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Database: UniProt
Entry: U2LXH1_9FIRM
LinkDB: U2LXH1_9FIRM
Original site: U2LXH1_9FIRM 
ID   U2LXH1_9FIRM            Unreviewed;       847 AA.
AC   U2LXH1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=RUMCAL_02514 {ECO:0000313|EMBL:ERJ91803.1};
OS   Ruminococcus callidus ATCC 27760.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ91803.1, ECO:0000313|Proteomes:UP000016662};
RN   [1] {ECO:0000313|EMBL:ERJ91803.1, ECO:0000313|Proteomes:UP000016662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ91803.1,
RC   ECO:0000313|Proteomes:UP000016662};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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:ERJ91803.1}.
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DR   EMBL; AWVF01000300; ERJ91803.1; -; Genomic_DNA.
DR   RefSeq; WP_021680680.1; NZ_KI260297.1.
DR   AlphaFoldDB; U2LXH1; -.
DR   STRING; 411473.RUMCAL_02514; -.
DR   GeneID; 78474313; -.
DR   PATRIC; fig|411473.3.peg.2103; -.
DR   eggNOG; COG4733; Bacteria.
DR   HOGENOM; CLU_008926_0_2_9; -.
DR   OrthoDB; 2078139at2; -.
DR   Proteomes; UP000016662; Unassembled WGS sequence.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide 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; 2.60.40.710; Endoglucanase-like; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS51766; DOCKERIN; 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|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..847
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039000301"
FT   DOMAIN          538..706
FT                   /note="CBM3"
FT                   /evidence="ECO:0000259|PROSITE:PS51172"
FT   DOMAIN          776..844
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000259|PROSITE:PS51766"
FT   REGION          733..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  93880 MW;  CDB8E920F4684FD6 CRC64;
     MKRFSKGSKR LLSVLLSGAM LAGTCSSVAV GAADEKEANF ARALQYSIYF YDGNMCGTEV
     QDNNRYTWRG NCHTYDAQVA MNSTATNLSA DFLTKYKDIL DPDGDGYIDV AGGFHDAGDH
     VKFGMPENYS AATLGWGYYE FRDAYQKTGQ DDHIETILRY FNDYLMKCTF LDSNGDVIAH
     CYQVGDGDID HAYWNAPELD EMDRPAFFLT GDKPQTDYVA SAAASLAINY LNFKDTDPEY
     AQKSLDYATA LYKFAETHEK QLSDNGDGPK AYYNSSKWED DYCWASAWMY KITGDHHYLE
     QIFPYYDYYA APCYVYCWND VWGGVQCILG EITSEQYPNF IDEYKKAAGK SPYEEMNCWS
     SVAEALNKYM TGGVGTITPA GYFWLNTWGS ARYNAAAQMM ALVYDKYNNN GKPGEYSEWA
     KGQMEYLLGD NPMNRAYEVG YDETAAKFPH HRAASGLTKC EDTDEQKHVL YGALVGGPDA
     QDKHNDITAD WIYNEVTIDY NAAFVGACAG LYDYYGTDAM EITPDFPPED KNSGSDNGGN
     DFWVDAYAVD DIQTSGAGVT KLAIQMRTNS ITPKTDLSMR YYFSIAEMEN KSNISKVTGN
     ELYDQASVEA APADGVISGP YQYDASYDPD IYYVEVKWDG YKIANSNKKY QFTVGLYYGD
     KWDPTNDWSY QGITKCKDTY QDGSETRTDY ICVYSNGELV GGIEPNGNKP AVTTTTTPAE
     TTITTTKTTT VTTKATSTSA ETTTTEQTSS AAPSTDTTET TANTTKTSES GSDVTPSVMY
     GDVNLDGRID VTDAVLLNKM AAGAVTGNDQ QRRAGDCNVD GEVDTADSVM LLQFLVHIIQ
     YLGPQAK
//
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