ID R5RQM8_9CLOT Unreviewed; 593 AA.
AC R5RQM8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative gamma-D-glutamyl-L-diamino acid endopeptidase 1 {ECO:0000313|EMBL:CCZ42963.1};
GN ORFNames=BN479_00504 {ECO:0000313|EMBL:CCZ42963.1};
OS Clostridium sp. CAG:122.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262773 {ECO:0000313|EMBL:CCZ42963.1, ECO:0000313|Proteomes:UP000017991};
RN [1] {ECO:0000313|EMBL:CCZ42963.1, ECO:0000313|Proteomes:UP000017991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:122 {ECO:0000313|Proteomes:UP000017991};
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 -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:CCZ42963.1}.
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DR EMBL; CAZY010000320; CCZ42963.1; -; Genomic_DNA.
DR AlphaFoldDB; R5RQM8; -.
DR Proteomes; UP000017991; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017991};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..593
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038541896"
FT DOMAIN 294..579
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 593 AA; 66119 MW; 307A803942659714 CRC64;
MLKRKRKLIA MLLALAVMLG GLQQTAMSGA KAQAAVKVQT VVNNKVTVRA QNADGKNTVK
KSNKAKAKLK GDSISEPADV TTGSAIYDDT LPTMDVSIKQ GGSKQIKLKW NSYEGAAYYT
VFYVKGSFHQ TPDNSGNTSE STNDGKTENL LQKTLYNETE FTLNVSRGEN YSFCVVAYSG
EDVALARTDR LTSCIPKKNS VSFTRLSSRR VKLSWNKSKG AEKYIIYKKV NNNKYKKLAE
TKKLRYNDGK VRAGKRYKYY IAAVGIYNNE TFKTESNAKS FVIANFVSMG HQKYSYHEMS
GDLKQLANTY SDYVKVKVIG KSNDKRNIYD VVVGNPKAKK TMLVVSSIHA REYMTAQLCM
AQIEHYLKNY NGRVKGVRLK STLNKIAIHY IPMTNPDGVT ISQFGISKIR DSKLRKALYR
MPGAKSTSSW KANARGVDLN RNYKYNYHAK YGGRRGSSGY SGPYAESEPE TKAVVKLINT
LKKNTKLKGT VNYHAMGSIA FGSVRRGIKK TTKKITIKMY NLVRKITGYA SSASYERGGK
SVGALREYTM YNMKVPSITL EIGVGGCPLP SSQFGSVWRR NYSLVIREAR LLG
//
