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Protein

Beta-glucanase

Gene

licB

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei136NucleophilePROSITE-ProRule annotation1
Active sitei140Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.73. 1530.

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucanase (EC:3.2.1.73)
Alternative name(s):
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Endo-beta-1,3-1,4 glucanase
Laminarinase
Lichenase
Gene namesi
Name:licB
Synonyms:lam1
OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001179228 – 334Beta-glucanaseAdd BLAST307

Proteomic databases

PRIDEiQ84C00.

Interactioni

Protein-protein interaction databases

STRINGi203119.Cthe_0211.

Structurei

3D structure databases

ProteinModelPortaliQ84C00.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 248GH16PROSITE-ProRule annotationAdd BLAST221
Domaini267 – 334DockerinPROSITE-ProRule annotationAdd BLAST68

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi252 – 269Pro/Thr-rich (linker)Add BLAST18

Sequence similaritiesi

Belongs to the glycosyl hydrolase 16 family.Curated
Contains 1 dockerin domain.PROSITE-ProRule annotation
Contains 1 GH16 (glycosyl hydrolase family 16) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108RZ2. Bacteria.
COG2273. LUCA.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR013320. ConA-like_dom.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR000757. GH16.
IPR008263. GH16_AS.
[Graphical view]
PfamiPF00404. Dockerin_1. 2 hits.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS01034. GH16_1. 1 hit.
PS51762. GH16_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q84C00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE
60 70 80 90 100
KADWANGSVF NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRSKSF
110 120 130 140 150
FGYGYYEVRM KAAKNVGIVS SFFTYTGPSD NNPWDEIDIE FLGKDTTKAQ
160 170 180 190 200
FNWYKNEVGG NEYLHNLGFD ASQDFHTYGF EWRPDYIDFY VDGKKVYRGT
210 220 230 240 250
RNIPVTPGKI MMNLWPGKGV DEWLGRYDGR TPLQAEYEYV KYYPNGVPQD
260 270 280 290 300
NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP
310 320 330
VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL
Length:334
Mass (Da):37,942
Last modified:June 1, 2003 - v1
Checksum:i3079DEF1CEE5A664
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti97S → T in CAA41281 (PubMed:1755832).Curated1
Sequence conflicti97S → T (Ref. 2) Curated1
Sequence conflicti149A → V in CAA41281 (PubMed:1755832).Curated1
Sequence conflicti149A → V (Ref. 2) Curated1
Sequence conflicti157E → G in CAA41281 (PubMed:1755832).Curated1
Sequence conflicti157E → G (Ref. 2) Curated1
Sequence conflicti218K → I in CAA41281 (PubMed:1755832).Curated1
Sequence conflicti218K → I (Ref. 2) Curated1
Sequence conflicti304 – 334QSVAD…AIPSL → PQDGCGRHDRVVDSGSK in CAA41281 (PubMed:1755832).CuratedAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58392 Genomic DNA. Translation: CAA41281.1.
AY225318 Genomic DNA. Translation: AAO74890.1.
PIRiJS0611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58392 Genomic DNA. Translation: CAA41281.1.
AY225318 Genomic DNA. Translation: AAO74890.1.
PIRiJS0611.

3D structure databases

ProteinModelPortaliQ84C00.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203119.Cthe_0211.

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Proteomic databases

PRIDEiQ84C00.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108RZ2. Bacteria.
COG2273. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.73. 1530.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR013320. ConA-like_dom.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR000757. GH16.
IPR008263. GH16_AS.
[Graphical view]
PfamiPF00404. Dockerin_1. 2 hits.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS01034. GH16_1. 1 hit.
PS51762. GH16_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUB_CLOTM
AccessioniPrimary (citable) accession number: Q84C00
Secondary accession number(s): P29716, P37074
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: June 1, 2003
Last modified: October 5, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.