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Database: UniProt
Entry: D4ILJ1_9BACT
LinkDB: D4ILJ1_9BACT
Original site: D4ILJ1_9BACT 
ID   D4ILJ1_9BACT            Unreviewed;       412 AA.
AC   D4ILJ1;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Predicted Zn-dependent peptidases {ECO:0000313|EMBL:CBK63803.1};
GN   ORFNames=AL1_13420 {ECO:0000313|EMBL:CBK63803.1};
OS   Alistipes shahii WAL 8301.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK63803.1, ECO:0000313|Proteomes:UP000008794};
RN   [1] {ECO:0000313|EMBL:CBK63803.1, ECO:0000313|Proteomes:UP000008794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK63803.1,
RC   ECO:0000313|Proteomes:UP000008794};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J.;
RT   "The genome sequence of Alistipes shahii WAL 8301.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK63803.1, ECO:0000313|Proteomes:UP000008794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK63803.1,
RC   ECO:0000313|Proteomes:UP000008794};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; FP929032; CBK63803.1; -; Genomic_DNA.
DR   RefSeq; WP_015546704.1; NZ_CP102253.1.
DR   AlphaFoldDB; D4ILJ1; -.
DR   STRING; 717959.AL1_13420; -.
DR   KEGG; ash:AL1_13420; -.
DR   PATRIC; fig|717959.3.peg.3021; -.
DR   HOGENOM; CLU_009902_1_1_10; -.
DR   OrthoDB; 9811314at2; -.
DR   BioCyc; ASHA717959:AL1_RS06260-MONOMER; -.
DR   Proteomes; UP000008794; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008794};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          15..129
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          169..344
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   412 AA;  46583 MW;  7D7EBCF47FA0ADDA CRC64;
     MIPYTRKTLP NGLTVVVNRD RASKLAAVNI LYRVGARNEN PARTGFAHLF EHLMFRGTRA
     VENFDLPVQM ASGDNNAFTN NDYTDFYITL PKDNLETALW LESDRMEGLD ITPAKLEAEK
     KVVIEEFRQR YLNQPYGDQT MLLRALAYKV HPYRWAAIGL ATDHIAGATL ADVESFYRAH
     YRPSNAILSI SADMEEEWML ELAEKWFAPL ADHPSETAAI PQEPVQTQAR RQEVERDVPA
     STVTVAYHMC ARTKLDFYTA DLVSDLLSGG DSGRLYTHLV KERNLLSSVN AYITGDVDPG
     LFVFTGQLLP GVTPEAAEAA FREEIEALQT TVATAYEIEK VKNKFEANTL FGELNVMNKA
     MNLGFYEMLG DLSLINREVD RYRAVTDEDI RSFSRRTLRP ENSSTLIYNA RK
//
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