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
//