ID   Q21N11_SACD2            Unreviewed;       507 AA.
AC   Q21N11;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=Putative mannan endo-1,4-b-mannosidase {ECO:0000313|EMBL:ABD79918.1};
GN   Name=man5O {ECO:0000313|EMBL:ABD79918.1};
GN   OrderedLocusNames=Sde_0656 {ECO:0000313|EMBL:ABD79918.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD79918.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD79918.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|RuleBase:RU361153}.
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DR   EMBL; CP000282; ABD79918.1; -; Genomic_DNA.
DR   RefSeq; WP_011467139.1; NC_007912.1.
DR   AlphaFoldDB; Q21N11; -.
DR   SMR; Q21N11; -.
DR   STRING; 203122.Sde_0656; -.
DR   CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   KEGG; sde:Sde_0656; -.
DR   eggNOG; COG2730; Bacteria.
DR   HOGENOM; CLU_537337_0_0_6; -.
DR   OrthoDB; 220114at2; -.
DR   Proteomes; UP000001947; Chromosome.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.30.32.30; CBM10; 3.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR036601; CBM10_sf.
DR   InterPro; IPR009031; CBM_fam10.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF02013; CBM_10; 3.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM01064; CBM_10; 3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF57615; Type X cellulose binding domain, CBDX; 2.
DR   PROSITE; PS51763; CBM10; 3.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..507
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004200496"
FT   DOMAIN          353..383
FT                   /note="CBM10"
FT                   /evidence="ECO:0000259|PROSITE:PS51763"
FT   DOMAIN          406..440
FT                   /note="CBM10"
FT                   /evidence="ECO:0000259|PROSITE:PS51763"
FT   DOMAIN          472..501
FT                   /note="CBM10"
FT                   /evidence="ECO:0000259|PROSITE:PS51763"
FT   REGION          442..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  52628 MW;  EDF09678902175A7 CRC64;
     MRIFSIALAL CAVLCAGQSL AGLSIQGTRL VDGNGSTVVL RGVNHPHAWY AGETAAAIPK
     IAATGANSVR VVMAMGTKWS RTSAAEIQTI IDLCKQNNMI AVLEFHDGTG WGEESGTAHI
     SDIADYWVSS DVMAVVKGEE DYVIINIANE PFGNGVSAST YTNDTIAAIQ KLRNAGYTHT
     LMVDAANWGQ DWQNLMRDNA QTIFNGDSLN NTMFSVHMYQ VYNTSAKVQS YMQAFSDKGL
     ALVVGEFAAD HFSEDVAEAA IMQYAEQFGF GYMGWSWTGN SSDLASLDIV KSFSDNTYTT
     WGNRLINGSN GIATTSRIAS VYTGTSSGGS SSSSSSSNSS SSGGTSACST GGSCDWSGTS
     FPLCENGNTN DWGYENGQSC VGVGLCDSNP DATTHCGTSS GGGSTSCGTT SDGHPVCCDA
     ASDPDGDGWG WENEASCVVE SGSSSSSSSS SSTSSSSSSS SSSSSSGGSS ATCNWYGTQY
     PMCTSTSSGW GWENNQSCIS PSTCSGQ
//