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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//