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Database: UniProt
Entry: A0A1C5HEI0_9ACTN
LinkDB: A0A1C5HEI0_9ACTN
Original site: A0A1C5HEI0_9ACTN 
ID   A0A1C5HEI0_9ACTN        Unreviewed;       968 AA.
AC   A0A1C5HEI0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Cellulose 1,4-beta-cellobiosidase {ECO:0000313|EMBL:SCG44390.1};
GN   ORFNames=GA0070614_1208 {ECO:0000313|EMBL:SCG44390.1};
OS   Micromonospora coxensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG44390.1, ECO:0000313|Proteomes:UP000198215};
RN   [1] {ECO:0000313|EMBL:SCG44390.1, ECO:0000313|Proteomes:UP000198215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG44390.1,
RC   ECO:0000313|Proteomes:UP000198215};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT607753; SCG44390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5HEI0; -.
DR   OrthoDB; 33861at2; -.
DR   Proteomes; UP000198215; Chromosome i.
DR   GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.170.160.10; Endo-1,4-beta-glucanase f. Domain 2; 1.
DR   Gene3D; 4.10.870.10; Endo-1,4-beta-glucanase f. Domain 3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR   InterPro; IPR027390; Endoglucanase_F_dom3.
DR   InterPro; IPR000556; Glyco_hydro_48F.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF17957; Big_7; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02011; Glyco_hydro_48; 1.
DR   PRINTS; PR00844; GLHYDRLASE48.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS51318; TAT; 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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..968
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008717587"
FT   DOMAIN          29..138
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          429..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   968 AA;  103584 MW;  469B9511075CC960 CRC64;
     MRLMARRRRM AMLAATALAI GGVTLPAGAA QAAPACDVVY TTNDWGSGFT GNVTIKNLGD
     AVNGWTLKWT FPNTSQRVTQ GWSAKWSQTG SVVTATNESW NGSLGTGAST TIGFNGAYSG
     SNPKPTSFTL NGVTCNGVGT NQPPTVALGV PTGPFEAPAD VPLTATASDP DGTISKVEFY
     RNGLLVNTDT TAPYGYTLED LPAGSYTVQA KAYDNANASA VAEKAFTVSP ASGPVLVATP
     SAVSVTEGGS STVNLKLSAA PSANVTVALA RTGDTDVTVS PASVTLTPSN WNTGATVTVS
     AAEDSDTVGG TATITASASG LAPLAITATE IDNDTPGGDN TYIARFLDQY GKIKNSGYFS
     PEGVPYHSIE TLIVEAPDHG HETTSEAFSF WLWLEANYGR VTQNWAPFNN AWTVMEKYII
     PSHADQPTAG AAGTPQYAAE HPLPSGYPSQ LQPNVPVGQD PLRSELQSTY GTGDIYGMHW
     LLDVDNVYGY GRCGDGTTKP AYINTFQRGT QESVWETVPQ PSCETFKHGG QYGYLDLFIK
     ESNAPAKQWK YTNAPDADAR AVQAAYWAMT WAEAQGKEAD VAATVAKAAK MGDYLRYAMF
     DKYFKKIGNC VGASTCPAGT GKDSAHYLMS WYYAWGGAYE AGQNWSWRIG SSHNHFGYQN
     PFAAWALTNV DALKPKSPTA VADWQKSFER QLEFYTWLQS AEGGIAGGAT NSWDGSYAQP
     PAGTATFYGM YYDVDPVYND PPSNQWFGMQ AWSMQRIAEL YLETGNAKAK ALLDKWVPWA
     IANTTLGANW SIPSDMKWTG QPNNWNPTNP QPNTNLHVEV TVKGQDVGVA AAYARTLIAY
     AAKSGNVSAK NTAKGLLDAL HAASDDKGVS MPEKRGDYKR FDDVYDAATG QGLYIPPGWT
     GRMPNGDAIA AGKSFTDIRS FYKNDPAWPK VQAYLDGGPE PVFNYHRFWA QADVAMAYAD
     YGHLFPNG
//
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