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Database: UniProt
Entry: A0A1F8RXK0_9CHLR
LinkDB: A0A1F8RXK0_9CHLR
Original site: A0A1F8RXK0_9CHLR 
ID   A0A1F8RXK0_9CHLR        Unreviewed;       707 AA.
AC   A0A1F8RXK0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN   ORFNames=A2Z32_13890 {ECO:0000313|EMBL:OGO52365.1};
OS   Chloroflexi bacterium RBG_16_69_14.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797661 {ECO:0000313|EMBL:OGO52365.1, ECO:0000313|Proteomes:UP000178994};
RN   [1] {ECO:0000313|EMBL:OGO52365.1, ECO:0000313|Proteomes:UP000178994}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO52365.1}.
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DR   EMBL; MGOC01000160; OGO52365.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8RXK0; -.
DR   STRING; 1797661.A2Z32_13890; -.
DR   Proteomes; UP000178994; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
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; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS50853; FN3; 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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          492..589
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   ACT_SITE        99
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        130
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        323
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   707 AA;  74774 MW;  E2AEA5A54505D248 CRC64;
     MLRSGADTAA VVEKARKRDG VKADRSYARA FRGFSAKLDE QQRIDLLADP NVVAVVPDGV
     VQLTQTVPTG VARVGGRQSD VAAIDGTDHR VDADVAIVDT GITYHPDLNV AGGYNCSTAD
     RTAWRDRNDH GTHVAGTVAA LDNSFGVVGV APGARVWAVK ILNDDGYGLI SWYICGLDWI
     LAQRDPNDAS RPLFEAVNMS VTKAGSDDGN CGFTNSDPLH QAICRLVAGG VTVVAAAAND
     SHNAAKNIPA SYNEVITVSA LADTDGKPGG LGGNRCYSWG TYDKDDTFAN FSNYGGDVDI
     IAPGKCILST IPGPGYAYLS GTSMAAPTVA GAVALYKESR PNATPSEVRE ALRYLGNLYW
     AVSTDPDGTH EPLLDVSRIR SLGVFDFAPA GPTAAPVEAG TTAQIPVHLV RSSTFFERVR
     ISITSLPDGW FGTPVPASLL GWTADTGRLS VVVPKDTPLG RYDIGVQATN QWRTKTTTLS
     VEVVQDAPTA TPPISLVKLG TKVMLNAVWA DVAWAPATDP TSAIAGYEVE TSRNGGPWAS
     TLAGSAAQRT ATFLVGFDAS YRFRVRAVDA AGHWSPWAVG AVPMVVHPVD DRSSSISRAG
     RWARGYSASP FRTTVTGSSR TGDTLTMTFT GHGVAVVGPR NPRRGSAKVY IDGVYVKTIF
     MWSRTGSSRQ VAFTRSFPAG GTHRITLRVV GGGSHPLFRL DAFVVSR
//
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