ID C5BLD5_TERTT Unreviewed; 723 AA.
AC C5BLD5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Glycoside hydrolase family 26 domain protein {ECO:0000313|EMBL:ACR12952.1};
GN OrderedLocusNames=TERTU_0149 {ECO:0000313|EMBL:ACR12952.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12952.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR12952.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC {ECO:0000256|ARBA:ARBA00007754, ECO:0000256|PROSITE-ProRule:PRU01100}.
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DR EMBL; CP001614; ACR12952.1; -; Genomic_DNA.
DR RefSeq; WP_015819065.1; NC_012997.1.
DR AlphaFoldDB; C5BLD5; -.
DR STRING; 377629.TERTU_0149; -.
DR CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH26; Glycoside Hydrolase Family 26.
DR KEGG; ttu:TERTU_0149; -.
DR eggNOG; COG4124; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_016930_2_2_6; -.
DR OrthoDB; 9816550at2; -.
DR Proteomes; UP000009080; Chromosome.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro.
DR GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.30.32.30; CBM10; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR036601; CBM10_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR009031; CBM_fam10.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR000805; Glyco_hydro_26.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR40079:SF4; GH26 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR40079; MANNAN ENDO-1,4-BETA-MANNOSIDASE E-RELATED; 1.
DR Pfam; PF02013; CBM_10; 2.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01064; CBM_10; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF57615; Type X cellulose binding domain, CBDX; 2.
DR PROSITE; PS51763; CBM10; 2.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51764; GH26; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU01100};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01100}; Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..723
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002948691"
FT DOMAIN 28..137
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 191..220
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 302..336
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 403..718
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT REGION 135..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 556
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT ACT_SITE 655
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ SEQUENCE 723 AA; 75698 MW; 92979574CF2A3F33 CRC64;
MNNNWFNKLW RGAACSALAV FASASLANTV TSAGGTAAAT INVNNDWGAG YCATVAISNQ
GSAPVTGWQV ELALNGATIS NLWNGSLTGN LVSNLSYNGT INVNGSSEFG YCANGSGGNY
LPSLASLTVQ GGGTTSSSSS NSSSSSSSSS SSSSSSSSSN SSSSSSSSSS SSSSSSSSSS
SSSSSGGACQ VCNWYGEIRP LCANQDSGWG WENSQSCIGA NTCNSQWGGG GVVNNCGSTS
SSSSSSSSSS SSSSSGASSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSG
GIPNAASNGW PYCRSADSDP DGDGWGWENS YSCIVFGSAA DPGPGDFDYC LIGDSELTLC
SADNGSWGAE NGEICLSASM CPGMGSGVQG AMRDTPVNPD ASAKTQSLYS YLQSIWGNHM
LSGQMDLTWQ DAIDQYQRCI NDTGRAPAMM GYDFLNYGLY WNGISGITQT EEAIEHWNRG
GIVSFTWHWR DPDAADGTIG EFYTEDTSFT IPIANGELDT SSPSYANIQA DIAMIAAELQ
KLEDENVPVL WRPLHEASGG WFWWGRSDRT DGVPAAYAQV VLWRHLYETL TNEYGLDNLI
WVWNGQSGAW YPGDNYVDIV SVDIYDGQQN YESQIGPYAL TANYPQQVKM VALSENSNIP
DPDLMAADGA WWLWFMVWND SDTAEGVSSS GNFWTGEYYN TNAHKTHVYN HEYVITLDEL
PAF
//
