ID R5APK0_9FIRM Unreviewed; 469 AA.
AC R5APK0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN ORFNames=BN455_00621 {ECO:0000313|EMBL:CCX45305.1};
OS Firmicutes bacterium CAG:103.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1262999 {ECO:0000313|EMBL:CCX45305.1, ECO:0000313|Proteomes:UP000018290};
RN [1] {ECO:0000313|EMBL:CCX45305.1, ECO:0000313|Proteomes:UP000018290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:103 {ECO:0000313|Proteomes:UP000018290};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CCX45305.1}.
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DR EMBL; CAWL010000015; CCX45305.1; -; Genomic_DNA.
DR AlphaFoldDB; R5APK0; -.
DR Proteomes; UP000018290; 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:UP000018290};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 469 AA; 51534 MW; 3DEB2FF8FFCC10DD CRC64;
MSEDKELKQW KEKLFYQPKN GYDRIGAEQA GEIFAYAEGY KQFLDAARTE REAVKEAIRM
AEAEGFVPYT FGMELQPGSK VYVNNRGKAL MLAVLGQQPL DHGCVIAGAH IDSPRLDLKQ
TPMYEDSELA YFKTHYYGGI KKYQWVTIPL ELHGTVALKD GSTVDIAIGR EPDEPQFVIT
DLLPHLGKDQ MRKTMEEGIT GEALNIVIGS MPYAGEGRDR VKLAVLSLLY DEYGITEEDF
LSAELAAVPA FPARDIGFDR SMIGAYGQDD RVCAYAELRA ILDLDGAPER TAVCILADKE
EIGSDGVSGM QSQAFEAFMA DLCEQQDVAL RHCFARSFCL SADVCAAFDP SFPEVSAKRT
EAKLNYGVGI CKFTGARGKS GTSDASAELV AYLRRLFADN GVVWQLSEMG KVDQGGGGTI
AKFMADRNID TIDAGVPVLS MHAPFELVAK FDCWMTYRGV LAAYCDTQA
//