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Database: UniProt
Entry: A0A1M6UXC0_9ACTN
LinkDB: A0A1M6UXC0_9ACTN
Original site: A0A1M6UXC0_9ACTN 
ID   A0A1M6UXC0_9ACTN        Unreviewed;       590 AA.
AC   A0A1M6UXC0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN   ORFNames=SAMN05421803_13044 {ECO:0000313|EMBL:SHK73937.1};
OS   Nocardiopsis flavescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=758803 {ECO:0000313|EMBL:SHK73937.1, ECO:0000313|Proteomes:UP000184452};
RN   [1] {ECO:0000313|EMBL:SHK73937.1, ECO:0000313|Proteomes:UP000184452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5723 {ECO:0000313|EMBL:SHK73937.1,
RC   ECO:0000313|Proteomes:UP000184452};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQZK01000030; SHK73937.1; -; Genomic_DNA.
DR   RefSeq; WP_073383959.1; NZ_FQZK01000030.1.
DR   AlphaFoldDB; A0A1M6UXC0; -.
DR   STRING; 758803.SAMN05421803_13044; -.
DR   OrthoDB; 309899at2; -.
DR   Proteomes; UP000184452; 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   PIRSF; PIRSF001100; Beta_cellobiohydrolase; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184452};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|RuleBase:RU361186"
FT   CHAIN           33..590
FT                   /note="Glucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361186"
FT                   /id="PRO_5039751662"
FT   DOMAIN          38..146
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          145..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT   ACT_SITE        304
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT   ACT_SITE        528
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         495
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         522
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         526
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ   SEQUENCE   590 AA;  61767 MW;  62418D5E54094318 CRC64;
     MSRIHSAATP GPSRARRGPA ALSALVVGAA LAVVPAAPAS ADSGCAVEYT VNDWGSGFTA
     NVEITNLGAA VNGWTLDWSF PGNQQVTNLW GGTHTQSGAN VSVSDAGYNS SISTDGAVSF
     GFNGSYSGSN AAPLAFELNG VLCDGAVDPG EPGEPGEPGE PGEPGEPGTS RVDNPYSGAD
     VYVNPVWSAN AAAEPGGEAV ANEPTGVWLD RIGAIEGNDS PTTGSMGLRD HLDEAVEQSG
     GEPLVFQVVI YNLPGRDCAA LASNGELGPD EIDRYRDEYI DPIADILADY EDTELRIVTT
     IEIDSLPNLV TNVSPRATAT PECDEMLANG NYVEGVGYAL ATLGDIDNVY NYVDAGHHGW
     IGWEDNFVPS AQIFYQAANA AGATPADVHG FIANTANYSA LEEENFSIGQ TIAGVPVRQS
     SWVDWNNYVD ELSFSQALRT ELVSQGFPSD IGMLIDTSRN GWGGADRPTG PGPQTDVDAY
     VDGGRYDRRV NPGNWCNQAG AGLGERPQTA PAAGIDAYVW MKPPGESDGS SELIDNDEGK
     GFDRMCDPTY EGNVRNGNSP SGALGDAPIS GHWFSAQFQE LLDNAYPPLD
//
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