SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P55297

- MANB_PIRSP

UniProt

P55297 - MANB_PIRSP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Mannan endo-1,4-beta-mannosidase B

Gene
MANB
Organism
Piromyces sp.
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. cellulase activity Source: InterPro
  3. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. substituted mannan metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.
mycoCLAPiMAN26B_PIRSP.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase B (EC:3.2.1.78)
Alternative name(s):
1,4-beta-D-mannan mannanohydrolase B
Beta-mannanase B
Gene namesi
Name:MANB
OrganismiPiromyces sp.
Taxonomic identifieri45796 [NCBI]
Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed predictionAdd
BLAST
Chaini20 – 571552Mannan endo-1,4-beta-mannosidase BPRO_0000012175Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP55297.
SMRiP55297. Positions 534-571.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 141120CBM6Add
BLAST
Domaini491 – 52636CBM10 1Add
BLAST
Domaini535 – 57036CBM10 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi475 – 4795Poly-Asn
Compositional biasi482 – 4887Poly-Asn

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
3.90.1220.10. 2 hits.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR005084. CMB_fam6.
IPR009034. Dockerin_dom_fun.
IPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 2 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF64571. SSF64571. 2 hits.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P55297-1 [UniParc]FASTAAdd to Basket

« Hide

MNSLSLLLFC IFFVFSTFAK KVYYEAENGK LDGVTVYKSD LTGFSGTGYV    50
GRFENPGNSV TVTVEVPQTG MYDLTIVYCA NMGQKINSLT VNGQSAGDIT 100
FTENTKFEDL NVGAIYLNKG KNTIGLVSSW GWMWVDAFVI NDAPNAAKDV 150
TSKLNPTLIN PKAIPAAKKL YDFLKTNYGK RILSGQVGAA GQAGDEGQEI 200
QRIQKATGKL PAVWNMDFIF ESNDCTWRPQ NPDITEMAIN WWKKYQGKGI 250
MSAQWHWNIA GKTGDFAFYK KDTTFSIDNA VTEGTWEYEK IIKDIDRVAG 300
HIKKLQAVNM PLIWRPLHEN DGDWFWWGNN PKSCAKLWKI LYERMVNYHG 350
LNNLIWLWNG KNDANTPVDY IDIIGVDIYA NDHGPQTTAY NTHFDFYGGK 400
KMVVLSENGR IPDIQQCVDQ NAWWGYFQTW NSEFILQDSY HTDAQLKEYF 450
THKTVMNMDE LPSFNVNSYE YQSGNNNNNS SNNNNNNNSS ECFSIPLGYP 500
CCKGNTVVYT DNDGDWGVEN NEWCGIGNSS SAVVCWSEAL GYPCCVSSSD 550
VYYTDNDGEW GVENGDWCGI I 571
Length:571
Mass (Da):64,397
Last modified:October 1, 1996 - v1
Checksum:iB13E44581FAA9DAA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97408 mRNA. Translation: CAA66061.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97408 mRNA. Translation: CAA66061.1 .

3D structure databases

ProteinModelPortali P55297.
SMRi P55297. Positions 534-571.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.
mycoCLAPi MAN26B_PIRSP.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
3.90.1220.10. 2 hits.
InterProi IPR002883. CBM10/Dockerin_dom.
IPR005084. CMB_fam6.
IPR009034. Dockerin_dom_fun.
IPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02013. CBM_10. 2 hits.
PF02156. Glyco_hydro_26. 1 hit.
[Graphical view ]
PRINTSi PR00739. GLHYDRLASE26.
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF64571. SSF64571. 2 hits.
PROSITEi PS51175. CBM6. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evidence that the Piromyces gene family encoding endo-1,4-mannanases arose through gene duplication."
    Millward-Sadler S.J., Hall J., Black G.W., Hazlewood G.P., Gilbert H.J.
    FEMS Microbiol. Lett. 141:183-188(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMANB_PIRSP
AccessioniPrimary (citable) accession number: P55297
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

External Data

Dasty 3

Similar proteinsi