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Protein
Submitted name:

Endoglucanase

Gene

cel12A

Organism
Trichoderma citrinoviride
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradationUniRule annotation

Protein family/group databases

CAZyiGH12. Glycoside Hydrolase Family 12.
mycoCLAPiEGL12A_HYPSC.

Names & Taxonomyi

Protein namesi
Submitted name:
EndoglucanaseImported
Gene namesi
Name:cel12AImported
OrganismiTrichoderma citrinovirideImported
Taxonomic identifieri58853 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 234218Sequence analysisPRO_5004311273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Pyrrolidone carboxylic acidCombined sources
Disulfide bondi20 ↔ 48Combined sources
Glycosylationi180 – 1801N-linked (GlcNAc...)Combined sourcesCAR_5005390047

Keywords - PTMi

Pyrrolidone carboxylic acidCombined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OA3X-ray1.70A/B/C/D17-234[»]
ProteinModelPortaliQ8NJY6.
SMRiQ8NJY6. Positions 17-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NJY6.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 12 (cellulase H) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR002594. GH12.
[Graphical view]
PfamiPF01670. Glyco_hydro_12. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8NJY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLQVLPAI LPAALAQTSC DQYATFSGNG YIVSNNLWGA SAGSGFGCVT
60 70 80 90 100
SVSLNGAASW HADWQWSGGQ NNVKSYQNVQ INIPQKRTVN SIGSMPTTAS
110 120 130 140 150
WSYSGSDIRA NVAYDLFTAA NPNHVTYSGD YELMIWLGKY GDIGPIGSSQ
160 170 180 190 200
GTVNVGGQTW TLYYGYNGAM QVYSFVAQSN TTSYSGDVKN FFNYLRDNKG
210 220 230
YNAGGQYVLS YQFGTEPFTG SGTLNVASWT ASIN
Length:234
Mass (Da):25,176
Last modified:October 1, 2002 - v1
Checksum:i909A1D3295D6C3B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF435068 Genomic DNA. Translation: AAM77711.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF435068 Genomic DNA. Translation: AAM77711.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OA3X-ray1.70A/B/C/D17-234[»]
ProteinModelPortaliQ8NJY6.
SMRiQ8NJY6. Positions 17-234.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH12. Glycoside Hydrolase Family 12.
mycoCLAPiEGL12A_HYPSC.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NJY6.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR002594. GH12.
[Graphical view]
PfamiPF01670. Glyco_hydro_12. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and relational analysis of 15 novel fungal endoglucanases from family 12 glycosyl hydrolase."
    Goedegebuur F., Fowler T., Phillips J., van der Kley P., van Solingen P., Dankmeyer L., Power S.D.
    Curr. Genet. 41:89-98(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability."
    Sandgren M., Gualfetti P.J., Shaw A., Gross L.S., Saldajeno M., Day A.G., Jones T.A., Mitchinson C.
    Protein Sci. 12:848-860(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 17-234, PYRROLIDONE CARBOXYLIC ACID AT GLN-17, GLYCOSYLATION AT ASN-180, DISULFIDE BONDS.

Entry informationi

Entry nameiQ8NJY6_9HYPO
AccessioniPrimary (citable) accession number: Q8NJY6
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2002
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.