ID R6AWB2_9BACT Unreviewed; 1302 AA.
AC R6AWB2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glycosyl hydrolase family 31/fibronectin type III domain protein {ECO:0000313|EMBL:CDA45422.1};
GN ORFNames=BN693_02281 {ECO:0000313|EMBL:CDA45422.1};
OS Prevotella sp. CAG:5226.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262930 {ECO:0000313|EMBL:CDA45422.1, ECO:0000313|Proteomes:UP000018184};
RN [1] {ECO:0000313|EMBL:CDA45422.1, ECO:0000313|Proteomes:UP000018184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:5226 {ECO:0000313|Proteomes:UP000018184};
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 glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
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:CDA45422.1}.
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DR EMBL; CBBW010000207; CDA45422.1; -; Genomic_DNA.
DR Proteomes; UP000018184; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14254; Dockerin_II; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd06596; GH31_CPE1046; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDA45422.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018184};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..1302
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004412865"
FT DOMAIN 882..964
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 952..1104
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1302 AA; 144424 MW; B641B410F60362D3 CRC64;
MKRNNQNKRG CKCATLVMAL PLAVAGLTIT PNGVQALPLA SGLVQNSAVA QTAAPSSNPI
KNVAKINPTT VEVTYADGKQ LTVDFYGDNI FRLFRDDNGG VVRDPQATPP AKILVENARR
STQSVDLRNE SNGVVISTPR IAVRFDKQTG LMTVVDTKSG ETVVESVAPV SFDKNSTTLT
LKAQSGEYFY GGGVQNGRFS HKGKSIAIEN TNNWVDGGVA SPTPFYWSTG GYGVMWNTFK
PGRYDFGATE EGKVILSHQE DYLDAFIMVD KQPVDLLNDF YQLTGNPVLL PKFGFYEGHL
NAYNRDYWKE ADNGFMLYED GKRYNESQKD NGGVKESLNG EKNNYQFSAR AAIDRYINND
MPLGWFLPND GYGAGYGQTS SLDGNIQNLK EFGDYARSKG VHIGLWTQSD LHPKEGIEPL
LQRDIVKEVR DAGVRVLKTD VAWVGYGYSF GLNGVADVAQ VMPYYGSNAR PFIISLDGWA
GTQRYAGIWS GDQTGGDWEY IRFHIPTFIG SGLSGQPNIT SDVDGIFGGK NVPVNVREFQ
WKTFTPMELN MDGWGANPKY PEVLGEPATS INRSYLKLKS ELLPYTYTIA RQAVDGKPMI
RAMFLDYPND YTLGSDTQYQ FMYGPSFLVA PIYKETKMDK DGNDIRNGIY LPEGRWVDYY
NGDVYEGGRI INTYDAPLWK LPVFVKADAI IPMTNPNNNP SQIRKDYRAY EIYSTAAGTN
GFSQYDDDGE TQEYLSGQCT RTAVSTYANG KGKLVVTINP TYGKFEGFEP QKETELRINV
SKAPKSVTAK VGKKGVKLTK VTSLADFEKG TDVYYYNEKP NLNRFATPGS EMAKKEIIKN
PQLLVKIGKT DVTANLIDVK VDGFEFNPAD RLRTHSGALS APKVDFAENN VGVFSLTPSW
NKQENADFYE IEYNGMLYST IRDNAFTIDG LDPETAYAFK VRAVNKDGYS DWSNVSATTK
SNPLEFAIKG IKAQNSAEDQ PGQGIDKMFD FDEKSPWHTK WGKGEGVPAD ITIDLRSVNK
LDRLEYIPRE DAGNGTLLAG SFSYSTDRQT WSAPVKFEWA QNADHKTFSF AGNPEARYVK
MHLDKAVGNF ASGSQMYIFK VAGSESFYQG DINHDKRIDE NDLTSYMNYT GLRKGDSDFD
YVSAGDINKN GLIDAYDISC VATELDGGVR NSNDKVAGKL VLTPNKKTFA AGDMVEVTVS
GKGLHYVNAL SFALPYITSE LEYAGVELLN MKDMVNLTYD RLHTNGQKEL FPTFVNRGNN
FLLDEGDHNL FVIKFKAKKA GKFNLTAKDG MLVDRNLGTV NF
//
