ID   A0A1C6V3J4_9ACTN        Unreviewed;       926 AA.
AC   A0A1C6V3J4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cellulose binding domain-containing protein {ECO:0000313|EMBL:SCL60480.1};
GN   ORFNames=GA0070617_4393 {ECO:0000313|EMBL:SCL60480.1};
OS   Micromonospora yangpuensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=683228 {ECO:0000313|EMBL:SCL60480.1, ECO:0000313|Proteomes:UP000198937};
RN   [1] {ECO:0000313|EMBL:SCL60480.1, ECO:0000313|Proteomes:UP000198937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45577 {ECO:0000313|EMBL:SCL60480.1,
RC   ECO:0000313|Proteomes:UP000198937};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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DR   EMBL; FMIA01000002; SCL60480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6V3J4; -.
DR   STRING; 683228.GA0070617_4393; -.
DR   OrthoDB; 9764804at2; -.
DR   Proteomes; UP000198937; Unassembled WGS sequence.
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; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR   PROSITE; PS51173; CBM2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
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:UP000198937};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..926
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038588008"
FT   DOMAIN          821..925
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          760..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..823
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   926 AA;  97711 MW;  2790F6D5DD243EB5 CRC64;
     MRRSLAGAVA SVLALATAVV AVQLTVAPVG PAVAAVSEPY TWKNVRIDGG GFVPGIVFNP
     TEKDLIYART DIGGLYRWEQ ASQSWRPLLD WVGYDKWGWN GVLSVATDPV QTSRVYAAVG
     MYTNDWDPNN GAILRSADKG ATWQATELPF KVGGNMPGRG MGERLAVDPH RNSTVYFAAE
     GGNGLWRSTD SGATWAKVAN FPNVGNYVAD PTDSTGYQSQ NQGLTWVAFD KSTGTAGSAT
     QTIYVGVADK QNPVYRSTNG GSSWERIPGQ PTGYLAHKGV VDHVGGHLYL ATSDTGGPYD
     GAKGDVWKFT RSTGAWTRIS PIPSSSSDAY FGYSGLTIDR KNPNTLIVAT QISWWPDAIF
     WRTTDGGATW SRIWDWGSYP ERVKKYKMDI SSVPWLDFGA NPQPPEETPK LGWMNESVEI
     DPHNPDRFLY GTGATIYGST DLTKWDTGGQ LTITPMVKGL EETAVLDLVS PPSGPPLVSA
     LGDIGGFRHD NLDAVPAKMF TQPVFTSSTS LDYAEANPAV MVRAGNFTDA DRPNDSHVAF
     STDGGANWFQ GTEPGGINNG GTVAAAANGS RFVWAPGDPG QQVVHSVGFG NSWTASTGVP
     ANATVESDRV DPNRFYAVSG GKLYVSTNGG VSFTASAATG LPTEGVKFKA VPGQQGHLWL
     AGAGGLWRST DSGASFTRLG GVTQADNVGF GKAAPGRSYP ALFLFGTVDG QPGLYRSDDT
     GASWVRINDD QHQYGNAGEA LTGDPRVFGR VYLGTNGRGI LVADRQGGPT TPPTTPPTTP
     PTTPPTTPPT TPPTTPPTTP PTTPPTTPPT TPPTTPPLPT TPGPITGCRA TYTVTGSWSG
     GFQGEVTVRN YDDTGIIGWT VTWTFANGQR VNQSWGGTVV QDGAGVTVTN ASYNGVLAPG
     ASTTFGFLAS WTGTNGVPTP TCTSRR
//