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Conserved domains on  [gi|753727049|gb|AJI22818|]
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glycosyl hydrolases 35 family protein [Priestia megaterium NBRC 15308 = ATCC 14581]

Protein Classification

beta-galactosidase( domain architecture ID 11448998)

beta-galactosidase catalyzes the hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
1-613 0e+00

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


:

Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 631.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049   1 MYIGVDYYPEHWPENMIEEDIQGIKELGSNMVRIGEFAWHLMEPKEGEYDFSFFDSVINKLKKQNIDVMFGTPTATFPAW 80
Cdd:COG1874   10 LILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIGYFAWNLHEPEEGVFDFDWLDRFIDLLHEAGLKVILRTPTAAPPAW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  81 LAKQHPSILSKDENGAVRAFGGRRQYCFNSPLYRKYSAQITEQLVKHYCSEEAIVAWQVDNEFGHEgsdmCYCEQCHKEF 160
Cdd:COG1874   90 LLKKYPEILPVDADGRRRGFGSRRHYCPSSPVYREAARRIVRALAERYGDHPAVIMWQVDNEYGSY----DYCDACAAAF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 161 QQFLERQYKDINELNEKYGTIFWGQTYNEFTEVPMPVKTITTHSPSLKLDWARFRSFSLNRYAHEQTAIVKKYkGDHQLL 240
Cdd:COG1874  166 RDWLRERYGTLDALNEAWGTAFWSQRYTDWDEIEPPRLTPTTANPSLRLDFRRFSSDQVLEYLRAQRDILREA-GPDVPV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 241 TTNVSGGFFDkwFDHEENLEVMDFVSYDNYPVWGGQtepiTPAHIALGHDFNRGLLH-KNFWIVEELMGAQGHDIIGYLP 319
Cdd:COG1874  245 TTNFMGPFPG--LDYWKLARDLDVVSWDNYPDGSAA----DPDEIAFAHDLMRGLKGgGPFMVMEQWPGWVNWGPYNPAK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 320 RPNQAKMWSYQAFAHGCTNMLYFRWRGMTRGAEQYCYGVVGHDNHYGRRYKEVQSLFSEIVHYEHVLESGIKSDVAVLYD 399
Cdd:COG1874  319 RPGQLRLWSLQALAHGADGVNYFQWRPSRGGTEYDHDAPLDHAGRPTRKFREVRELGAELARLPEVPGSRVTARVALLFD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 400 YENIWSWRFQ--QQSEGFDFTQELLRGYTPFYKLNTPIDVIPASRDFSSYKVLVVPALQIIDEELGKRFTEFTENGGVIV 477
Cdd:COG1874  399 WESWWALEIQspPLGQDLGYVDLVRALYRALRRAGVTVDIVPPFADLSGYKLLVAPALYLVSDALAERLLAYVENGGRVN 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 478 FTFRTGIKDKQNNIHfKQTLPGYVKEITGIEIHEVEALSSTQKAAIKGVGpyegeqaSVSVWRDIITPVTAEVLYEYDDP 557
Cdd:COG1874  479 YGPRSGIVDEKDRVR-LGGYPGILRDLLGVRVEEFDPLPPGEPVPLSGGY-------TGWLWYELLPLDGAEVLARYADG 550
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 753727049 558 FY-NQAAVTKNQFGRGTVYYVGCGIEEQTFEKIALDIVKQQHIEHTESEEGIEVYPR 613
Cdd:COG1874  551 FYaGRPAVTRNTFGKGVAWYNGTNLDDWLLAALLARLLAEAGLYPVDLPEGVEAVRR 607
 
Name Accession Description Interval E-value
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
1-613 0e+00

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 631.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049   1 MYIGVDYYPEHWPENMIEEDIQGIKELGSNMVRIGEFAWHLMEPKEGEYDFSFFDSVINKLKKQNIDVMFGTPTATFPAW 80
Cdd:COG1874   10 LILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIGYFAWNLHEPEEGVFDFDWLDRFIDLLHEAGLKVILRTPTAAPPAW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  81 LAKQHPSILSKDENGAVRAFGGRRQYCFNSPLYRKYSAQITEQLVKHYCSEEAIVAWQVDNEFGHEgsdmCYCEQCHKEF 160
Cdd:COG1874   90 LLKKYPEILPVDADGRRRGFGSRRHYCPSSPVYREAARRIVRALAERYGDHPAVIMWQVDNEYGSY----DYCDACAAAF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 161 QQFLERQYKDINELNEKYGTIFWGQTYNEFTEVPMPVKTITTHSPSLKLDWARFRSFSLNRYAHEQTAIVKKYkGDHQLL 240
Cdd:COG1874  166 RDWLRERYGTLDALNEAWGTAFWSQRYTDWDEIEPPRLTPTTANPSLRLDFRRFSSDQVLEYLRAQRDILREA-GPDVPV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 241 TTNVSGGFFDkwFDHEENLEVMDFVSYDNYPVWGGQtepiTPAHIALGHDFNRGLLH-KNFWIVEELMGAQGHDIIGYLP 319
Cdd:COG1874  245 TTNFMGPFPG--LDYWKLARDLDVVSWDNYPDGSAA----DPDEIAFAHDLMRGLKGgGPFMVMEQWPGWVNWGPYNPAK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 320 RPNQAKMWSYQAFAHGCTNMLYFRWRGMTRGAEQYCYGVVGHDNHYGRRYKEVQSLFSEIVHYEHVLESGIKSDVAVLYD 399
Cdd:COG1874  319 RPGQLRLWSLQALAHGADGVNYFQWRPSRGGTEYDHDAPLDHAGRPTRKFREVRELGAELARLPEVPGSRVTARVALLFD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 400 YENIWSWRFQ--QQSEGFDFTQELLRGYTPFYKLNTPIDVIPASRDFSSYKVLVVPALQIIDEELGKRFTEFTENGGVIV 477
Cdd:COG1874  399 WESWWALEIQspPLGQDLGYVDLVRALYRALRRAGVTVDIVPPFADLSGYKLLVAPALYLVSDALAERLLAYVENGGRVN 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 478 FTFRTGIKDKQNNIHfKQTLPGYVKEITGIEIHEVEALSSTQKAAIKGVGpyegeqaSVSVWRDIITPVTAEVLYEYDDP 557
Cdd:COG1874  479 YGPRSGIVDEKDRVR-LGGYPGILRDLLGVRVEEFDPLPPGEPVPLSGGY-------TGWLWYELLPLDGAEVLARYADG 550
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 753727049 558 FY-NQAAVTKNQFGRGTVYYVGCGIEEQTFEKIALDIVKQQHIEHTESEEGIEVYPR 613
Cdd:COG1874  551 FYaGRPAVTRNTFGKGVAWYNGTNLDDWLLAALLARLLAEAGLYPVDLPEGVEAVRR 607
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
6-379 2.83e-141

Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.


Pssm-ID: 396834  Cd Length: 376  Bit Score: 416.67  E-value: 2.83e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049    6 DYYPEHWPENMIEEDIQGIKELGSNMVRIGEFAWHLMEPKEGEYDFSFFDSVINKLKKQNIDVMFGTPTATFPAWLAKQH 85
Cdd:pfam02449   1 DYNPEQWPEETWEEDIRLMKEAGVNVVRIGIFAWAKLEPEEGKYDFEWLDEVIDLLAKAGIKVILATPTAAPPAWLVKKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049   86 PSILSKDENGAVRAFGGRRQYCFNSPLYRKYSAQITEQLVKHYCSEEAIVAWQVDNEFGHEGSDmCYCEQCHKEFQQFLE 165
Cdd:pfam02449  81 PEILPVDADGRRRGFGSRHHYCPSSPVYREYAARIVEALAERYGDHPALIGWHIDNEYGCHVSE-CYCETCERAFRKWLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  166 RQYKDINELNEKYGTIFWGQTYNEFTEVPMPVKTITTHSPSLKLDWARFRSFSLNRYAHEQTAIVKKYKGDhQLLTTNVS 245
Cdd:pfam02449 160 NRYGTIDALNEAWGTAFWSQTYSDFDEIEPPRPAPTFPNPSQILDYRRFSSDQLLEFYRAEREIIREYSPD-IPVTTNFM 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  246 GGFFdKWFDHEENLEVMDFVSYDNYPVWGGQTEPITPAHIALGHDFNRGLL-HKNFWIVEELMGAQGHDIIGYLPRPNQA 324
Cdd:pfam02449 239 GSYF-KDLDYFKWAKELDFVSWDSYPTGDTEPEEEDPDALAFAHDLYRSLKkGKPFWLMEQSPSPVNWAPYNPAKRPGMM 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 753727049  325 KMWSYQAFAHGCTNMLYFRWRGMTRGAEQYCYGVVGHDNH-YGRRYKEVQSLFSEI 379
Cdd:pfam02449 318 RLWSLQAVAHGADAVCYFQWRQSRGGSEKFHSGVLDHDGReDTRVFREVAELGEEL 373
A4_beta-galactosidase_middle_domain cd03143
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; ...
394-492 1.21e-27

A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.


Pssm-ID: 153237 [Multi-domain]  Cd Length: 154  Bit Score: 109.04  E-value: 1.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 394 VAVLYDYENIWSWRFQQQSEGFDFTQELLRGYTPFYKLNTPIDVIPASRDFSSYKVLVVPALQIIDEELGKRFTEFTENG 473
Cdd:cd03143    1 VAIVFDYESWWALELQPQSAGLRYLDLALALYRALRELGIPVDVVPPDADLSGYKLVVLPDLYLLSDATAAALRAYVENG 80
                         90
                 ....*....|....*....
gi 753727049 474 GVIVFTFRTGIKDKQNNIH 492
Cdd:cd03143   81 GTLVAGPRSGAVDEHDAIP 99
 
Name Accession Description Interval E-value
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
1-613 0e+00

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 631.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049   1 MYIGVDYYPEHWPENMIEEDIQGIKELGSNMVRIGEFAWHLMEPKEGEYDFSFFDSVINKLKKQNIDVMFGTPTATFPAW 80
Cdd:COG1874   10 LILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIGYFAWNLHEPEEGVFDFDWLDRFIDLLHEAGLKVILRTPTAAPPAW 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  81 LAKQHPSILSKDENGAVRAFGGRRQYCFNSPLYRKYSAQITEQLVKHYCSEEAIVAWQVDNEFGHEgsdmCYCEQCHKEF 160
Cdd:COG1874   90 LLKKYPEILPVDADGRRRGFGSRRHYCPSSPVYREAARRIVRALAERYGDHPAVIMWQVDNEYGSY----DYCDACAAAF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 161 QQFLERQYKDINELNEKYGTIFWGQTYNEFTEVPMPVKTITTHSPSLKLDWARFRSFSLNRYAHEQTAIVKKYkGDHQLL 240
Cdd:COG1874  166 RDWLRERYGTLDALNEAWGTAFWSQRYTDWDEIEPPRLTPTTANPSLRLDFRRFSSDQVLEYLRAQRDILREA-GPDVPV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 241 TTNVSGGFFDkwFDHEENLEVMDFVSYDNYPVWGGQtepiTPAHIALGHDFNRGLLH-KNFWIVEELMGAQGHDIIGYLP 319
Cdd:COG1874  245 TTNFMGPFPG--LDYWKLARDLDVVSWDNYPDGSAA----DPDEIAFAHDLMRGLKGgGPFMVMEQWPGWVNWGPYNPAK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 320 RPNQAKMWSYQAFAHGCTNMLYFRWRGMTRGAEQYCYGVVGHDNHYGRRYKEVQSLFSEIVHYEHVLESGIKSDVAVLYD 399
Cdd:COG1874  319 RPGQLRLWSLQALAHGADGVNYFQWRPSRGGTEYDHDAPLDHAGRPTRKFREVRELGAELARLPEVPGSRVTARVALLFD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 400 YENIWSWRFQ--QQSEGFDFTQELLRGYTPFYKLNTPIDVIPASRDFSSYKVLVVPALQIIDEELGKRFTEFTENGGVIV 477
Cdd:COG1874  399 WESWWALEIQspPLGQDLGYVDLVRALYRALRRAGVTVDIVPPFADLSGYKLLVAPALYLVSDALAERLLAYVENGGRVN 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 478 FTFRTGIKDKQNNIHfKQTLPGYVKEITGIEIHEVEALSSTQKAAIKGVGpyegeqaSVSVWRDIITPVTAEVLYEYDDP 557
Cdd:COG1874  479 YGPRSGIVDEKDRVR-LGGYPGILRDLLGVRVEEFDPLPPGEPVPLSGGY-------TGWLWYELLPLDGAEVLARYADG 550
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 753727049 558 FY-NQAAVTKNQFGRGTVYYVGCGIEEQTFEKIALDIVKQQHIEHTESEEGIEVYPR 613
Cdd:COG1874  551 FYaGRPAVTRNTFGKGVAWYNGTNLDDWLLAALLARLLAEAGLYPVDLPEGVEAVRR 607
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
6-379 2.83e-141

Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.


Pssm-ID: 396834  Cd Length: 376  Bit Score: 416.67  E-value: 2.83e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049    6 DYYPEHWPENMIEEDIQGIKELGSNMVRIGEFAWHLMEPKEGEYDFSFFDSVINKLKKQNIDVMFGTPTATFPAWLAKQH 85
Cdd:pfam02449   1 DYNPEQWPEETWEEDIRLMKEAGVNVVRIGIFAWAKLEPEEGKYDFEWLDEVIDLLAKAGIKVILATPTAAPPAWLVKKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049   86 PSILSKDENGAVRAFGGRRQYCFNSPLYRKYSAQITEQLVKHYCSEEAIVAWQVDNEFGHEGSDmCYCEQCHKEFQQFLE 165
Cdd:pfam02449  81 PEILPVDADGRRRGFGSRHHYCPSSPVYREYAARIVEALAERYGDHPALIGWHIDNEYGCHVSE-CYCETCERAFRKWLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  166 RQYKDINELNEKYGTIFWGQTYNEFTEVPMPVKTITTHSPSLKLDWARFRSFSLNRYAHEQTAIVKKYKGDhQLLTTNVS 245
Cdd:pfam02449 160 NRYGTIDALNEAWGTAFWSQTYSDFDEIEPPRPAPTFPNPSQILDYRRFSSDQLLEFYRAEREIIREYSPD-IPVTTNFM 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  246 GGFFdKWFDHEENLEVMDFVSYDNYPVWGGQTEPITPAHIALGHDFNRGLL-HKNFWIVEELMGAQGHDIIGYLPRPNQA 324
Cdd:pfam02449 239 GSYF-KDLDYFKWAKELDFVSWDSYPTGDTEPEEEDPDALAFAHDLYRSLKkGKPFWLMEQSPSPVNWAPYNPAKRPGMM 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 753727049  325 KMWSYQAFAHGCTNMLYFRWRGMTRGAEQYCYGVVGHDNH-YGRRYKEVQSLFSEI 379
Cdd:pfam02449 318 RLWSLQAVAHGADAVCYFQWRQSRGGSEKFHSGVLDHDGReDTRVFREVAELGEEL 373
Glyco_hydro_42M pfam08532
Beta-galactosidase trimerization domain; This is non catalytic domain B of beta-galactosidase ...
392-588 5.86e-57

Beta-galactosidase trimerization domain; This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerization.


Pssm-ID: 369931  Cd Length: 207  Bit Score: 191.34  E-value: 5.86e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  392 SDVAVLYDYENIWSWRFQQ--QSEGFDFTQELLRGYTPFYKLNTPIDVIPASRDFSSYKVLVVPALQIIDEELGKRFTEF 469
Cdd:pfam08532   1 AQVAILFDWESWWAIEDQQgpSNRGLDYRSTVQDWYRALWDLGIPVDFVPPDADLSGYKLVVAPMLYLVSEELAKRLEAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  470 TENGGVIVFTFRTGIKDKQNNIHFKQtLPGYVKEITGIEIHEVEALSSTQKAAIKgvgpYEGEQASVSVWRDIITPVTAE 549
Cdd:pfam08532  81 VENGGTLVLTYRSGVVDENDLIHLGG-YPGPLRELLGIRVEEFDPLPPEESNTVS----YNGKTYEARLWCEILEPEGAE 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 753727049  550 VLYEYDDPFY-NQAAVTKNQFGRGTVYYVGCGIEEQTFEK 588
Cdd:pfam08532 156 VLATYADDFYaGTPAVTRNNYGKGKAYYVGTRLEDDFLDA 195
A4_beta-galactosidase_middle_domain cd03143
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; ...
394-492 1.21e-27

A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.


Pssm-ID: 153237 [Multi-domain]  Cd Length: 154  Bit Score: 109.04  E-value: 1.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049 394 VAVLYDYENIWSWRFQQQSEGFDFTQELLRGYTPFYKLNTPIDVIPASRDFSSYKVLVVPALQIIDEELGKRFTEFTENG 473
Cdd:cd03143    1 VAIVFDYESWWALELQPQSAGLRYLDLALALYRALRELGIPVDVVPPDADLSGYKLVVLPDLYLLSDATAAALRAYVENG 80
                         90
                 ....*....|....*....
gi 753727049 474 GVIVFTFRTGIKDKQNNIH 492
Cdd:cd03143   81 GTLVAGPRSGAVDEHDAIP 99
COG3934 COG3934
Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism];
1-143 2.48e-07

Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism];


Pssm-ID: 443135 [Multi-domain]  Cd Length: 331  Bit Score: 53.05  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049   1 MYIGVDYYPEH--------WPENMIEEDIQGIKELGSNMVRIgeFA-WHLMEPKEGEYD---FSFFDSVINKLKKQNIDV 68
Cdd:COG3934    7 FFLGVNYWPRAggfhmwrdWDPDRVRRELDDLAALGLDVVRV--FLlWEDFQPNPGLINeeaLERLDYFLDAAAERGLKV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049  69 MfgtPTAtFPAWlakqhpsilskdengavrAFGGRRQYCFNSP---------LY------RKYSAQItEQLVKHYCSEEA 133
Cdd:COG3934   85 V---LTL-FNNW------------------WSGHMSGYNWLPSwvggwhrrnFYtdpeavEAQKAYV-RTLANRYKDDPA 141
                        170
                 ....*....|
gi 753727049 134 IVAWQVDNEF 143
Cdd:COG3934  142 ILGWELGNEP 151
Glyco_hydro_35 pfam01301
Glycosyl hydrolases family 35;
9-152 1.66e-05

Glycosyl hydrolases family 35;


Pssm-ID: 396048 [Multi-domain]  Cd Length: 316  Bit Score: 47.25  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049    9 PEHWPENmieedIQGIKELGSNMVRIGEFaWHLMEPKEGEYDFS-FFDSV--INKLKKQNIDVM------------FGtp 73
Cdd:pfam01301  23 PEMWPDR-----LQKAKALGLNAIETYVF-WNLHEPEPGQYDFSgILDLVkfIKLAQEAGLYVIlrpgpyicaewdFG-- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753727049   74 taTFPAWlakqhpsiLSKDENGAVRAfggrrqycfNSPLY----RKYSAQITEQLVKHYCSEEA-IVAWQVDNEFGHEGS 148
Cdd:pfam01301  95 --GLPAW--------LLTVPGIRLRT---------SDPPFleavERYLTALLPKMKPLQATNGGpIIMVQVENEYGSYGV 155

                  ....
gi 753727049  149 DMCY 152
Cdd:pfam01301 156 DKAY 159
 
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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