P22534 · GUNA_CALSA
- ProteinEndoglucanase A
- GenecelA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1742 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
The N-terminal domain of CelA codes for an endoglucanase activity on carboxymethylcellulose. The C-terminal domain probably acts synergistically to hydrolyze crystalline cellulose.
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 80 | Nucleophile | ||||
Sequence: D | ||||||
Active site | 396 | |||||
Sequence: H | ||||||
Active site | 434 | |||||
Sequence: D | ||||||
Active site | 443 | |||||
Sequence: E |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | cellulase activity | |
Molecular Function | cellulose binding | |
Biological Process | cellulose catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEndoglucanase A
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageBacteria > Bacillota > Bacillota incertae sedis > Caldicellulosiruptorales > Caldicellulosiruptoraceae > Caldicellulosiruptor
Accessions
- Primary accessionP22534
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MVVTFLFILGVVYGVKPWQEARA | ||||||
Chain | PRO_0000007944 | 24-1742 | Endoglucanase A | |||
Sequence: GSFNYGEALQKAIMFYEFQMSGKLPNWVRNNWRGDSALKDGQDNGLDLTGGWFDAGDHVKFNLPMSYTGTMLSWAAYEYKDAFVKSGQLEHILNQIEWVNDYFVKCHPSKYVYYYQVGDGGKDHAWWGPAEVMQMERPSFKVTQSSPGSAVVAETAASLAAASIVLKDRNPTKAATYLQHAKDLYEFAEVTKSDSGYTAANGYYNSWSGFYDELSWAAVWLYLATNDSTYLTKAESYVQNWPKISGSNIIDYKWAHCWDDVHNGAALLLAKITDKDTYKQIIESHLDYWTTGYNGERIKYTPKGLAWLDQWGSLRYATTTAFLAFVYSDWSGCPTGKKETYRKFGESQIDYALGSTGRSFVVGFGTNPPKRPHHRTAHSSWADSQSIPSYHRHTLYGALVGGPGSDDSYTDDISNYVNNEVACDYNAGFVGALAKMYLLYGGNPIPDFKAIETPTNDEFFVEAGINASGTNFIEIKAIVNNQSGWPARATNKLKFRYFVDLSELIKAGYSPNQLTLSTNYNQGAKVSGPYVWDSSRNIYYILVDFTGTLIYPGGQDKYKKEVQFRIAAPQNVQWDNSNDYSFQDIKGVSSGSVVKTKYIPLYDEDIKVWGEEPGTSGVSPTPTASVTPTPTPTPTATPTPTPTPTVTPTPTVTATPTPTPTPTSTPTVTPTPTPVSTPATSGQIKVLYANKETNSTTNTIRPWLKVVNSGSSSIDLSRVTIRYWYTVDGERAQSAISDWAQIGASNVTFKFVKLSSSVSGADYYLEIGFKSGAGQLQPGKDTGEIQIRFNKDDWSNYNQGNDWSWIQSMTSYGENEKVTAYIDGVLVWGQEPSGTTPAPTSTPTVTVTPTPTPTPTVTPTPTVTATPTPTPTPTSTPVSTPATGGQIKVLYANKETNSTTNTIRPWLKVVNSGSSSIDLSRVTIRYWYTVDGERAQSAISDWAQIGASNVTFKFVKLSSSVSGADYYLEIGFKSGAGQLQPGKDTGEIQIRFNKDDWSNYNQGNDWSWIQSMTSYGENEKVTAYIDGVLVWGQEPSGATPAPTVTPTPTVTPTPTPAPTPTATPTPTPTPTVTPTPTVAPTPTPSSTPSGLGKYGQRFMWLWNKIHDPASGYFNQDGIPYHSVETLICEAPDYGHLTTSEAFSYYVWLEAVYGKLTGDWSKFKTAWDTLEKYMIPSAEDQPMRSYDPNKPATYAGEWETPDKYPSPLEFNVPVGKDPLHNELVSTYGSTLMYGMHWLMDVDNWYGYGKRGDGVSRASFINTFQRGPEESVWETVPHPSWEEFKWGGPNGFLDLFIKDQNYSKQWRYTNAPDADARAIQATYWAKVWAKEQGKFNEISSYVGKAAKMGDYLRYAMFDKYFKPLGCQDKNAAGGTGYDSAHYLLSWYYAWGGALDGAWSWKIGCSHAHFGYQNPMAAWALANDSDMKPKSPNGASDWAKSLKRQIEFYRWLQSAEGAIAGGATNSWNGRYEKYPAGTATFYGMAYEPNPVYRDPGSNTWFGFQAWSMQRVAEYYYVTGDKDAGTLLEKWVSWIKSVVKLNSDGTFAIPSTLDWSGQPDTWNGTYTGNPNLHVKVVDYGTDLGITASLANALLYYSAGTKKYGVFDEEAKNLAKELLDRMWKLYRDEKGLSAPEKRADYKRFFEQEVYIPAGWTGKMPNGDVIKSGVKFIDIRSKYKQDPDWPKLEAAYKSGQVPEFRYHRFWAQCDIAIVNATYEILFGNQ |
Post-translational modification
The linker region (also termed 'hinge') may be a potential site for proteolysis.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 24-476 | Catalytic 1 | ||||
Sequence: GSFNYGEALQKAIMFYEFQMSGKLPNWVRNNWRGDSALKDGQDNGLDLTGGWFDAGDHVKFNLPMSYTGTMLSWAAYEYKDAFVKSGQLEHILNQIEWVNDYFVKCHPSKYVYYYQVGDGGKDHAWWGPAEVMQMERPSFKVTQSSPGSAVVAETAASLAAASIVLKDRNPTKAATYLQHAKDLYEFAEVTKSDSGYTAANGYYNSWSGFYDELSWAAVWLYLATNDSTYLTKAESYVQNWPKISGSNIIDYKWAHCWDDVHNGAALLLAKITDKDTYKQIIESHLDYWTTGYNGERIKYTPKGLAWLDQWGSLRYATTTAFLAFVYSDWSGCPTGKKETYRKFGESQIDYALGSTGRSFVVGFGTNPPKRPHHRTAHSSWADSQSIPSYHRHTLYGALVGGPGSDDSYTDDISNYVNNEVACDYNAGFVGALAKMYLLYGGNPIPDFKAIET | ||||||
Domain | 477-637 | CBM3 1 | ||||
Sequence: PTNDEFFVEAGINASGTNFIEIKAIVNNQSGWPARATNKLKFRYFVDLSELIKAGYSPNQLTLSTNYNQGAKVSGPYVWDSSRNIYYILVDFTGTLIYPGGQDKYKKEVQFRIAAPQNVQWDNSNDYSFQDIKGVSSGSVVKTKYIPLYDEDIKVWGEEPG | ||||||
Region | 634-703 | Disordered | ||||
Sequence: EEPGTSGVSPTPTASVTPTPTPTPTATPTPTPTPTVTPTPTVTATPTPTPTPTSTPTVTPTPTPVSTPAT | ||||||
Region | 638-702 | Linker ('hinge') (Pro-Thr box) | ||||
Sequence: TSGVSPTPTASVTPTPTPTPTATPTPTPTPTVTPTPTVTATPTPTPTPTSTPTVTPTPTPVSTPA | ||||||
Compositional bias | 648-696 | Pro residues | ||||
Sequence: SVTPTPTPTPTATPTPTPTPTVTPTPTVTATPTPTPTPTSTPTVTPTPT | ||||||
Domain | 703-856 | CBM3 2 | ||||
Sequence: TSGQIKVLYANKETNSTTNTIRPWLKVVNSGSSSIDLSRVTIRYWYTVDGERAQSAISDWAQIGASNVTFKFVKLSSSVSGADYYLEIGFKSGAGQLQPGKDTGEIQIRFNKDDWSNYNQGNDWSWIQSMTSYGENEKVTAYIDGVLVWGQEPS | ||||||
Region | 855-906 | Disordered | ||||
Sequence: PSGTTPAPTSTPTVTVTPTPTPTPTVTPTPTVTATPTPTPTPTSTPVSTPAT | ||||||
Region | 857-905 | Linker ('hinge') (Pro-Thr box) | ||||
Sequence: GTTPAPTSTPTVTVTPTPTPTPTVTPTPTVTATPTPTPTPTSTPVSTPA | ||||||
Compositional bias | 867-899 | Pro residues | ||||
Sequence: TVTVTPTPTPTPTVTPTPTVTATPTPTPTPTST | ||||||
Domain | 906-1059 | CBM3 3 | ||||
Sequence: TGGQIKVLYANKETNSTTNTIRPWLKVVNSGSSSIDLSRVTIRYWYTVDGERAQSAISDWAQIGASNVTFKFVKLSSSVSGADYYLEIGFKSGAGQLQPGKDTGEIQIRFNKDDWSNYNQGNDWSWIQSMTSYGENEKVTAYIDGVLVWGQEPS | ||||||
Region | 1059-1113 | Disordered | ||||
Sequence: SGATPAPTVTPTPTVTPTPTPAPTPTATPTPTPTPTVTPTPTVAPTPTPSSTPSG | ||||||
Region | 1060-1112 | Linker ('hinge') (Pro-Thr box) | ||||
Sequence: GATPAPTVTPTPTVTPTPTPAPTPTATPTPTPTPTVTPTPTVAPTPTPSSTPS | ||||||
Compositional bias | 1064-1106 | Pro residues | ||||
Sequence: APTVTPTPTVTPTPTPAPTPTATPTPTPTPTVTPTPTVAPTPT | ||||||
Region | 1113-1742 | Catalytic 2 | ||||
Sequence: GLGKYGQRFMWLWNKIHDPASGYFNQDGIPYHSVETLICEAPDYGHLTTSEAFSYYVWLEAVYGKLTGDWSKFKTAWDTLEKYMIPSAEDQPMRSYDPNKPATYAGEWETPDKYPSPLEFNVPVGKDPLHNELVSTYGSTLMYGMHWLMDVDNWYGYGKRGDGVSRASFINTFQRGPEESVWETVPHPSWEEFKWGGPNGFLDLFIKDQNYSKQWRYTNAPDADARAIQATYWAKVWAKEQGKFNEISSYVGKAAKMGDYLRYAMFDKYFKPLGCQDKNAAGGTGYDSAHYLLSWYYAWGGALDGAWSWKIGCSHAHFGYQNPMAAWALANDSDMKPKSPNGASDWAKSLKRQIEFYRWLQSAEGAIAGGATNSWNGRYEKYPAGTATFYGMAYEPNPVYRDPGSNTWFGFQAWSMQRVAEYYYVTGDKDAGTLLEKWVSWIKSVVKLNSDGTFAIPSTLDWSGQPDTWNGTYTGNPNLHVKVVDYGTDLGITASLANALLYYSAGTKKYGVFDEEAKNLAKELLDRMWKLYRDEKGLSAPEKRADYKRFFEQEVYIPAGWTGKMPNGDVIKSGVKFIDIRSKYKQDPDWPKLEAAYKSGQVPEFRYHRFWAQCDIAIVNATYEILFGNQ |
Sequence similarities
In the C-terminal section; belongs to the glycosyl hydrolase 48 (cellulase L) family.
In the N-terminal section; belongs to the glycosyl hydrolase 9 (cellulase E) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,742
- Mass (Da)193,697
- Last updated1996-10-01 v2
- Checksum3F0699A2123EED07
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 648-696 | Pro residues | ||||
Sequence: SVTPTPTPTPTATPTPTPTPTVTPTPTVTATPTPTPTPTSTPTVTPTPT | ||||||
Compositional bias | 867-899 | Pro residues | ||||
Sequence: TVTVTPTPTPTPTVTPTPTVTATPTPTPTPTST | ||||||
Compositional bias | 1064-1106 | Pro residues | ||||
Sequence: APTVTPTPTVTPTPTPAPTPTATPTPTPTPTVTPTPTVAPTPT | ||||||
Sequence conflict | 1545 | in Ref. 2; AAA72860 | ||||
Sequence: T → A |