ID   A0A1H9VEU8_9PSEU        Unreviewed;       445 AA.
AC   A0A1H9VEU8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN   ORFNames=SAMN05216188_1262 {ECO:0000313|EMBL:SES20089.1};
OS   Lentzea xinjiangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=402600 {ECO:0000313|EMBL:SES20089.1, ECO:0000313|Proteomes:UP000199352};
RN   [1] {ECO:0000313|Proteomes:UP000199352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3525 {ECO:0000313|Proteomes:UP000199352};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC       {ECO:0000256|RuleBase:RU361186}.
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DR   EMBL; FOFR01000026; SES20089.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9VEU8; -.
DR   STRING; 402600.SAMN05216188_1262; -.
DR   OrthoDB; 309899at2; -.
DR   Proteomes; UP000199352; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR   InterPro; IPR016288; Beta_cellobiohydrolase.
DR   InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR001524; Glyco_hydro_6_CS.
DR   PANTHER; PTHR34876; -; 1.
DR   PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361186};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361186};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361186};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361186};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361186}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          340..445
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
SQ   SEQUENCE   445 AA;  45627 MW;  8A6DA76A76495DB3 CRC64;
     MARWKRGSGA CLLAGAVVAG VATLVVSGGT TVSAAESAFY VDPATAGARW VAANPGDSRA
     AVIRDRIASV PQARWYTTTN TSTVRSEVSS FVGAAASAGK IPIMVVYNIP NRDCGGASGG
     GAPSHEAYRA WVDEVAAGLA GRPATIVLEP DVLPLMTNCQ NADQQNQTRA SMAYAGKKLK
     SGSAQAKVYF DIGHSAWLNP AEAANRLRGA DISNSADGIS TNVSNYRTTS DSVNFAKAVL
     NAVGDSRLKA VVDTSRNGNG PAGSEWCDPA GRAIGTPSTT NTGDSKIDAF LWVKLPGEAD
     GCIAPAGQFV PQRAYELAVA AGPITTTTTT TTTTTTTTTG TNPGGGCRAT HRVISQWQGG
     YSAEIVIENR GAAINGWTFT FSAPGVSVLQ GWSGTWTDTG DVVRVANAAW NGSIASGAQM
     TIGYNASYAG TPPFSSPVLN DVACS
//