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Database: UniProt
Entry: R6PNC5_9BACT
LinkDB: R6PNC5_9BACT
Original site: R6PNC5_9BACT 
ID   R6PNC5_9BACT            Unreviewed;       490 AA.
AC   R6PNC5;
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=S1C subfamily peptidase MucD {ECO:0000313|EMBL:CDC25005.1};
GN   ORFNames=BN637_01431 {ECO:0000313|EMBL:CDC25005.1};
OS   Prevotella sp. CAG:386.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262925 {ECO:0000313|EMBL:CDC25005.1, ECO:0000313|Proteomes:UP000018046};
RN   [1] {ECO:0000313|EMBL:CDC25005.1, ECO:0000313|Proteomes:UP000018046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:386 {ECO:0000313|Proteomes:UP000018046};
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   -!- 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:CDC25005.1}.
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DR   EMBL; CBEZ010000065; CDC25005.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6PNC5; -.
DR   STRING; 1262925.BN637_01431; -.
DR   Proteomes; UP000018046; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 2.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR025926; PDZ-like_dom.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR   Pfam; PF12812; PDZ_1; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018046};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..490
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004415472"
FT   DOMAIN          303..371
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   490 AA;  51951 MW;  59EC548E648F19C4 CRC64;
     MRKVSKYVLA VLCISSLAFS AGAFMKVNAA APSVTSVAPG QPVDLTYAAE KALPAVVHIK
     YVQNSKVQTV DVQSNPFGDF FDPFGFFGNP GGGQGGTRKQ KVQTPKREAT GSGVIISSDG
     YIVTNNHVVE GADELTVTLN DNREFSARII GTDKSTDLAL IKVNAKDLPT LPIANSDNVK
     VGEWVIAVGN PFGLNNTVTA GIISAKARSL GANGVESFIQ TDAAINAGNS GGALVNTQGE
     LVGINAMLYS QTGSYAGYGF AIPTSIMNKV VDDLKKYGSV QRVMLSIQGS DVLNYINSQK
     ENGKEVDLGT NEGVYVTKVD EDGNGADAGL KEGDIITKID GKKVTKMAEL QEALNSKRPG
     DKLSITYLRN KRSYTKSITL KNAQGNTSVI KSADLDVLGG TFRPVTEAQK KELGIKYGLE
     VLKVGAGALK DAGISRGLII QRVNDTNITT LDDLQKIVKS ASTSKEPVLY IQGVWPTGKK
     SYFAVPLQKD
//
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