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Conserved domains on  [gi|575878312|gb|AHH02585|]
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glycosyl hydrolase family 5 mannanase [Exiguobacterium sp. HJ18]

Protein Classification

glycoside hydrolase family 5 protein( domain architecture ID 11457687)

glycoside hydrolase family 5 (GH5) protein may act as glucan 1,3-beta-glucosidase, which catalyzes successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose

CATH:  3.20.20.80
CAZY:  GH5
EC:  3.2.1.-
Gene Ontology:  GO:0004553|GO:0071704|GO:0000272
SCOP:  4003164

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
13-326 2.15e-53

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 177.93  E-value: 2.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  13 DNNQVHFRGFTLTALYWENPEVvTSLYPTDDIYRRMSEMGANTVRLTVHYRLFEDDAAPFQYKQDGLVWLDRQIQFAASH 92
Cdd:COG2730    1 AAMGPRLRGVNLGNWLELWFET-LWGNITEEDIDAIADWGFNTVRLPVSWERLQDPDNPYTLDEAYLERVDEVVDWAKAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  93 GLYVILCL-ILPPGGDWMDEKPeldfslwedatkQERFIRLWEMLTKRYRGTDlgeAIAAFDLFNAPatNDSSGQAYRAL 171
Cdd:COG2730   80 GLYVILDLhHAPGYQGWYDAAT------------QERFIAFWRQLAERYKDYP---NVLGFELLNEP--HGATWADWNAL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312 172 AVRTVERLRRIDADRLFIIgklyGTNGINHDKELETFIQLDAPNLIYDAHFYAPFLYTHQYAdWVSvhgeggrypdsdma 251
Cdd:COG2730  143 AQRAIDAIRATNPDRLIIV----EGNNWGGAHNLRALDPLDDDNLVYSVHFYGPFVFTHQGA-WFA-------------- 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575878312 252 eyavdGTEYPrdiTYLASRLEHLIRFREQHDVPILVSEFGLIHhcFKNERGGLAYVRDIVQLLRQHEIGYTYWDF 326
Cdd:COG2730  204 -----GPTYP---ANLEARLDNWGDWAADNGVPVFVGEFGAYN--DDPDASRLAWLRDLLDYLEENGIGWTYWSF 268
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
13-326 2.15e-53

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 177.93  E-value: 2.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  13 DNNQVHFRGFTLTALYWENPEVvTSLYPTDDIYRRMSEMGANTVRLTVHYRLFEDDAAPFQYKQDGLVWLDRQIQFAASH 92
Cdd:COG2730    1 AAMGPRLRGVNLGNWLELWFET-LWGNITEEDIDAIADWGFNTVRLPVSWERLQDPDNPYTLDEAYLERVDEVVDWAKAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  93 GLYVILCL-ILPPGGDWMDEKPeldfslwedatkQERFIRLWEMLTKRYRGTDlgeAIAAFDLFNAPatNDSSGQAYRAL 171
Cdd:COG2730   80 GLYVILDLhHAPGYQGWYDAAT------------QERFIAFWRQLAERYKDYP---NVLGFELLNEP--HGATWADWNAL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312 172 AVRTVERLRRIDADRLFIIgklyGTNGINHDKELETFIQLDAPNLIYDAHFYAPFLYTHQYAdWVSvhgeggrypdsdma 251
Cdd:COG2730  143 AQRAIDAIRATNPDRLIIV----EGNNWGGAHNLRALDPLDDDNLVYSVHFYGPFVFTHQGA-WFA-------------- 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575878312 252 eyavdGTEYPrdiTYLASRLEHLIRFREQHDVPILVSEFGLIHhcFKNERGGLAYVRDIVQLLRQHEIGYTYWDF 326
Cdd:COG2730  204 -----GPTYP---ANLEARLDNWGDWAADNGVPVFVGEFGAYN--DDPDASRLAWLRDLLDYLEENGIGWTYWSF 268
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
10-325 7.25e-25

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 101.68  E-value: 7.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312   10 VDEDNNQVHFRGFTLtALYWENPEVvtslyPTDDIYRRMSEMGANTVRLTVHYRLFEDDAAPFQYKQDGLVWLDRQIQFA 89
Cdd:pfam00150   1 VDANGKPVQLRGVTH-GGQWGNPYV-----TTKAMIDLVKDWGFNVVRLPVSWGGYVPNNPDYLIDENWLNRVDEVVDYA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312   90 ASHGLYVILclilppggDWMDEKPELDFSLWEDATKQERFIRLWEMLTKRYRGTDlgeaIAAFDLFNAPATNDSSG--QA 167
Cdd:pfam00150  75 IDNGMYVII--------DWHHDGGWPGDPNGNIDTAKAFFKKIWTQIATRYGNNP----NVIFELMNEPHGNDQATwaDD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  168 YRALAVRTVERLRRIDADRLFIIGklygTNGINHDKELETF-IQLDAPNLIYDAHFYAPFLYTHQYADWVSVhgeggryp 246
Cdd:pfam00150 143 VKDYAQEAIDAIRAAGPNNLIIVG----GNSWSQNPDGAALnDPNDDDNLIYSVHFYAPSDFSGTWFDCEDP-------- 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575878312  247 dsdmaeyavdgteyprdiTYLASRLEHLIRFREQHDVPILVSEFGLIHhcfkNERGGLAYVRDIVQLLRQHEIGYTYWD 325
Cdd:pfam00150 211 ------------------TNLAQRLRAAANWALDNGIPVFIGEFGGGN----ADGPCRDEAEKWLDYLKENGISWTGWS 267
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
273-326 7.75e-03

Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is responsible for Smc3 deacetylation. Smc3 is an important player during the establishment of sister chromatid cohesion. Hos1 belongs to the class I histone deacetylases (HDACs). HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Other class I HDACs are animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.


Pssm-ID: 212543 [Multi-domain]  Cd Length: 294  Bit Score: 37.63  E-value: 7.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 575878312 273 HLIRFREQhdvPILVSEFGLIHHCFKNERGGLAYVRDIV---QLLRQHEIG-YTYWDF 326
Cdd:cd11680   97 HLITQVER---DIAINWYGGRHHAQKSRASGFCYVNDIVlaiLRLRRARFRrVFYLDL 151
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
13-326 2.15e-53

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 177.93  E-value: 2.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  13 DNNQVHFRGFTLTALYWENPEVvTSLYPTDDIYRRMSEMGANTVRLTVHYRLFEDDAAPFQYKQDGLVWLDRQIQFAASH 92
Cdd:COG2730    1 AAMGPRLRGVNLGNWLELWFET-LWGNITEEDIDAIADWGFNTVRLPVSWERLQDPDNPYTLDEAYLERVDEVVDWAKAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  93 GLYVILCL-ILPPGGDWMDEKPeldfslwedatkQERFIRLWEMLTKRYRGTDlgeAIAAFDLFNAPatNDSSGQAYRAL 171
Cdd:COG2730   80 GLYVILDLhHAPGYQGWYDAAT------------QERFIAFWRQLAERYKDYP---NVLGFELLNEP--HGATWADWNAL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312 172 AVRTVERLRRIDADRLFIIgklyGTNGINHDKELETFIQLDAPNLIYDAHFYAPFLYTHQYAdWVSvhgeggrypdsdma 251
Cdd:COG2730  143 AQRAIDAIRATNPDRLIIV----EGNNWGGAHNLRALDPLDDDNLVYSVHFYGPFVFTHQGA-WFA-------------- 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575878312 252 eyavdGTEYPrdiTYLASRLEHLIRFREQHDVPILVSEFGLIHhcFKNERGGLAYVRDIVQLLRQHEIGYTYWDF 326
Cdd:COG2730  204 -----GPTYP---ANLEARLDNWGDWAADNGVPVFVGEFGAYN--DDPDASRLAWLRDLLDYLEENGIGWTYWSF 268
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
10-325 7.25e-25

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 101.68  E-value: 7.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312   10 VDEDNNQVHFRGFTLtALYWENPEVvtslyPTDDIYRRMSEMGANTVRLTVHYRLFEDDAAPFQYKQDGLVWLDRQIQFA 89
Cdd:pfam00150   1 VDANGKPVQLRGVTH-GGQWGNPYV-----TTKAMIDLVKDWGFNVVRLPVSWGGYVPNNPDYLIDENWLNRVDEVVDYA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312   90 ASHGLYVILclilppggDWMDEKPELDFSLWEDATKQERFIRLWEMLTKRYRGTDlgeaIAAFDLFNAPATNDSSG--QA 167
Cdd:pfam00150  75 IDNGMYVII--------DWHHDGGWPGDPNGNIDTAKAFFKKIWTQIATRYGNNP----NVIFELMNEPHGNDQATwaDD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  168 YRALAVRTVERLRRIDADRLFIIGklygTNGINHDKELETF-IQLDAPNLIYDAHFYAPFLYTHQYADWVSVhgeggryp 246
Cdd:pfam00150 143 VKDYAQEAIDAIRAAGPNNLIIVG----GNSWSQNPDGAALnDPNDDDNLIYSVHFYAPSDFSGTWFDCEDP-------- 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575878312  247 dsdmaeyavdgteyprdiTYLASRLEHLIRFREQHDVPILVSEFGLIHhcfkNERGGLAYVRDIVQLLRQHEIGYTYWD 325
Cdd:pfam00150 211 ------------------TNLAQRLRAAANWALDNGIPVFIGEFGGGN----ADGPCRDEAEKWLDYLKENGISWTGWS 267
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
42-115 6.11e-03

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 38.37  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575878312  42 DDIyRRMSEMGANTVRLTV-----------HYRlFEddaapfqykqdglvWLDRQIQFAASHGLYVILC---LILPPggd 107
Cdd:COG1874   28 EDI-RLMKAAGLNTVRIGYfawnlhepeegVFD-FD--------------WLDRFIDLLHEAGLKVILRtptAAPPA--- 88

                 ....*....
gi 575878312 108 WM-DEKPEL 115
Cdd:COG1874   89 WLlKKYPEI 97
HDAC_Hos1 cd11680
Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is ...
273-326 7.75e-03

Class I histone deacetylases Hos1 and related proteins; Saccharomyces cerevisiae Hos1 is responsible for Smc3 deacetylation. Smc3 is an important player during the establishment of sister chromatid cohesion. Hos1 belongs to the class I histone deacetylases (HDACs). HDACs are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Other class I HDACs are animal HDAC1, HDAC2, HDAC3, HDAC8, fungal RPD3 and HOS2, plant HDA9, protist, archaeal and bacterial (AcuC) deacetylases. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.


Pssm-ID: 212543 [Multi-domain]  Cd Length: 294  Bit Score: 37.63  E-value: 7.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 575878312 273 HLIRFREQhdvPILVSEFGLIHHCFKNERGGLAYVRDIV---QLLRQHEIG-YTYWDF 326
Cdd:cd11680   97 HLITQVER---DIAINWYGGRHHAQKSRASGFCYVNDIVlaiLRLRRARFRrVFYLDL 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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