCSYASLRAF VDGKDREKTC VAIFADKEEI GSVGNTSMSA NYFKNALGEV
LHAMGNDDHL AINRALANSY VLSADVTAAM DPNYPEVMDK LNAAQLGEGV CMMKYTGARG
KSGTSDANAE FLAALRKKFD EDGVIWQVGE MGKVDEGGGG TVAYILAETG AEVVDLGTAL
FSMHAPYEVA SKADIYSTYK AYASFLTMK
//