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Database: UniProt
Entry: A0A327YWR2_9ACTN
LinkDB: A0A327YWR2_9ACTN
Original site: A0A327YWR2_9ACTN 
ID   A0A327YWR2_9ACTN        Unreviewed;       659 AA.
AC   A0A327YWR2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=B0I29_13122 {ECO:0000313|EMBL:RAK25671.1};
OS   Actinoplanes lutulentus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1287878 {ECO:0000313|EMBL:RAK25671.1, ECO:0000313|Proteomes:UP000249341};
RN   [1] {ECO:0000313|EMBL:RAK25671.1, ECO:0000313|Proteomes:UP000249341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7090 {ECO:0000313|EMBL:RAK25671.1,
RC   ECO:0000313|Proteomes:UP000249341};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000966};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAK25671.1}.
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DR   EMBL; QLMJ01000031; RAK25671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327YWR2; -.
DR   OrthoDB; 4902692at2; -.
DR   Proteomes; UP000249341; Unassembled WGS sequence.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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; 2.60.40.10; 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; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00150; Cellulase; 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.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249341};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..659
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039574668"
FT   DOMAIN          471..556
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          558..659
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
SQ   SEQUENCE   659 AA;  70423 MW;  CCB34CFCE72E079F CRC64;
     MFQRRGRKRL AAAVAAVALA LTGGQAFPAA APAAPAAASA ALQATAFEAA AAPGSDWLHV
     DGNQIVDAAG NPVWLTGVNW FGFNASERVF HGLWSANITE ITRSMAQRGI NIVRVPISTQ
     LLLEWKAGTF GTVNVNTYAN PELTGKNSLQ IFDYWLALCE QYGIKVLLDV HSAEADNSGH
     IHPVWYKGTI TPELYYQAWE WVTARYKAND TIVAMDLKNE PHGTPGTTPR AKWDNSTDVD
     NWKYTAETAA KRILAINPEV LVLVEGQEVY PREGETWSSP NTDPDLSPNY YYNWWGGNLR
     GVRDYPINLG ANQDQLVYSP HDYGPLVFNQ PWFDKPFDKT SLTNDVWRPN WLYIHENDTA
     PLLIGEWGGR LGQDERQDRW MTALRDLIVE HRLHQTFWVL NPNSGDTGGL LLDDWKTWDE
     QKYALLKPAL WQQSGKFVSL DHEVALGGAG STTGISLSAA YGSADTVAPS VPGQPASSSI
     TSTGVTLTWA ASTDNVGVTS YDVLRGGSVV ATVSGTTYNA TGLTANTAYS FTVRARDAAG
     NVSAASTARS VTTAASGGGG GDGGCTATYR TTSSWSGGFQ AEVTVRNTGT AAGTSWVVNW
     TYPSGTTVAS LWNGVQGTPA VTVRNADHNG ALAGGASAAF GLVGTGTAAT PATVSCTLS
//
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