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Database: UniProt
Entry: D9SUM6_CLOC7
LinkDB: D9SUM6_CLOC7
Original site: D9SUM6_CLOC7 
ID   D9SUM6_CLOC7            Unreviewed;       375 AA.
AC   D9SUM6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Dockerin type 1 {ECO:0000313|EMBL:ADL50931.1};
GN   OrderedLocusNames=Clocel_1175 {ECO:0000313|EMBL:ADL50931.1};
OS   Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL50931.1, ECO:0000313|Proteomes:UP000002730};
RN   [1] {ECO:0000313|EMBL:ADL50931.1, ECO:0000313|Proteomes:UP000002730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC   {ECO:0000313|Proteomes:UP000002730};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium cellulovorans 743B.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002160; ADL50931.1; -; Genomic_DNA.
DR   RefSeq; WP_010076215.1; NC_014393.1.
DR   AlphaFoldDB; D9SUM6; -.
DR   STRING; 573061.Clocel_1175; -.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   KEGG; ccb:Clocel_1175; -.
DR   eggNOG; COG4124; Bacteria.
DR   HOGENOM; CLU_038234_0_0_9; -.
DR   OrthoDB; 9802773at2; -.
DR   Proteomes; UP000002730; Chromosome.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   CDD; cd14256; Dockerin_I; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; PF00404; Dockerin_1; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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; 2.
DR   PROSITE; PS51764; GH26; 1.
PE   3: Inferred from homology;
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:UP000002730};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..375
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003128441"
FT   DOMAIN          2..299
FT                   /note="GH26"
FT                   /evidence="ECO:0000259|PROSITE:PS51764"
FT   DOMAIN          308..375
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000259|PROSITE:PS51766"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        245
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ   SEQUENCE   375 AA;  41754 MW;  95C4DA9E725AC6BD CRC64;
     MVKKKLFIKP LIFALAVSSL GISQAAYANA AELKIGAWPG SQPTASNIDT LEALQQRNLD
     YIQTFIDWKT NFDGVRSCAD ATYANGSIFM ITWEPWQYNT VQIKDGAADS YIKKMADDMK
     AYGKELWLRP LHEANGNWYP WGIGDSKVNT NESYIAAYRH IVDIFRAEGA TNVKFVFNVN
     CSNVGQGASF MGHYPGDAYV DYNSIDGYNW GTTQSWGSTW QSFDQIFSSA YNALKPVNKP
     IFIAEMSSAE KGGDKAQWIT DTYNTIKTFY DKIFSVMWFN ENKETNWTIN SSEASLAAYI
     KAIGGSTPTA IVGDINKDGK INALDYAKLK AYLLGSSTET PNMNTWDVNG DGKLNAIDLA
     IFKKYILGQI TAFPR
//
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