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Conserved domains on  [gi|915258521|ref|WP_050758146|]
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beta-galactosidase [Xylanimonas cellulosilytica]

Protein Classification

beta-galactosidase( domain architecture ID 11449001)

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];
9-621 0e+00

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


:

Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 739.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   9 GLLYGGDYNPEQWDPSVWREDARLMREAGVNLVTVGVFSWARYEPEPGVRDFAWLDEVLDVLQAHGIAVDLATPTASPPP 88
Cdd:COG1874    9 FLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIGYFAWNLHEPEEGVFDFDWLDRFIDLLHEAGLKVILRTPTAAPPA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  89 WLGIDHPETLPVDRDGVRLVAGSRNQFAPSSRVYREAALAITCDLAARYARHPAVRMWHVGNEYGQVDFGDEAAREFRAW 168
Cdd:COG1874   89 WLLKKYPEILPVDADGRRRGFGSRRHYCPSSPVYREAARRIVRALAERYGDHPAVIMWQVDNEYGSYDYCDACAAAFRDW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 169 LHDRYGSIDALNEAWGTAFWSQRYRDFEDVLPPRRAPYLVNPTQALDFRRFTSDELLACYREQHAALREAGVTAPITTNF 248
Cdd:COG1874  169 LRERYGTLDALNEAWGTAFWSQRYTDWDEIEPPRLTPTTANPSLRLDFRRFSSDQVLEYLRAQRDILREAGPDVPVTTNF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 249 MGFFPGADYWRWADAVDVVADDQYPDhADPRSPADAALVQDLMRGLGGGAPWLLLEQAAGATSWREHNLPKSPERMRLDS 328
Cdd:COG1874  249 MGPFPGLDYWKLARDLDVVSWDNYPD-GSAADPDEIAFAHDLMRGLKGGGPFMVMEQWPGWVNWGPYNPAKRPGQLRLWS 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 329 LQAVARGADGVCFFQWRASTAGAERFHSAMLPHAGPDTAVHRGVRRLGTDLARLHPVIGSRVAARTALLFDWESWWAAEE 408
Cdd:COG1874  328 LQALAHGADGVNYFQWRPSRGGTEYDHDAPLDHAGRPTRKFREVRELGAELARLPEVPGSRVTARVALLFDWESWWALEI 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 409 PGRITER-LRTLDQVRAYYRPLWDRGVAVDVVRPGAALDAYDVVVVPQTYLLDDDAATSLRAAAEGGACVVVGPMTGVAD 487
Cdd:COG1874  408 QSPPLGQdLGYVDLVRALYRALRRAGVTVDIVPPFADLSGYKLLVAPALYLVSDALAERLLAYVENGGRVNYGPRSGIVD 487
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 488 RNAHVLPGRFPVRLADVLGVSGEEWVALPDGG-VPVTGAlvtgtpgkGSAHTHAELLRADDAEVLSRFADGHLAGAPAVT 566
Cdd:COG1874  488 EKDRVRLGGYPGILRDLLGVRVEEFDPLPPGEpVPLSGG--------YTGWLWYELLPLDGAEVLARYADGFYAGRPAVT 559
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 915258521 567 RRDVpGGGAAWYVGAVLDEPLLAAVLDDALTRAGV-PAAVPgavglDDVEAVVRGD 621
Cdd:COG1874  560 RNTF-GKGVAWYNGTNLDDWLLAALLARLLAEAGLyPVDLP-----EGVEAVRRVG 609
Glyco_hydro_42C pfam08533
Beta-galactosidase C-terminal domain; This domain is found at the C-terminus of ...
619-664 1.64e-05

Beta-galactosidase C-terminal domain; This domain is found at the C-terminus of beta-galactosidase enzymes that belong to the glycosyl hydrolase 42 family.


:

Pssm-ID: 400716  Cd Length: 58  Bit Score: 42.75  E-value: 1.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 915258521  619 RGDVVFLLNRGGETARVAVPGTWTDLLTGDDVIDVVDLPPHDAAVL 664
Cdd:pfam08533  11 RGRYLFVFNYSNEEVTVDLPASAGDLLTGELEAGEVTLEPYDVRVL 56
 
Name Accession Description Interval E-value
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
9-621 0e+00

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 739.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   9 GLLYGGDYNPEQWDPSVWREDARLMREAGVNLVTVGVFSWARYEPEPGVRDFAWLDEVLDVLQAHGIAVDLATPTASPPP 88
Cdd:COG1874    9 FLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIGYFAWNLHEPEEGVFDFDWLDRFIDLLHEAGLKVILRTPTAAPPA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  89 WLGIDHPETLPVDRDGVRLVAGSRNQFAPSSRVYREAALAITCDLAARYARHPAVRMWHVGNEYGQVDFGDEAAREFRAW 168
Cdd:COG1874   89 WLLKKYPEILPVDADGRRRGFGSRRHYCPSSPVYREAARRIVRALAERYGDHPAVIMWQVDNEYGSYDYCDACAAAFRDW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 169 LHDRYGSIDALNEAWGTAFWSQRYRDFEDVLPPRRAPYLVNPTQALDFRRFTSDELLACYREQHAALREAGVTAPITTNF 248
Cdd:COG1874  169 LRERYGTLDALNEAWGTAFWSQRYTDWDEIEPPRLTPTTANPSLRLDFRRFSSDQVLEYLRAQRDILREAGPDVPVTTNF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 249 MGFFPGADYWRWADAVDVVADDQYPDhADPRSPADAALVQDLMRGLGGGAPWLLLEQAAGATSWREHNLPKSPERMRLDS 328
Cdd:COG1874  249 MGPFPGLDYWKLARDLDVVSWDNYPD-GSAADPDEIAFAHDLMRGLKGGGPFMVMEQWPGWVNWGPYNPAKRPGQLRLWS 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 329 LQAVARGADGVCFFQWRASTAGAERFHSAMLPHAGPDTAVHRGVRRLGTDLARLHPVIGSRVAARTALLFDWESWWAAEE 408
Cdd:COG1874  328 LQALAHGADGVNYFQWRPSRGGTEYDHDAPLDHAGRPTRKFREVRELGAELARLPEVPGSRVTARVALLFDWESWWALEI 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 409 PGRITER-LRTLDQVRAYYRPLWDRGVAVDVVRPGAALDAYDVVVVPQTYLLDDDAATSLRAAAEGGACVVVGPMTGVAD 487
Cdd:COG1874  408 QSPPLGQdLGYVDLVRALYRALRRAGVTVDIVPPFADLSGYKLLVAPALYLVSDALAERLLAYVENGGRVNYGPRSGIVD 487
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 488 RNAHVLPGRFPVRLADVLGVSGEEWVALPDGG-VPVTGAlvtgtpgkGSAHTHAELLRADDAEVLSRFADGHLAGAPAVT 566
Cdd:COG1874  488 EKDRVRLGGYPGILRDLLGVRVEEFDPLPPGEpVPLSGG--------YTGWLWYELLPLDGAEVLARYADGFYAGRPAVT 559
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 915258521 567 RRDVpGGGAAWYVGAVLDEPLLAAVLDDALTRAGV-PAAVPgavglDDVEAVVRGD 621
Cdd:COG1874  560 RNTF-GKGVAWYNGTNLDDWLLAALLARLLAEAGLyPVDLP-----EGVEAVRRVG 609
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
15-382 1.12e-171

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: 495.25  E-value: 1.12e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   15 DYNPEQWDPSVWREDARLMREAGVNLVTVGVFSWARYEPEPGVRDFAWLDEVLDVLQAHGIAVDLATPTASPPPWLGIDH 94
Cdd:pfam02449   1 DYNPEQWPEETWEEDIRLMKEAGVNVVRIGIFAWAKLEPEEGKYDFEWLDEVIDLLAKAGIKVILATPTAAPPAWLVKKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   95 PETLPVDRDGVRLVAGSRNQFAPSSRVYREAALAITCDLAARYARHPAVRMWHVGNEYG---QVDFGDEAAREFRAWLHD 171
Cdd:pfam02449  81 PEILPVDADGRRRGFGSRHHYCPSSPVYREYAARIVEALAERYGDHPALIGWHIDNEYGchvSECYCETCERAFRKWLKN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  172 RYGSIDALNEAWGTAFWSQRYRDFEDVLPPRRAPYLVNPTQALDFRRFTSDELLACYREQHAALREAGVTAPITTNFMGF 251
Cdd:pfam02449 161 RYGTIDALNEAWGTAFWSQTYSDFDEIEPPRPAPTFPNPSQILDYRRFSSDQLLEFYRAEREIIREYSPDIPVTTNFMGS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  252 -FPGADYWRWADAVDVVADDQYPDHADPRSPADA---ALVQDLMRGLGGGAPWLLLEQAAGATSWREHNLPKSPERMRLD 327
Cdd:pfam02449 241 yFKDLDYFKWAKELDFVSWDSYPTGDTEPEEEDPdalAFAHDLYRSLKKGKPFWLMEQSPSPVNWAPYNPAKRPGMMRLW 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 915258521  328 SLQAVARGADGVCFFQWRASTAGAERFHSAMLPHAG-PDTAVHRGVRRLGTDLARL 382
Cdd:pfam02449 321 SLQAVAHGADAVCYFQWRQSRGGSEKFHSGVLDHDGrEDTRVFREVAELGEELKKL 376
A4_beta-galactosidase_middle_domain cd03143
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; ...
394-518 3.05e-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: 107.88  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 394 TALLFDWESWWAaEEPGRITERLRTLDQVRAYYRPLWDRGVAVDVVRPGAALDAYDVVVVPQTYLLDDDAATSLRAAAEG 473
Cdd:cd03143    1 VAIVFDYESWWA-LELQPQSAGLRYLDLALALYRALRELGIPVDVVPPDADLSGYKLVVLPDLYLLSDATAAALRAYVEN 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 915258521 474 GACVVVGPMTGVADRNAHVLPGRFPV--RLADVLGVSGEEWVALPDG 518
Cdd:cd03143   80 GGTLVAGPRSGAVDEHDAIPLGLPPPlgRLLGGLGVRVEELNAYGKG 126
Glyco_hydro_42C pfam08533
Beta-galactosidase C-terminal domain; This domain is found at the C-terminus of ...
619-664 1.64e-05

Beta-galactosidase C-terminal domain; This domain is found at the C-terminus of beta-galactosidase enzymes that belong to the glycosyl hydrolase 42 family.


Pssm-ID: 400716  Cd Length: 58  Bit Score: 42.75  E-value: 1.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 915258521  619 RGDVVFLLNRGGETARVAVPGTWTDLLTGDDVIDVVDLPPHDAAVL 664
Cdd:pfam08533  11 RGRYLFVFNYSNEEVTVDLPASAGDLLTGELEAGEVTLEPYDVRVL 56
 
Name Accession Description Interval E-value
GanA COG1874
Beta-galactosidase GanA [Carbohydrate transport and metabolism];
9-621 0e+00

Beta-galactosidase GanA [Carbohydrate transport and metabolism];


Pssm-ID: 441478 [Multi-domain]  Cd Length: 609  Bit Score: 739.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   9 GLLYGGDYNPEQWDPSVWREDARLMREAGVNLVTVGVFSWARYEPEPGVRDFAWLDEVLDVLQAHGIAVDLATPTASPPP 88
Cdd:COG1874    9 FLILGGDYHPERWPPEVWAEDIRLMKAAGLNTVRIGYFAWNLHEPEEGVFDFDWLDRFIDLLHEAGLKVILRTPTAAPPA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  89 WLGIDHPETLPVDRDGVRLVAGSRNQFAPSSRVYREAALAITCDLAARYARHPAVRMWHVGNEYGQVDFGDEAAREFRAW 168
Cdd:COG1874   89 WLLKKYPEILPVDADGRRRGFGSRRHYCPSSPVYREAARRIVRALAERYGDHPAVIMWQVDNEYGSYDYCDACAAAFRDW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 169 LHDRYGSIDALNEAWGTAFWSQRYRDFEDVLPPRRAPYLVNPTQALDFRRFTSDELLACYREQHAALREAGVTAPITTNF 248
Cdd:COG1874  169 LRERYGTLDALNEAWGTAFWSQRYTDWDEIEPPRLTPTTANPSLRLDFRRFSSDQVLEYLRAQRDILREAGPDVPVTTNF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 249 MGFFPGADYWRWADAVDVVADDQYPDhADPRSPADAALVQDLMRGLGGGAPWLLLEQAAGATSWREHNLPKSPERMRLDS 328
Cdd:COG1874  249 MGPFPGLDYWKLARDLDVVSWDNYPD-GSAADPDEIAFAHDLMRGLKGGGPFMVMEQWPGWVNWGPYNPAKRPGQLRLWS 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 329 LQAVARGADGVCFFQWRASTAGAERFHSAMLPHAGPDTAVHRGVRRLGTDLARLHPVIGSRVAARTALLFDWESWWAAEE 408
Cdd:COG1874  328 LQALAHGADGVNYFQWRPSRGGTEYDHDAPLDHAGRPTRKFREVRELGAELARLPEVPGSRVTARVALLFDWESWWALEI 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 409 PGRITER-LRTLDQVRAYYRPLWDRGVAVDVVRPGAALDAYDVVVVPQTYLLDDDAATSLRAAAEGGACVVVGPMTGVAD 487
Cdd:COG1874  408 QSPPLGQdLGYVDLVRALYRALRRAGVTVDIVPPFADLSGYKLLVAPALYLVSDALAERLLAYVENGGRVNYGPRSGIVD 487
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 488 RNAHVLPGRFPVRLADVLGVSGEEWVALPDGG-VPVTGAlvtgtpgkGSAHTHAELLRADDAEVLSRFADGHLAGAPAVT 566
Cdd:COG1874  488 EKDRVRLGGYPGILRDLLGVRVEEFDPLPPGEpVPLSGG--------YTGWLWYELLPLDGAEVLARYADGFYAGRPAVT 559
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 915258521 567 RRDVpGGGAAWYVGAVLDEPLLAAVLDDALTRAGV-PAAVPgavglDDVEAVVRGD 621
Cdd:COG1874  560 RNTF-GKGVAWYNGTNLDDWLLAALLARLLAEAGLyPVDLP-----EGVEAVRRVG 609
Glyco_hydro_42 pfam02449
Beta-galactosidase; This group of beta-galactosidase enzymes belong to the glycosyl hydrolase ...
15-382 1.12e-171

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: 495.25  E-value: 1.12e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   15 DYNPEQWDPSVWREDARLMREAGVNLVTVGVFSWARYEPEPGVRDFAWLDEVLDVLQAHGIAVDLATPTASPPPWLGIDH 94
Cdd:pfam02449   1 DYNPEQWPEETWEEDIRLMKEAGVNVVRIGIFAWAKLEPEEGKYDFEWLDEVIDLLAKAGIKVILATPTAAPPAWLVKKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   95 PETLPVDRDGVRLVAGSRNQFAPSSRVYREAALAITCDLAARYARHPAVRMWHVGNEYG---QVDFGDEAAREFRAWLHD 171
Cdd:pfam02449  81 PEILPVDADGRRRGFGSRHHYCPSSPVYREYAARIVEALAERYGDHPALIGWHIDNEYGchvSECYCETCERAFRKWLKN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  172 RYGSIDALNEAWGTAFWSQRYRDFEDVLPPRRAPYLVNPTQALDFRRFTSDELLACYREQHAALREAGVTAPITTNFMGF 251
Cdd:pfam02449 161 RYGTIDALNEAWGTAFWSQTYSDFDEIEPPRPAPTFPNPSQILDYRRFSSDQLLEFYRAEREIIREYSPDIPVTTNFMGS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  252 -FPGADYWRWADAVDVVADDQYPDHADPRSPADA---ALVQDLMRGLGGGAPWLLLEQAAGATSWREHNLPKSPERMRLD 327
Cdd:pfam02449 241 yFKDLDYFKWAKELDFVSWDSYPTGDTEPEEEDPdalAFAHDLYRSLKKGKPFWLMEQSPSPVNWAPYNPAKRPGMMRLW 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 915258521  328 SLQAVARGADGVCFFQWRASTAGAERFHSAMLPHAG-PDTAVHRGVRRLGTDLARL 382
Cdd:pfam02449 321 SLQAVAHGADAVCYFQWRQSRGGSEKFHSGVLDHDGrEDTRVFREVAELGEELKKL 376
Glyco_hydro_42M pfam08532
Beta-galactosidase trimerization domain; This is non catalytic domain B of beta-galactosidase ...
392-602 2.95e-52

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: 179.40  E-value: 2.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  392 ARTALLFDWESWWAAE-EPGRITERLRTLDQVRAYYRPLWDRGVAVDVVRPGAALDAYDVVVVPQTYLLDDDAATSLRAA 470
Cdd:pfam08532   1 AQVAILFDWESWWAIEdQQGPSNRGLDYRSTVQDWYRALWDLGIPVDFVPPDADLSGYKLVVAPMLYLVSEELAKRLEAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  471 AEGGACVVVGPMTGVADRNAHVLPGRFPVRLADVLGVSGEEWVALPDG-GVPVTGalvtgtPGKG-SAHTHAELLRADDA 548
Cdd:pfam08532  81 VENGGTLVLTYRSGVVDENDLIHLGGYPGPLRELLGIRVEEFDPLPPEeSNTVSY------NGKTyEARLWCEILEPEGA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 915258521  549 EVLSRFADGHLAGAPAVTRRDVpGGGAAWYVGAVLDEPLLAAVLDDALTRAGVP 602
Cdd:pfam08532 155 EVLATYADDFYAGTPAVTRNNY-GKGKAYYVGTRLEDDFLDALYRRLLDEAGLS 207
A4_beta-galactosidase_middle_domain cd03143
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain; ...
394-518 3.05e-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: 107.88  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521 394 TALLFDWESWWAaEEPGRITERLRTLDQVRAYYRPLWDRGVAVDVVRPGAALDAYDVVVVPQTYLLDDDAATSLRAAAEG 473
Cdd:cd03143    1 VAIVFDYESWWA-LELQPQSAGLRYLDLALALYRALRELGIPVDVVPPDADLSGYKLVVLPDLYLLSDATAAALRAYVEN 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 915258521 474 GACVVVGPMTGVADRNAHVLPGRFPV--RLADVLGVSGEEWVALPDG 518
Cdd:cd03143   80 GGTLVAGPRSGAVDEHDAIPLGLPPPlgRLLGGLGVRVEELNAYGKG 126
COG3934 COG3934
Endo-1,4-beta-mannosidase [Carbohydrate transport and metabolism];
13-169 7.05e-07

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


Pssm-ID: 443135 [Multi-domain]  Cd Length: 331  Bit Score: 51.89  E-value: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  13 GGDYNPEQWDPSVWREDARLMREAGVNLVTVGVFsWARYEPEPGVRD---FAWLDEVLDVLQAHGI--AVDLATPTAS-- 85
Cdd:COG3934   18 GGFHMWRDWDPDRVRRELDDLAALGLDVVRVFLL-WEDFQPNPGLINeeaLERLDYFLDAAAERGLkvVLTLFNNWWSgh 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521  86 ------PPPWLGIDHpetlpvdrdgvrlvagSRNQFAPSSRVYREAALAITcdLAARYARHPAVRMWHVGNEYGQvdFGD 159
Cdd:COG3934   97 msgynwLPSWVGGWH----------------RRNFYTDPEAVEAQKAYVRT--LANRYKDDPAILGWELGNEPRN--FGD 156
                        170
                 ....*....|.
gi 915258521 160 EAARE-FRAWL 169
Cdd:COG3934  157 PASPEaALAWL 167
Glyco_hydro_14 pfam01373
Glycosyl hydrolase family 14; This family are beta amylases.
18-201 5.50e-06

Glycosyl hydrolase family 14; This family are beta amylases.


Pssm-ID: 366599  Cd Length: 402  Bit Score: 49.17  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   18 PEQWDPSVWREDARLMREAGVNLVTVGVFsWARYEPE-PGVRDFAWLDEVLDVLQAHGIAV---------------DLAT 81
Cdd:pfam01373  10 TMSGHWNAFNASLMALKGNGVYAITVDAW-WGLVEKDgDMQFDWSYYAELAQMVKKAGLKLqpiisthqcggnvgdDCNI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   82 PTaspPPWL---------------GIDHPETL-PVDRDGVR-----LVAGSRNQFAPSSRVYREAALAITCDLAARYARH 140
Cdd:pfam01373  89 PL---PSWVleeiskddlvfkdesGRRNPEYLsPLLSGRTIkvyseLYRSFAERFEGYKGVIAKIYLSGGPCGELRYPSY 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915258521  141 PAVRMWHVGNEyGQVDFGDEAAR-EFRAWLHDRYGSIDALNEAWGTAFWSQRYrdfedVLPP 201
Cdd:pfam01373 166 PESNGWRYPGR-GKFQAYTEYAKsSFRAYAENKYGSLGKTNKAWGTKLPSDAY-----INPP 221
Glyco_hydro_42C pfam08533
Beta-galactosidase C-terminal domain; This domain is found at the C-terminus of ...
619-664 1.64e-05

Beta-galactosidase C-terminal domain; This domain is found at the C-terminus of beta-galactosidase enzymes that belong to the glycosyl hydrolase 42 family.


Pssm-ID: 400716  Cd Length: 58  Bit Score: 42.75  E-value: 1.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 915258521  619 RGDVVFLLNRGGETARVAVPGTWTDLLTGDDVIDVVDLPPHDAAVL 664
Cdd:pfam08533  11 RGRYLFVFNYSNEEVTVDLPASAGDLLTGELEAGEVTLEPYDVRVL 56
DUF4434 pfam14488
Domain of unknown function (DUF4434);
11-169 2.73e-03

Domain of unknown function (DUF4434);


Pssm-ID: 433985 [Multi-domain]  Cd Length: 169  Bit Score: 39.30  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   11 LYGGDYNPEQWDPSVWREDARLMREAGVNLVtvgVFSWARYEPE---------PGVRDFAWLDEVLDVL---QAHGIAVD 78
Cdd:pfam14488   8 LQHHDLPHQNWTDAQWDEDLHELKELGMDTL---ILQWVGYGGKatypskylsSNKFDIPPVDLVELILdaaEELGMKVF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915258521   79 LATPtASPPPWlgiDHPETLpvdrdgvrlvagsRNQFAPSSRvyreaalaITCDLAARYARHPAVRMWHVGNEYGQVDFG 158
Cdd:pfam14488  85 FGLN-YDGEWW---DHQGDL-------------SWEAELANL--------IAEELYKNYGHHPAFYGWYIPYEIDQYKWN 139
                         170
                  ....*....|..
gi 915258521  159 DEAARE-FRAWL 169
Cdd:pfam14488 140 APEYINlLGKHL 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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