ID A0A1C5K3P3_9ACTN Unreviewed; 960 AA.
AC A0A1C5K3P3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=GA0070213_117121 {ECO:0000313|EMBL:SCG77201.1};
OS Micromonospora humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=745366 {ECO:0000313|EMBL:SCG77201.1, ECO:0000313|Proteomes:UP000199360};
RN [1] {ECO:0000313|EMBL:SCG77201.1, ECO:0000313|Proteomes:UP000199360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45647 {ECO:0000313|EMBL:SCG77201.1,
RC ECO:0000313|Proteomes:UP000199360};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|PROSITE-ProRule:PRU10059, ECO:0000256|RuleBase:RU361166}.
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DR EMBL; FMDM01000017; SCG77201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5K3P3; -.
DR STRING; 745366.GA0070213_117121; -.
DR OrthoDB; 9758662at2; -.
DR Proteomes; UP000199360; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01067; CBM_3; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10059};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 38..960
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5008449735"
FT DOMAIN 507..652
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 663..755
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 765..852
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 850..960
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 648..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 473
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 960 AA; 100593 MW; CD5E0DD4748B72A8 CRC64;
MPRPTPPPRG RPSRRLLAAG AALVAALATA VPLPAAAAPA AAPAGAQAAP AFNYAEALQK
SLFFYEAQQS GRKPAWNRVS WRGDSALTDG ADVGVDLTGG WYDAGDHVKF GFPMAFSTTM
LAWGAVEYRD GYVASGQLSY LLNNLRFVND YFVKAHPAPN VLYGQVGKGD DDHKWWGPAE
VLPMARPAYK IDASCGGADL AGETAAAMAA SSMVFRPTDA AYADKLLGHA KQLYTFADTV
RKAYSECITD AASFYKSWSG YQDELVWGAI WLYRATGDAT YLAKAENEYD KLGTEPQSTT
RSYKWTLAWD NKQFGAYVLL ANLTGKQKYV DDANRWLDYW TVGVNGQKVP YSPGGMAVLD
SWGALRYAAN TSFAALVYSD KTTDATRKAR YHDFAVRQVN YALGDNPRNS SYMIGFGTNP
PKNPHHRTAH GSWWDSQTVP VETRHVLYGA LVGGPSSAND AYSDSRSDYV MNEVATDYNA
GFTSALARLT NEYGGSPRAG FPTAETPDMD ELTVETTVMQ AEPRATGLKA IIYNKSAFPA
RALTTGKFRY YFRPDGTGPV TVTPGYTQGC PSPSSAKQYS GDIWYVEVDC TGYTIAPAGQ
SQHRMEVQFK IGVPEGGTWD PTNDPSYQAT AGPNRKVPLY SGGVRVWGDE PGPATPDTTA
PSTPGTPVAS AVTSSGLTLT WPASTDTGGS GLAGYDIVQT QPGGDVLVLL KSTTNTLAVT
GLAPQQAYQF TVVARDGAGN RSTASPALTV TTAAASTPDT TAPTAPGTPT ASAVGATGLT
LTWGPATDAV GVTGYRVYRG GTVLVGSTTG TTLAVTGLTA ATTYTFTVVA VDAAGNVSPA
SPGVTVTTTA PPAGGGCAVT WTANSWDTGF TANVTVTNTG TTAINGWTLA FTFGNAGQKV
GQAWSANVTQ TGTAVTATNL AYNGTLAAGA STSFGFNGTH TGANPRPTGF TLNGSACTVS
//
