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Database: UniProt
Entry: E0I6W4_9BACL
LinkDB: E0I6W4_9BACL
Original site: E0I6W4_9BACL 
ID   E0I6W4_9BACL            Unreviewed;       707 AA.
AC   E0I6W4;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=Glycoside hydrolase family 5 {ECO:0000313|EMBL:EFM11780.1};
GN   ORFNames=PaecuDRAFT_1386 {ECO:0000313|EMBL:EFM11780.1};
OS   Paenibacillus curdlanolyticus YK9.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11780.1, ECO:0000313|Proteomes:UP000005387};
RN   [1] {ECO:0000313|EMBL:EFM11780.1, ECO:0000313|Proteomes:UP000005387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YK9 {ECO:0000313|EMBL:EFM11780.1,
RC   ECO:0000313|Proteomes:UP000005387};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA   Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT   "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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DR   EMBL; AEDD01000003; EFM11780.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0I6W4; -.
DR   STRING; 717606.PaecuDRAFT_1386; -.
DR   eggNOG; COG2730; Bacteria.
DR   eggNOG; COG3325; Bacteria.
DR   eggNOG; COG3525; Bacteria.
DR   OrthoDB; 220114at2; -.
DR   Proteomes; UP000005387; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFM11780.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005387};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..707
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038585089"
FT   DOMAIN          15..156
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          318..405
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
SQ   SEQUENCE   707 AA;  74954 MW;  E7255BC5B5242F59 CRC64;
     MRKILACLIM FSMLVSGIAV PAKTSAAATN AALNKPASAS SIEDSGKTAA MAFDGNASTR
     WSSTYADPQW ISVDLGSAVD ITGVMLNWEV AYGKAYQIQT SLDNSSWSTV YSTTTGDGGI
     DNISFSTQKA RYVKMYGTQR GTSYGYSLWD FEVYAVGSTN EPAPITSGSV YKLTAQHSGK
     ALDVAGGAVN DGANVQQWSD NGSDEQKWKV ISVGDGYYKL ISQKSGKALE VAGFATNDGA
     NVQQWTDTGQ SNQKWKIVDA GSGYYKLIAQ HSGKALDVVG GASNDGANVQ QWTDNGNSQQ
     KWKFTEVTVV QDTTAPTAPT NLASPSKTAS TVNLTWSAST DNVAVTGYDV YRGATLAGTT
     TSTSYTATGL TANTAYSFTV KAKDAAGNVS SASSALSVTT STQPTTAAGF YINGTKLYDA
     NGNPFVMRGI NHAYTWYKGQ EETAFPAIAR TGANTIRIVL SDGQQWSKDS LATIQKLITL
     AEQNKMVAIV EVHDGTGSDS AAVLDNIANY WIEMKSALIG KESTVILNIA NEWYGTWNGA
     GWAAGYKSVI PKLRNAGIKN TIMVDGAGWG QYPQSIVDYG TEVFNADPLK NTMFSIHMYE
     YAGGNAATVK SNIDNVLAKN LALVIGEFGI KHTNGDVDEA TIMSYSEQKG VGYLGWSWKG
     NGSGLEYLDM SNDWAGTSYT EQGNAIINGA NGIKATSKIA TVFGSSN
//
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