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Database: UniProt
Entry: Q04ND1_LEPBJ
LinkDB: Q04ND1_LEPBJ
Original site: Q04ND1_LEPBJ 
ID   Q04ND1_LEPBJ            Unreviewed;       654 AA.
AC   Q04ND1;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Cellulase (Glycosyl hydrolase family 5) domain protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=LBJ_4208 {ECO:0000313|EMBL:ABJ77589.1};
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ77589.1, ECO:0000313|Proteomes:UP000000656};
RN   [1] {ECO:0000313|EMBL:ABJ77589.1, ECO:0000313|Proteomes:UP000000656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197 {ECO:0000313|EMBL:ABJ77589.1,
RC   ECO:0000313|Proteomes:UP000000656};
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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DR   EMBL; CP000351; ABJ77589.1; -; Genomic_DNA.
DR   RefSeq; WP_011672210.1; NC_008511.1.
DR   AlphaFoldDB; Q04ND1; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   KEGG; lbj:LBJ_4208; -.
DR   HOGENOM; CLU_009024_1_0_12; -.
DR   Proteomes; UP000000656; Chromosome 2.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:1901136; P:carbohydrate derivative catabolic process; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR041036; GH5_C.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31308; -; 1.
DR   PANTHER; PTHR31308:SF5; ERGOSTERYL-BETA-GLUCOSIDASE; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF18564; Glyco_hydro_5_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          64..243
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   DOMAIN          546..616
FT                   /note="Glycoside hydrolase family 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18564"
SQ   SEQUENCE   654 AA;  76484 MW;  C16109F8CE5D227E CRC64;
     MEELFVKNGH FASKDGTIYQ LRGVNLSGSA KLPSKPDGTT HFDQTLTFLN HRNVSFVGRP
     LEEKQASEHF DRLRKWGFNF LRFLITWEAI EHKGPGKYDT EYIDYVERMV SLAGQKGFYL
     FIDPHQDVWS RFTGGDGAPG WTLEEIGMDI SKIQGSETAI VHHHQGRHYR RMSWPLNYQK
     YVCGTMFSLF FGGKEFAPNT KIDGKNAQDF LQDHYIDSVL KIVRKLKKYK NVIGFDTLNE
     PSPGWIGKRN LGEFEGFGFG KVIKTSPFKE MYLSEGRTVS TEQAYMLGFW SFPWGKVRLN
     DGGVSLWKRG YQCVWRDHRV WDYDPNGAPM MLKPEYFYKR NGKKYEFYSD FMHPFIKKLK
     EAVQRVESRF HIFVESDPSK LELEWKEIPK KNYGSVVNAT HWYDISVLML KRYFPWFGVH
     VFKQKPVFGK ENVDRAYEET VRMIREMSEK KMGNCPTVIG ETGIPMDINH SIAYHKKDYR
     ILEQALDRVM KAVEKNFVHL ALWNYTPDHT HSLGDRWNEE DLSIYSEDTP TSYDEDGGRA
     VRAFSRPYPI RTKGLPVALS FDMERSLFKY SFRQEGDVLP ETEIFIPEIH YKNGFEVSIN
     AGKYHYDSRT KVLKFKGEKG VIHYGITIHS SKKSLFREQD RTKVVPNTQK RNIR
//
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