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Database: UniProt
Entry: A0A0J1G5P3_9FIRM
LinkDB: A0A0J1G5P3_9FIRM
Original site: A0A0J1G5P3_9FIRM 
ID   A0A0J1G5P3_9FIRM        Unreviewed;      1767 AA.
AC   A0A0J1G5P3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN   ORFNames=RHS_3626 {ECO:0000313|EMBL:KLU70613.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU70613.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU70613.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU70613.1};
RX   PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA   Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA   Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA   Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA   Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT   "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL   Cell 159:253-266(2014).
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:KLU70613.1}.
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DR   EMBL; JNGB01000038; KLU70613.1; -; Genomic_DNA.
DR   PATRIC; fig|1504536.3.peg.4553; -.
DR   Proteomes; UP000036477; Unassembled WGS sequence.
DR   CDD; cd00063; FN3; 5.
DR   Gene3D; 2.60.40.1080; -; 4.
DR   Gene3D; 1.20.1270.90; AF1782-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR46708:SF2; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46708; TENASCIN; 1.
DR   Pfam; PF02368; Big_2; 3.
DR   Pfam; PF00041; fn3; 5.
DR   SMART; SM00635; BID_2; 4.
DR   SMART; SM00060; FN3; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 4.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS50853; FN3; 5.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1767
FT                   /note="Fibronectin type-III domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038740683"
FT   DOMAIN          930..1015
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1023..1108
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1115..1204
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1211..1296
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1304..1390
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1188..1219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1767 AA;  190079 MW;  BF7C3AB08C0CCD21 CRC64;
     MKKKLLSMIT ALAVIVSSIA PGITVSAAAD QEATTGTTYY VSTLNGKDSN DGTSESNAFY
     SLQKINELTL QPGDRVLLES GSEFTNGYLH LYEQSGSPES PIVIDKYGDG NNPVINTNGQ
     GIWYQNYGGM LDNVNHVFKG YVSSSVLLYD SEYIEIKNLE ITNRGPKIET VYNNQKVMER
     TGVAAIAQNK GTVDHIYLNQ LNIHDVIGNV YDKHMDNGGI QMNVLKPKNE EATGISRYND
     VKIENCYLDN VNRWGIAIGY TAYFDKFAGT AIPDDVIAKY GHGNVEIRNN YVKEAGGDAI
     TTMYCDRPLI EYNVSDGAAR QINDADYIAT GQGKVAAGIW PWKCKDAVFQ YNEAFDTYFN
     GDGQAWDADS GDGTIYQYNY SHNNGGGCVM FCLQQSYRNI FRYNISQNDL SGVINAPAQP
     DSHIYNNVFY VKEGVPFIRP GMTGGVMNVE NNIIYYAGDQ AKTESWTLNG TRASYSNNLY
     YNYANIPGDD ENAVNVTAGT QVFEDPGKAP SATNGVINSH EDPSQKTVFD GYKLAENSPA
     INAGKVIQDN GEQDFFGNEV TGIPDIGAHE SDIASMGLFS SVYTIADRQI SGLAMNTTVE
     QFLGNLVYDK KLEVHVFDRE EQELTGKDIV SGGSKLTLSD GNETVEYVVT ASTDNSIKDS
     IFEIRDDAVY VPMTEKAAVS VEDILTGITV HDTAVKKLYQ NDAEVTQGNV KDGMTLKVIA
     EDGSEADYTI TAKNEYHWAK DFVEEQQGNV WFAQQKENDT YSNMTVFDPT YATWNGKEYA
     IIGLQGNKGQ PTADKNGLFC DSLAVAQRAQ GYSAAYRSPV SGNIIMSFKD MGDKKNAYLR
     QASAASTNTG SNVFLTITKN GEQVGEKVQI PNDGSGVEIA PSAMQVAKGD YIRLEINNEG
     SQNASRPSAY VTPVITYVDA AETDTQAPTT PDNIKAEDIT STSANISWDA SADNVGVTGY
     EVKNGNEIIK NISEGTSASL DGLIPSTEYT ITVTAFDAAG NKSEPGSVTF ETKQLEDTQK
     PTAPANIKVT DITDTSATIT WNASADNVGV RGYKVLNGSE ELADVTDTKV TLQELAPETD
     YALTIVAYDA AGNHSDPAAA TFTTAEKPDT ESPTVPADVR AEDITDTTAM ILWTASADNK
     AVAGYRVKNG NVILKDQVTD TKVQLVNLEP GTDYVINVVA YDAAGNESAP GSVSFTTLGE
     TAEPDTEKPS VPADVKAENV TSDTAEISWT ASADNIGVIG YKVMNQETLL ANVTDGTSFQ
     LKELAAATEY TIDIIAYDAA GNESDPGSVT FTTSELIDEE APSTPANIKA ERIAQTSAWI
     SWNPSNDNIG VTGYEVKNGD SILAEVTGET RVELKDLLRG TEYTISITAH DAAGNRSEPG
     IVSFTTLRAD ASGLNAKIIE AQAIKNDNGI YTKSSYADLQ NAILDAKETA ENKNSSDEDI
     RTAIADLQDA MKLVKVTLTL NTGKAEMEAG DMLQLTPLTN ETEAVVTWSS SNEKAVSVDT
     KGMVKAIAPG TAAVKANLGT ITAVCTITVK SRPAPTPGPT LTLNKSRVTI YTQGTKTVKL
     TAKVTGPSKK VTWKSSDSKI ATVKNGKVTA KKAGKVTITA KANGIQKTCL ITVKKPALKL
     SRSRLTLYTK GKTTAEINAK ITGSSKRIVW KTSNKKIAAV KNGKVTAKKS GRVTITAKAN
     GITRRCEVTV KKPSLKVKSG MEIFLKKGKT AKISAKAKPD GKIIFKSSKS KIVTVSKKGV
     VKALKKGRAE ITVSCNGVKK IIKVHVD
//
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