ID A0A0F4JT44_9ACTN Unreviewed; 577 AA.
AC A0A0F4JT44;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN ORFNames=VR44_06890 {ECO:0000313|EMBL:KJY36918.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY36918.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY36918.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY36918.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC {ECO:0000256|RuleBase:RU361186}.
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:KJY36918.1}.
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DR EMBL; JZWV01000128; KJY36918.1; -; Genomic_DNA.
DR RefSeq; WP_045946486.1; NZ_JZWV01000128.1.
DR AlphaFoldDB; A0A0F4JT44; -.
DR PATRIC; fig|68223.7.peg.3462; -.
DR eggNOG; COG5297; Bacteria.
DR OrthoDB; 309899at2; -.
DR Proteomes; UP000033551; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 25..577
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5039747963"
FT DOMAIN 31..140
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 135..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 292
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT ACT_SITE 516
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 483
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT BINDING 514
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ SEQUENCE 577 AA; 60250 MW; A4C1F33F2F08F2CA CRC64;
MSRIIPRTAL LAALGLVTAA GATATVFGTP AGAATAGCKV EYRITNQWNT GFGADVVVTN
TGDPVAAWTL EWTYANGQQV TQGWNAAITQ SGAAVTAKSL SYNGSLATGG STSFGFNGSH
TGTNGVPATF KLNGVTCNGA DPTQPPTTPP TTPPTTPPPS GGKVDNPYAG ARVYVNPEWS
AKAAAEPGGT RVSNQPTAVW LDRIALVTGG SGKMGLRDHL DAALAQKGSG ELVVQLVVYD
LPGRDCSALA SNGELGPTEI DKYKTQFIDP IAAILADPKY AGLRIVAAVE IDSLPNLVTN
VSGRPTATPA CDVMKTNGNY IKGVGYALNK LGSIANVYNY VDAGHHGWLG WDDNFGASAE
MFKQAATAEG STLSKVHGFI VNTANFSALK EDNFKIDDSV GGTSVRQSKW VDWNRYTDEL
SYAQAMRAKV VSLGFDPGVG MLIDTSRNGW GGTARPTGPG ATTSVDSYVN GGRYDRRIHL
GNWCNQAGAG LGERPQAAPA PGIDAYVWMK PPGESDGASK EIPNNEGKGF DRMCDPTYTG
NVRNGNSMSG ALPDAPLAGQ WFPAQFQELM KNAYPAL
//