ID R3WP42_9ENTE Unreviewed; 1860 AA.
AC R3WP42;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:EOL43605.1};
GN ORFNames=UC7_02935 {ECO:0000313|EMBL:EOL43605.1};
OS Enterococcus caccae ATCC BAA-1240.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158612 {ECO:0000313|EMBL:EOL43605.1, ECO:0000313|Proteomes:UP000013840};
RN [1] {ECO:0000313|EMBL:EOL43605.1, ECO:0000313|Proteomes:UP000013840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1240 {ECO:0000313|EMBL:EOL43605.1,
RC ECO:0000313|Proteomes:UP000013840};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus caccae BAA-1240.";
RL Submitted (FEB-2013) 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:EOL43605.1}.
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DR EMBL; AJAU01000022; EOL43605.1; -; Genomic_DNA.
DR RefSeq; WP_010773014.1; NZ_KE136472.1.
DR STRING; 317735.RU98_GL000109; -.
DR PATRIC; fig|1158612.3.peg.2901; -.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG1501; Bacteria.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000013840; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.20.1270.90; AF1782-like; 6.
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; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
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; PF07554; FIVAR; 6.
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; 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; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
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:EOL43605.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1834..1853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 898..981
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 970..1078
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1129..1198
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT REGION 749..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1860 AA; 204563 MW; C5F443D44FE29ECA CRC64;
MNKEQQVVNS SGKKRWLQVL LISSSVLALH SFVTMNPQTA AAQEQTAKET TTDLAESVGA
IVSIEKSSEN FVVTYASGEK AQVSILNDHV FRYHLDPIGK FAEYPTPNDP KHVAKITAKK
MADYGTETFK QTSVTDSGEQ FILENSGLKI IFTKATALMQ VVDKQKNKTI LEETAPLSFK
NNKVTQTLKQ NNQEQYFGGG TQNGRFTHKG TAIQIVNTNN WVDGGVASPN PFYWSTEGYG
VVRNTWKPGT YDFGSHDPQT TTTTHDGVDF DAFYFFDGSS AGILKDYYEL TGKATLMPEY
GFYEAHLNAY NRDYWVKVAD GTSGAVKFED GNYYKEYQPG DLGNLKGTLE SLNGEKNNYQ
FSARAVIDRY KKNDMPLGWF LPNDGYGAGY GQTDSLDGDV QNLKEFTDYA NGNGVEVGLW
TQSNLHPADP QKPKKGERDI EKEVSVAGVK ALKTDVAWVG NGYSFGLNGV EDAANVFVKE
TDGAVRPMIV SLDGWAGTQR HAGIWTGDQT GGQWEYIRFH IPTYIGTSLS GQPNVGSDMD
GIFGGKNKDV NIRDFQWKTF TPVQLNMDGW GSNPKTPFAL DQETTDLNRA YLKLKSMMMP
YNYSIAHEAV DGLPMVRAMS LEFPNESAAY TKDSQYQYMW GPNLLVAPIY NGNKDAEGKS
VRDGIYLPDE KQVWVDLFTG EKYQGGRVLN GMKTPLWKVP VFVKDGGIIP MTNPNNNPTE
IKRDQRTFLI YPNGPTSFEM YEDDGISTSY ESGQSATTKI SSQGPKSNEK GELTVTIEPT
KGSYKGFVDE RSTTLDLMAS EAPESVTATI GGTQVTLKQA ANKEDFSTGT NMYYFDKEFQ
VNSYLSKASG EKLNQSALSV KLDKQSVTTK DVQVTVKGFI NKGTVDGGNT EVDDQLTIPA
NIAINEEKTT PSSLTVQWDK VTEATSYEVE RDGTVFGNIQ DSTATFDGFS FLTEHTFKVR
TVGKSGVSKW SEPIKGITRD DPYKETIDQV KATSSLPEQP GEELKHLTDK DLSSGWHTNW
STGIANPNSG NFLTLKFDLG AEFQMDKIEY LPRENAGNGN ILQLQYRISK DGVNWTEFSA
PISWKQDALI KTIETKDQIY RFVEMKVLKS VGNFGSGREM LFYKQPGTEG ILHGDITNDG
VIDENDAMSY RNYTGLESID SDFNGYVEKG DLNKNGVIDS YDIHYVLRQL DGGIDLPNTE
EIAGGLVLSV VNENGKNTYL PGDSLSFTLK GQELKNINAL SIRMSFDSSK FELVGQPTTT
SATRQMANYS KYRKHSNDLE NIYLVISNQG NKPLLNGAMD LITFKIKVKE TTRAKRAAEK
TEPQPLQFDM SQGLLVGQAL QQAMLSDFSV TVNPTKEIDK TMLQEMVTLN QGRIEKEYTP
ETWSIFRPVL EKAVAILVND QATQTEVDAT VKNLEQAVNQ LVKVPDVADK TALEKAIQEG
AAKKPSEGNE FTKETKKVLD DALVAAQKIF AQEGATQAEI DKARQTLTEA ITQVKEQAIT
VDKEVLKKRI AEAKAITPKE GFEFTEKTKA QLQQAIQLSE TIVAKTDATK EEVTTILTTL
NEAIAQLKEV PVTNKNPLQA VLKQASQVTP SEGHQFTADS LQTLQAAIVA AEKVLNNPFA
NQEMIDQTTT ALTEAIKGLQ EEPLVTDKTA LKAILVQAKA VKPTAGKEFT PVTKARLTEV
IEIGESVLSN VNARQEQIDT AEMTVKTALD GLVEQVIQTD KTKLMELIQQ AETLKPKSGN
QFTKDTQEAL TEAIKQGKAV VNDPNATQAA VNKSFDTLSQ MMKAMKEEST TSGNGTGAGT
GGVIGQGSSK TGGVTGKTNA IGKLPKANEV VSPVWGISGL LIILSISLVK AFFKNKKNQN
//
