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Database: UniProt
Entry: A0A0F4JT44_9ACTN
LinkDB: A0A0F4JT44_9ACTN
Original site: A0A0F4JT44_9ACTN 
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
//
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