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Database: UniProt
Entry: R5W4Q4_9BACT
LinkDB: R5W4Q4_9BACT
Original site: R5W4Q4_9BACT 
ID   R5W4Q4_9BACT            Unreviewed;       871 AA.
AC   R5W4Q4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Fibronectin type-III domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN505_01193 {ECO:0000313|EMBL:CCZ98198.1};
OS   Alistipes sp. CAG:157.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1262692 {ECO:0000313|EMBL:CCZ98198.1, ECO:0000313|Proteomes:UP000018346};
RN   [1] {ECO:0000313|EMBL:CCZ98198.1, ECO:0000313|Proteomes:UP000018346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:157 {ECO:0000313|Proteomes:UP000018346};
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   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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:CCZ98198.1}.
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DR   EMBL; CBAZ010000028; CCZ98198.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5W4Q4; -.
DR   Proteomes; UP000018346; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR032304; Peptidase_S8_N.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF16361; Peptidase_S8_N; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000018346};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..871
FT                   /note="Fibronectin type-III domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004396035"
FT   DOMAIN          63..204
FT                   /note="Subtilase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16361"
FT   DOMAIN          236..524
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        243
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        298
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        485
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   871 AA;  92907 MW;  B696E6953D8B3493 CRC64;
     MRVSCLRRTF INQPYYRMKR YLNLLFLAAA ALCASCARDA VVSDVPPKGE DVGGYDNNVI
     VPGWVRIRLD DEAAPLRTGV FTRGEADSGN PLLDELAAGL GATEIREVFP TDPRFEERHR
     KYGLHLWFDI RLGDEVPVSR AEQEFAALPG VRHAQPIYRI VALDGADYPL PSEVSEPSSW
     EGSSREMPFN DPGLKMQWHY DNDGTMTNAE GETVAVEGAD IGLFEAWEIY GAGDPSVIVA
     VMDTGVFSGH EDLQGNMWVN EAELNGTAGK DDDGNGYRDD IHGYDFYKKS PDVEPGEHGT
     HVAGTIAAVN DNGIGVSGVA GGTGNGDGVR IMTCAIYDYM GYGTATPTGY VYAADNGAVI
     SQNSWNYPMI NILPEDMSVA FDYFIDNAGI GPDGEQTGPM KGGVIIFAAG NEFSPKVGCP
     SDDPRVITVT SMMADYVKAS YSNYGTEADI FAPGGAGERD AAFPQQGQVY STGLDNTYTY
     HSGTSMACPH VSGVAALIVS HYGANASGFT NEELKTILLR SYRNVDMWQT RPDIAAGLGA
     GLVDASLMEL ENPGVPPEAP AGLEVAEGTV EERLTVSVTG LPADGNGMGI AYVNLRYAPE
     EARAESGAWT SVTIPCRMSP GEALEYEVSG LADATTYVFE AGAIDRFGNE SGYVGGEGRT
     IDHINRPPAI QKPLPGVELP DAAGEEPFVT AVELSDYFTD PDLPADELSY AARSNDESVA
     TVSVSGSMLT VEGLKLGATY VSVTVTDLAG ESIVKNMSVK VLEERFPEDP PTPIPPEEGV
     ELTEGALTLF PNPAPDALFI GVGGEAGKRA DIRVYDSAAR EVVRLDGAAF GSEGELKDVI
     RYDVSGLVPG SYTVRVKLAD GRELRSTFVK A
//
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