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Database: UniProt
Entry: J9G6V7_9ZZZZ
LinkDB: J9G6V7_9ZZZZ
Original site: J9G6V7_9ZZZZ 
ID   J9G6V7_9ZZZZ            Unreviewed;      1249 AA.
AC   J9G6V7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Glycosyl hydrolase, family 31/fibronectin type III domain protein {ECO:0000313|EMBL:EJX02579.1};
GN   ORFNames=EVA_09320 {ECO:0000313|EMBL:EJX02579.1};
OS   gut metagenome.
OC   unclassified sequences; metagenomes; organismal metagenomes.
OX   NCBI_TaxID=749906 {ECO:0000313|EMBL:EJX02579.1};
RN   [1] {ECO:0000313|EMBL:EJX02579.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23251564; DOI=10.1371/journal.pone.0051521;
RA   Alcaide M., Messina E., Richter M., Bargiela R., Peplies J., Huws S.A.,
RA   Newbold C.J., Golyshin P.N., Simon M.A., Lopez G., Yakimov M.M., Ferrer M.;
RT   "Gene sets for utilization of primary and secondary nutrition supplies in
RT   the distal gut of endangered iberian lynx.";
RL   PLoS ONE 7:E51521-E51521(2012).
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:EJX02579.1}.
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DR   EMBL; AMCI01002488; EJX02579.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9G6V7; -.
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; 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; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR   PANTHER; PTHR43863:SF2; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 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   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:EJX02579.1}.
FT   DOMAIN          827..910
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          900..1048
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
SQ   SEQUENCE   1249 AA;  138641 MW;  4CBD94B64863E396 CRC64;
     MRQQAVQIVN ARMINPTTVE ILYANGQMMT LDFYGENIFR VFQDNKGGIV RDPQATPEAQ
     ILVNNARRNP GLVHLNADDS QVTIKTARIA VVFDRTSGLM TIFKGKAGSE KVVEAVAPFA
     FSDKNVTLSL KERDNEYFYG GGVQNGRFSH KGKAIAIVNT NNWIDGGVAS PTPFYWSTKG
     YGLLWHTFKP GRYDFGATEP GKVILSHDEN YLDVFFMVND GAVPLLNDFY QLTGNPVLLP
     KFGFYEGHLN AYNRDYWTVT DKGTMAYEDG KFYAESQKDN GGIKESLNGE LPGNYLFSAR
     AAIDRYLNND MPLGWFLPND GYGAGYGQTS TLDGNIQNLK EFGDYARSKG VEIGLWTQSD
     LHPKEGVEAL LQRDIVKEVR DAGVRVLKTD VAWVGAGYSF GLNGVADVGE IMPYYGSNAR
     PFIISLDGWA GTQRYAGIWS GDQTGGDWEY IRFHVPTFIG SGLSGQPNIT NDMDGIFGGK
     NLPVNIRDFQ WKTFTPMELN MDGWGANPKY PQALGEPATS INRTYLKMKS ELLPYTYTIA
     REAVNGKPMV RAMFLDYPNA YTLGTATQYQ FLFGPSFLVA PIYQETAMDK DGNDIRNGIY
     LPEGKWVDYF NGDVYEGGRV INNYPTPIWK LPVFVKSGAI IPVTHPNNNP SEIRKDYRAY
     EIYADGKTEF VDYDDDGKTQ EYLGGMCTRV ALMTNVDGNK LTVNIGKTEG EFTGFEPVKE
     TELRVNVSQE PKKVVAKVGK KKVKLTAVTS LDEFNRSSNV YFYNAAPNLN RFATKGSAFE
     SVKMIKNPQL WIKLDKCNVS ETETEVLVEG FAFQPADHLR KSTGALAVPN VKFTKEGVQP
     YDLTPSWEKV ANADFYEIEF NGMLYSTITD LKLNFEGLIP ETAYSFKVRA VNKEGYSDWA
     TATATTLSNP LEFAVKGIKA TVTCADQPGQ AVGKLFDFDP KSEWHTKWGK GEAVPFDMTM
     DLRSVNQLDR LDYHPRESGG NGTLLEGTVA YSMDKQQWSE PVAFTWANNT EVKTIAFAGH
     PKARYVKLSI TKAIGNFGSG KELYVFKVAD TESELQGDIN RDKRIDENDL TSYMNYTGLR
     SVDSDFGYVS VGDVNKNGMI DAFDISVVAT ELDGGVSNSA DKVAGSLVLT PNVKTFKAGD
     IVEVKVTGKG LHAVNALGFG LPYSTDDFEF AGLDLVGMKN MVNLTYDRLH SNGQKALYPT
     FVNKGNNFLL DEGEPYLFTI KFKAKRNGKF NLKAVDGILV DRNLGTVKF
//
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