ID GUNF_RUMCH Reviewed; 722 AA. AC P37698; B8I7V1; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 27-MAR-2024, entry version 138. DE RecName: Full=Endoglucanase F; DE EC=3.2.1.4; DE AltName: Full=Cellulase F; DE AltName: Full=EGCCF; DE AltName: Full=Endo-1,4-beta-glucanase F; DE Flags: Precursor; GN Name=celCCF; OrderedLocusNames=Ccel_0729; OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / OS H10) (Clostridium cellulolyticum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Ruminiclostridium. OX NCBI_TaxID=394503; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8936327; DOI=10.1099/00221287-142-4-1013; RA Reverbel-Leroy C., Belaich A., Bernadac A., Gaudin C., Belaich J.-P., RA Tardif C.; RT "Molecular study and overexpression of the Clostridium cellulolyticum celF RT cellulase gene in Escherichia coli."; RL Microbiology 142:1013-1023(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Zhou J., Richardson P.; RT "Complete sequence of Clostridium cellulolyticum H10."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 387-722. RX PubMed=1398087; DOI=10.1016/0378-1119(92)90062-t; RA Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., RA Belaich J.-P.; RT "Sequence analysis of a gene cluster encoding cellulases from Clostridium RT cellulolyticum."; RL Gene 119:17-28(1992). CC -!- FUNCTION: Probable endoglucanase involved in the degradation of CC cellulose or related beta-glucans. 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 48 (cellulase L) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U30321; AAB41452.1; -; Genomic_DNA. DR EMBL; CP001348; ACL75108.1; -; Genomic_DNA. DR EMBL; M87018; AAA73866.1; -; Genomic_DNA. DR PIR; PC1139; PC1139. DR RefSeq; WP_015924275.1; NC_011898.1. DR PDB; 1F9D; X-ray; 2.30 A; A=30-658. DR PDB; 1F9O; X-ray; 2.50 A; A=30-658. DR PDB; 1FAE; X-ray; 2.00 A; A=30-658. DR PDB; 1FBO; X-ray; 2.30 A; A=30-658. DR PDB; 1FBW; X-ray; 2.00 A; A=30-658. DR PDB; 1FCE; X-ray; 2.00 A; A=30-658. DR PDB; 1G9G; X-ray; 1.90 A; A=30-658. DR PDB; 1G9J; X-ray; 1.90 A; A=30-658. DR PDB; 2QNO; X-ray; 2.00 A; A=30-658. DR PDBsum; 1F9D; -. DR PDBsum; 1F9O; -. DR PDBsum; 1FAE; -. DR PDBsum; 1FBO; -. DR PDBsum; 1FBW; -. DR PDBsum; 1FCE; -. DR PDBsum; 1G9G; -. DR PDBsum; 1G9J; -. DR PDBsum; 2QNO; -. DR AlphaFoldDB; P37698; -. DR SMR; P37698; -. DR STRING; 394503.Ccel_0729; -. DR DrugBank; DB03857; 1,4-dithio-beta-D-glucopyranose. DR DrugBank; DB03584; 4-Thio-beta-D-glucopyranose. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB02252; Iodobenzene. DR DrugBank; DB01642; methyl beta-D-glucopyranoside. DR CAZy; GH48; Glycoside Hydrolase Family 48. DR KEGG; cce:Ccel_0729; -. DR eggNOG; COG5297; Bacteria. DR HOGENOM; CLU_009014_1_0_9; -. DR OrthoDB; 33861at2; -. DR BRENDA; 3.2.1.4; 1468. DR EvolutionaryTrace; P37698; -. DR Proteomes; UP000001349; Chromosome. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR CDD; cd14256; Dockerin_I; 1. DR Gene3D; 1.50.10.10; -; 1. DR Gene3D; 1.10.1330.10; Dockerin domain; 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 InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR002105; Dockerin_1_rpt. DR InterPro; IPR016134; Dockerin_dom. DR InterPro; IPR036439; Dockerin_dom_sf. DR InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2. DR InterPro; IPR027390; Endoglucanase_F_dom3. DR InterPro; IPR000556; Glyco_hydro_48F. DR Pfam; PF00404; Dockerin_1; 1. DR Pfam; PF02011; Glyco_hydro_48; 1. DR PRINTS; PR00844; GLHYDRLASE48. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. DR SUPFAM; SSF63446; Type I dockerin domain; 1. DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2. DR PROSITE; PS51766; DOCKERIN; 1. DR PROSITE; PS00018; EF_HAND_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..722 FT /note="Endoglucanase F" FT /id="PRO_0000008026" FT DOMAIN 661..722 FT /note="Dockerin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102" FT REGION 142..165 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 150..165 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT HELIX 36..50 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 73..77 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 83..100 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 104..116 FT /evidence="ECO:0007829|PDB:1G9G" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 166..173 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 174..177 FT /evidence="ECO:0007829|PDB:2QNO" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 202..207 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 223..227 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 251..256 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 258..276 FT /evidence="ECO:0007829|PDB:1G9G" FT TURN 277..279 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 283..295 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 296..300 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 310..314 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 330..337 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 346..349 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 355..363 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 365..367 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 374..391 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 402..407 FT /evidence="ECO:0007829|PDB:1G9G" FT TURN 408..411 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 424..429 FT /evidence="ECO:0007829|PDB:1G9G" FT TURN 433..438 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 442..458 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 461..475 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 486..496 FT /evidence="ECO:0007829|PDB:1G9G" FT TURN 503..505 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 514..521 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 524..541 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 544..560 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 561..563 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 570..572 FT /evidence="ECO:0007829|PDB:1G9G" FT TURN 574..577 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 578..581 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 606..609 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 611..615 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 619..627 FT /evidence="ECO:0007829|PDB:1G9G" FT STRAND 633..635 FT /evidence="ECO:0007829|PDB:1G9G" FT HELIX 639..655 FT /evidence="ECO:0007829|PDB:1G9G" SQ SEQUENCE 722 AA; 80544 MW; 5E48F85319D70AE5 CRC64; MSKNFKRVGA VAVAAAMSLS IMATTSINAA SSPANKVYQD RFESMYSKIK DPANGYFSEQ GIPYHSIETL MVEAPDYGHV TTSEAMSYYM WLEAMHGRFS GDFTGFDKSW SVTEQYLIPT EKDQPNTSMS RYDANKPATY APEFQDPSKY PSPLDTSQPV GRDPINSQLT SAYGTSMLYG MHWILDVDNW YGFGARADGT SKPSYINTFQ RGEQESTWET IPQPCWDEHK FGGQYGFLDL FTKDTGTPAK QFKYTNAPDA DARAVQATYW ADQWAKEQGK SVSTSVGKAT KMGDYLRYSF FDKYFRKIGQ PSQAGTGYDA AHYLLSWYYA WGGGIDSTWS WIIGSSHNHF GYQNPFAAWV LSTDANFKPK SSNGASDWAK SLDRQLEFYQ WLQSAEGAIA GGATNSWNGR YEAVPSGTST FYGMGYVENP VYADPGSNTW FGMQVWSMQR VAELYYKTGD ARAKKLLDKW AKWINGEIKF NADGTFQIPS TIDWEGQPDT WNPTQGYTGN ANLHVKVVNY GTDLGCASSL ANTLTYYAAK SGDETSRQNA QKLLDAMWNN YSDSKGISTV EQRGDYHRFL DQEVFVPAGW TGKMPNGDVI KSGVKFIDIR SKYKQDPEWQ TMVAALQAGQ VPTQRLHRFW AQSEFAVANG VYAILFPDQG PEKLLGDVNG DETVDAIDLA ILKKYLLNSS TTINTANADM NSDNAIDAID YALLKKALLS IQ //