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Database: UniProt
Entry: I9SCN5_9BACE
LinkDB: I9SCN5_9BACE
Original site: I9SCN5_9BACE 
ID   I9SCN5_9BACE            Unreviewed;       971 AA.
AC   I9SCN5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN   ORFNames=HMPREF1068_00816 {ECO:0000313|EMBL:EIY53646.1};
OS   Bacteroides nordii CL02T12C05.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=997884 {ECO:0000313|EMBL:EIY53646.1, ECO:0000313|Proteomes:UP000003089};
RN   [1] {ECO:0000313|EMBL:EIY53646.1, ECO:0000313|Proteomes:UP000003089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL02T12C05 {ECO:0000313|EMBL:EIY53646.1,
RC   ECO:0000313|Proteomes:UP000003089};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA   Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides nordii CL02T12C05.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00001255};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC         galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001271};
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:EIY53646.1}.
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DR   EMBL; AGXS01000011; EIY53646.1; -; Genomic_DNA.
DR   RefSeq; WP_007483740.1; NZ_JH724314.1.
DR   AlphaFoldDB; I9SCN5; -.
DR   STRING; 997884.HMPREF1068_00816; -.
DR   PATRIC; fig|997884.3.peg.826; -.
DR   eggNOG; COG3866; Bacteria.
DR   HOGENOM; CLU_004997_0_0_10; -.
DR   Proteomes; UP000003089; Unassembled WGS sequence.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006558; LamG-like.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR42970; PECTATE LYASE C-RELATED; 1.
DR   PANTHER; PTHR42970:SF1; PECTATE LYASE C-RELATED; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00560; LamGL; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000003089};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..971
FT                   /note="Fibronectin type-III domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003726070"
FT   DOMAIN          470..558
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
SQ   SEQUENCE   971 AA;  106520 MW;  2665011CDA1FE667 CRC64;
     MLYKKLITTL LLPLCMGTMY AQQLAFPGAE GYGRFAKGAR ASESPEIYHV TNLDDSGKGS
     LRDAVSQPNR IIVFDVAGVI KLKSRLVFSK NLTIAGQTAP GEGVVVYGNG VSFSAAENII
     VRYLRIRMGI GGTSGADAAG IANGGNMIFD HVSATWGLDE NFSINWDSKG FEPYNITIQN
     SIIGQGIMVH ACGGLIQTNG GVTLYRNLYI DNKTRNPKVK GLNQFVNNVV YNWGEGGAYI
     LGDTEASSWG VITNNYFIKG PVEGTKAFTR AKAAFQVYQK GNMIDYNKDG ILNGYEATED
     DYRRDASNPE SENVTFIKSI DEFDYSDYDR RKLVDGEKVV VTTIPEKHPV IEGETTAAEA
     YDWIINRVGA SLPVRDEADN YMIDELLSLG TKGALLSGES ELGLPNGVGN IFDGEKMLDT
     DNDGMPDVWE DANGLDKNNP NDALLMAENG YLNIENYVNS ITAPMPYVKY PTNLQLTSLS
     TDYLSFKWVN NAPESTSVIL EYSIDNKDFT SISLAPGTTT HKLESLAPNT TYYIRLKTVN
     GEKESLYTST QEFATRGIPA PPIASVNPIP GNETTITDYT SVRLSWENKT GAWAGALSYT
     VYLGKSVEDM DVVLTASTAN VVTVNVEAAT TYYWRVDAKN LLGDCKGDVW SFTTGTKPER
     GKVAYYSFNE TEGTILENMY GENATAKDFT PLWVKGIQNN AAQFDKANAA FVQEHYDALT
     LGNESFSIEL WFKSAGGSVD WYLLHKGSHA TNSYEGATGK WFGIQYQKNS KNDRLTWAID
     DNVTKTDINV TGATTKYFNN EWVHLVCVRD VEEKQLKMYA NGILVASGAD KTGDIGTIER
     MAIGNCNTAY ENGFQGLMDE LTIYNEALTA EEVSDHYKQG TSTHIENIIT PNTGCAYPMP
     FADDFYIPVM GAEDLTAQVS VMNTAGQTVY QAQVIIQGGI AHVANVGFLP KGYYVYTLKI
     DQRILVGKIV K
//
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