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Database: UniProt
Entry: D9TBD3_MICAI
LinkDB: D9TBD3_MICAI
Original site: D9TBD3_MICAI 
ID   D9TBD3_MICAI            Unreviewed;       685 AA.
AC   D9TBD3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Cellulose-binding family II {ECO:0000313|EMBL:ADL46538.1};
GN   OrderedLocusNames=Micau_3007 {ECO:0000313|EMBL:ADL46538.1};
OS   Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS   129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL46538.1, ECO:0000313|Proteomes:UP000001908};
RN   [1] {ECO:0000313|EMBL:ADL46538.1, ECO:0000313|Proteomes:UP000001908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC   {ECO:0000313|Proteomes:UP000001908};
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., Ovchinnikova G.,
RA   Hirsch A.M., Woyke T.;
RT   "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002162; ADL46538.1; -; Genomic_DNA.
DR   RefSeq; WP_013286165.1; NC_014391.1.
DR   AlphaFoldDB; D9TBD3; -.
DR   STRING; 644283.Micau_3007; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   KEGG; mau:Micau_3007; -.
DR   eggNOG; COG3534; Bacteria.
DR   HOGENOM; CLU_030937_0_0_11; -.
DR   OrthoDB; 9758333at2; -.
DR   Proteomes; UP000001908; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR43576:SF3; ALPHA-L-ARABINOFURANOSIDASE C; 1.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..685
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003128943"
FT   DOMAIN          485..575
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          573..685
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          477..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  71711 MW;  5D39939B5F37C7BB CRC64;
     MRRTTAFAAS LLLLATALST VGGPVAAADP TDPVTVTVNT RAGLATVPAT ALGVNHAIWD
     SQLGSAETSD LLKAAGVKML RYPGGSYADI YHWETHTAPG GYVAPNTDFD TFMAGARRVG
     AEPMIIANYG TGTPAEAAAW VRYANVTKGY GAKWWTVGNE NYGNGHYGSA WEADDHPDKS
     ASQYARLVVE YADAMKAVDP SIKVGAVLTM PGNWPDGITA GSDPGPWNQT VLSIAGPKID
     FVDVHWYPGG SAADSLARTN HLPDAAWLLR QQIARYAGPG ADRIGISFTE LNVDAGRTTA
     PGALFLADAY SGLLEQGVFT VQWWNVHNGI GTVSEVAGQT DYGDFGLLSS GNCTSDGEVC
     QPAFNTPFAP YHALSMMNLF VRPGDQLVRA GTDQPLVAAH AVRRPDGSVA VLLLNKDPDN
     AYPVALDYAG FTPADEAPTV HTFTNGATGI STGRSGSAAA RTLPPYSLTT LVLRPAGSSA
     GRPGAPGRPT ASTVTDRAAT ISWPAATPGG SPIAKYEVHR QYGAVSEQLG ETAGTSLTVG
     NLEPGPRYTV NVLARDTAGR VSWSSPPLTF ATGSPAESSC AVRFDDDNDW GNGYVANVEV
     INTGAKAVDG WTLTWTWPTA WQQVSSGWSA TWDQQGRDVR VTPTADNRRL AADGGSTTVG
     FVGAYSGPNV PVGAFRLNGT VCTLR
//
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