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Conserved domains on  [gi|441434730|gb|ELR68171|]
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Glycogen debranching enzyme [Fulvivirga imtechensis AK7]

Protein Classification

amylo-alpha-1,6-glucosidase( domain architecture ID 11465557)

amylo-alpha-1,6-glucosidase catalyzes the hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin and with 4-alpha-D-glucanotransferase, constitute a glycogen debranching enzyme

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
271-658 1.09e-156

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


:

Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 457.80  E-value: 1.09e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 271 HWINRSLTDLVSlmSTTVYGKYPYAGVPWYNTAFGRDGILTAFETLWLAPELSKDVLRFLAKNQAselneasdaEPGKIL 350
Cdd:COG3408    2 RALRRAADQLRT--NTPGDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQE---------EPGKIP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 351 HETRGGEMValnevpfkkYYGTIDATPLFVMLAGEYYDRTADLDFIKEIWPNLEAAIGWIDNyGDLDNDGFVEYKHKaan 430
Cdd:COG3408   71 HEVRDGEEP---------YYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 431 GLANQGWKDSL-DSVSHedgqladPPIALCEVQGYVYAAKMHAAKLARILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQ 509
Cdd:COG3408  138 GLDNQTWMDSKvDSVTP-------RSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELG 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 510 CYVLALDGNKQPCRVVSSNA--GHVLFTGIADHDKAEKVAKAMMAEDMFSEWGIRTLSTTAKRYNPMSYHNGSVWPHDVA 587
Cdd:COG3408  211 YLADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNG 290
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 441434730 588 LISYGLALYGMQNESAKILQGLFDASLFIDLQRLPELFCGFpkrngegpTAYPVACSPQAWSVAAVFMLLQ 658
Cdd:COG3408  291 LYAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGF--------DGYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
32-229 8.52e-56

N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the N-terminal of some glycogen debranching enzymes and is usually followed by the GDE_C (PF06202) and in this sense it is analogous (but probably not homologous) to the GDE_N (PF12439). Its exact function is unknown


:

Pssm-ID: 434175  Cd Length: 193  Bit Score: 188.95  E-value: 8.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730   32 LNHCDTFGIFDSWGDILPIGKQIHGLYHQDTRYISRIQLKINNYRPTLLSSTIKEENEMLSVDLTNPEMKLDNGQIVhHG 111
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPPGGGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDLTNPDLEDDGGGLP-DG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  112 SIHIRRMHFMRtNMFHEKTQFTNFNDSALTIILSLRFEGDFKDIFEVRGLKRARRGNVLNNEFSDQRnLTLGYEGLDQVK 191
Cdd:pfam14742  80 TLHIRRERFLG-GGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGRRARRGRLLPPVVEGDE-LRLAYRGLDGVL 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 441434730  192 RTAQIQFSQPffDKSEDTGTMYFELFLQPNETSELDYH 229
Cdd:pfam14742 158 RETRIRFDPA--PDELDGGRATFRVELAPGESWTLTLR 193
 
Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
271-658 1.09e-156

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 457.80  E-value: 1.09e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 271 HWINRSLTDLVSlmSTTVYGKYPYAGVPWYNTAFGRDGILTAFETLWLAPELSKDVLRFLAKNQAselneasdaEPGKIL 350
Cdd:COG3408    2 RALRRAADQLRT--NTPGDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQE---------EPGKIP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 351 HETRGGEMValnevpfkkYYGTIDATPLFVMLAGEYYDRTADLDFIKEIWPNLEAAIGWIDNyGDLDNDGFVEYKHKaan 430
Cdd:COG3408   71 HEVRDGEEP---------YYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 431 GLANQGWKDSL-DSVSHedgqladPPIALCEVQGYVYAAKMHAAKLARILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQ 509
Cdd:COG3408  138 GLDNQTWMDSKvDSVTP-------RSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELG 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 510 CYVLALDGNKQPCRVVSSNA--GHVLFTGIADHDKAEKVAKAMMAEDMFSEWGIRTLSTTAKRYNPMSYHNGSVWPHDVA 587
Cdd:COG3408  211 YLADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNG 290
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 441434730 588 LISYGLALYGMQNESAKILQGLFDASLFIDLQRLPELFCGFpkrngegpTAYPVACSPQAWSVAAVFMLLQ 658
Cdd:COG3408  291 LYAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGF--------DGYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
32-229 8.52e-56

N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the N-terminal of some glycogen debranching enzymes and is usually followed by the GDE_C (PF06202) and in this sense it is analogous (but probably not homologous) to the GDE_N (PF12439). Its exact function is unknown


Pssm-ID: 434175  Cd Length: 193  Bit Score: 188.95  E-value: 8.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730   32 LNHCDTFGIFDSWGDILPIGKQIHGLYHQDTRYISRIQLKINNYRPTLLSSTIKEENEMLSVDLTNPEMKLDNGQIVhHG 111
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPPGGGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDLTNPDLEDDGGGLP-DG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  112 SIHIRRMHFMRtNMFHEKTQFTNFNDSALTIILSLRFEGDFKDIFEVRGLKRARRGNVLNNEFSDQRnLTLGYEGLDQVK 191
Cdd:pfam14742  80 TLHIRRERFLG-GGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGRRARRGRLLPPVVEGDE-LRLAYRGLDGVL 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 441434730  192 RTAQIQFSQPffDKSEDTGTMYFELFLQPNETSELDYH 229
Cdd:pfam14742 158 RETRIRFDPA--PDELDGGRATFRVELAPGESWTLTLR 193
GDE_C pfam06202
Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. ...
369-653 7.64e-20

Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog Swiss:O93808 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).


Pssm-ID: 428822  Cd Length: 370  Bit Score: 92.01  E-value: 7.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  369 YYGTIDATPLFVMLAGEYYDRTADLDFIKEIWPNLEAAIGW----IDNYGDLD-NDGFVeykHKAANGlaNQG-WkdsLD 442
Cdd:pfam06202  79 RYNTVDASLWFIYAVQKYLEYAPDAEFLRRIFPTIQEILGAyfkgTDFNIGLDpEDGLI---HGGSRG--NQLtW---MD 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  443 SVSHedGQLADPPI-ALCEVQGYVYAAKMHAAKLAR-ILGrnDEAEEWEKQAGYLKEKFNKTFWDNELQCYVLALDGNKQ 520
Cdd:pfam06202 151 AKVG--GWPVTPRDgKAVEINALWYNALRFASRLANkILG--EDKSSYKELAEKIKDNFEKKFWNNKRGILYDVIDPSLP 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  521 PCRVVSSNAG------HVLFTgiadhDKAEKVAKAMMAEDMFSEWGIRTLSTTAKRYNP----------MSYHNGSVWPH 584
Cdd:pfam06202 227 KDYQLRPNFLialslaPTLLS-----PEKAKKALDLAEEELLTPYGLRTLDPDDPDYLGtyrgdqdsrdMAYHQGTVWPW 301
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 441434730  585 dvaLISYGLALYGMQNESAK--------ILQGLFDASLFIDLQRLPELFcgfpkrNGEGPTAyPVACSPQAWSVAAV 653
Cdd:pfam06202 302 ---LIGYFLRAKLKFGDDSKlaldlvapLLEGHYKHLQEAGWGGIPELF------DGDGPYC-PRGCIAQAWSVAEI 368
PRK10137 PRK10137
alpha-glucosidase; Provisional
406-611 5.14e-08

alpha-glucosidase; Provisional


Pssm-ID: 236653  Cd Length: 786  Bit Score: 56.32  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 406 AIGW---IDN---YGDLDNDGFVEYkhkAANGLANQGWKDSLDSVSHEDGQLADPPIALCEVQ--GYVYAAKMHAAKLAR 477
Cdd:PRK10137 520 AASWesgRDDaavFGFIDKEQLDKY---VANGGKRSDWTVKFAENRSQDGTLLGYSLLQESVDqaSYMYSDNHYLAEMAT 596
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 478 ILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQCYvlaLDGNKQPCRVVSSNAGHV-------------LFTGIADHDKAE 544
Cdd:PRK10137 597 ILGKPEEAKRYRQLAQQLADYINTCMFDETTGFY---YDVRIEDKPLANGCAGKPivergkgpegwspLFNGAATQANAD 673
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 441434730 545 KVAKAMMAEDMFSEW-GIRTLSTTAKRYNPMSYHNGSVWPHDVALISYGLALYGMQNESAKILQGLFD 611
Cdd:PRK10137 674 AVVKVMLDPKEFNTFvPLGTAALTNPAFGADIYWRGRVWVDQFYFGLKGMERYGYRDDALKLADTFFR 741
 
Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
271-658 1.09e-156

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 457.80  E-value: 1.09e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 271 HWINRSLTDLVSlmSTTVYGKYPYAGVPWYNTAFGRDGILTAFETLWLAPELSKDVLRFLAKNQAselneasdaEPGKIL 350
Cdd:COG3408    2 RALRRAADQLRT--NTPGDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQE---------EPGKIP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 351 HETRGGEMValnevpfkkYYGTIDATPLFVMLAGEYYDRTADLDFIKEIWPNLEAAIGWIDNyGDLDNDGFVEYKHKaan 430
Cdd:COG3408   71 HEVRDGEEP---------YYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 431 GLANQGWKDSL-DSVSHedgqladPPIALCEVQGYVYAAKMHAAKLARILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQ 509
Cdd:COG3408  138 GLDNQTWMDSKvDSVTP-------RSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELG 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 510 CYVLALDGNKQPCRVVSSNA--GHVLFTGIADHDKAEKVAKAMMAEDMFSEWGIRTLSTTAKRYNPMSYHNGSVWPHDVA 587
Cdd:COG3408  211 YLADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNG 290
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 441434730 588 LISYGLALYGMQNESAKILQGLFDASLFIDLQRLPELFCGFpkrngegpTAYPVACSPQAWSVAAVFMLLQ 658
Cdd:COG3408  291 LYAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGF--------DGYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
32-229 8.52e-56

N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the N-terminal of some glycogen debranching enzymes and is usually followed by the GDE_C (PF06202) and in this sense it is analogous (but probably not homologous) to the GDE_N (PF12439). Its exact function is unknown


Pssm-ID: 434175  Cd Length: 193  Bit Score: 188.95  E-value: 8.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730   32 LNHCDTFGIFDSWGDILPIGKQIHGLYHQDTRYISRIQLKINNYRPTLLSSTIKEENEMLSVDLTNPEMKLDNGQIVhHG 111
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPPGGGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDLTNPDLEDDGGGLP-DG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  112 SIHIRRMHFMRtNMFHEKTQFTNFNDSALTIILSLRFEGDFKDIFEVRGLKRARRGNVLNNEFSDQRnLTLGYEGLDQVK 191
Cdd:pfam14742  80 TLHIRRERFLG-GGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGRRARRGRLLPPVVEGDE-LRLAYRGLDGVL 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 441434730  192 RTAQIQFSQPffDKSEDTGTMYFELFLQPNETSELDYH 229
Cdd:pfam14742 158 RETRIRFDPA--PDELDGGRATFRVELAPGESWTLTLR 193
GDE_C pfam06202
Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. ...
369-653 7.64e-20

Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog Swiss:O93808 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).


Pssm-ID: 428822  Cd Length: 370  Bit Score: 92.01  E-value: 7.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  369 YYGTIDATPLFVMLAGEYYDRTADLDFIKEIWPNLEAAIGW----IDNYGDLD-NDGFVeykHKAANGlaNQG-WkdsLD 442
Cdd:pfam06202  79 RYNTVDASLWFIYAVQKYLEYAPDAEFLRRIFPTIQEILGAyfkgTDFNIGLDpEDGLI---HGGSRG--NQLtW---MD 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  443 SVSHedGQLADPPI-ALCEVQGYVYAAKMHAAKLAR-ILGrnDEAEEWEKQAGYLKEKFNKTFWDNELQCYVLALDGNKQ 520
Cdd:pfam06202 151 AKVG--GWPVTPRDgKAVEINALWYNALRFASRLANkILG--EDKSSYKELAEKIKDNFEKKFWNNKRGILYDVIDPSLP 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  521 PCRVVSSNAG------HVLFTgiadhDKAEKVAKAMMAEDMFSEWGIRTLSTTAKRYNP----------MSYHNGSVWPH 584
Cdd:pfam06202 227 KDYQLRPNFLialslaPTLLS-----PEKAKKALDLAEEELLTPYGLRTLDPDDPDYLGtyrgdqdsrdMAYHQGTVWPW 301
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 441434730  585 dvaLISYGLALYGMQNESAK--------ILQGLFDASLFIDLQRLPELFcgfpkrNGEGPTAyPVACSPQAWSVAAV 653
Cdd:pfam06202 302 ---LIGYFLRAKLKFGDDSKlaldlvapLLEGHYKHLQEAGWGGIPELF------DGDGPYC-PRGCIAQAWSVAEI 368
Bac_rhamnosid6H pfam17389
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial ...
365-555 3.04e-14

Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.


Pssm-ID: 407469  Cd Length: 340  Bit Score: 74.66  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  365 PFKKYYGTIDATPLFVMLAGEYYDRTADLDFIKEIWPNLEAAIGWIDNYGDLDNDGFveykhkAANGLANQGWKDSLDSV 444
Cdd:pfam17389  89 VRGPGSPGPEWGDAIVIVPWALYRNYGDTRILQDQYPSMKRWLDYLLQRSDDGLWGL------SGWGLGDWLDPDGRPGD 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  445 SHEDGQLadppIALCevqgYVYAAKMHAAKLARILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQCYVlaldGNKQpcrv 524
Cdd:pfam17389 163 APTPGDL----VATA----YYYRSLGLMAKMAELLGKDEDAKRYAALAEELKAAFNKKYLDTETGSYA----NDTQ---- 226
                         170       180       190
                  ....*....|....*....|....*....|.
gi 441434730  525 vSSNAgHVLFTGIADHDKAEKVAKAMMAEDM 555
Cdd:pfam17389 227 -TANA-LPLAFGLVPDALRAAVAAERLAKKV 255
PRK10137 PRK10137
alpha-glucosidase; Provisional
406-611 5.14e-08

alpha-glucosidase; Provisional


Pssm-ID: 236653  Cd Length: 786  Bit Score: 56.32  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 406 AIGW---IDN---YGDLDNDGFVEYkhkAANGLANQGWKDSLDSVSHEDGQLADPPIALCEVQ--GYVYAAKMHAAKLAR 477
Cdd:PRK10137 520 AASWesgRDDaavFGFIDKEQLDKY---VANGGKRSDWTVKFAENRSQDGTLLGYSLLQESVDqaSYMYSDNHYLAEMAT 596
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 478 ILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQCYvlaLDGNKQPCRVVSSNAGHV-------------LFTGIADHDKAE 544
Cdd:PRK10137 597 ILGKPEEAKRYRQLAQQLADYINTCMFDETTGFY---YDVRIEDKPLANGCAGKPivergkgpegwspLFNGAATQANAD 673
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 441434730 545 KVAKAMMAEDMFSEW-GIRTLSTTAKRYNPMSYHNGSVWPHDVALISYGLALYGMQNESAKILQGLFD 611
Cdd:PRK10137 674 AVVKVMLDPKEFNTFvPLGTAALTNPAFGADIYWRGRVWVDQFYFGLKGMERYGYRDDALKLADTFFR 741
TreA COG1626
Neutral trehalase [Carbohydrate transport and metabolism];
473-553 3.24e-07

Neutral trehalase [Carbohydrate transport and metabolism];


Pssm-ID: 441233  Cd Length: 438  Bit Score: 53.31  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730 473 AKLARILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQCYvlaLDGN---KQPCRVVSSNAGHVLFTGIADHDKAEKVAKA 549
Cdd:COG1626  252 AKAYALAGDPAKAAEYRARAERRKEAINRYLWDEERGFY---FDYDfvtGKQTAVLSAAAFYPLFAGIATPEQAARVAET 328

                 ....
gi 441434730 550 MMAE 553
Cdd:COG1626  329 LEPQ 332
DUF608 pfam04685
Glycosyl-hydrolase family 116, catalytic region; This represents a family of archaeal, ...
374-612 2.53e-06

Glycosyl-hydrolase family 116, catalytic region; This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.


Pssm-ID: 461391  Cd Length: 362  Bit Score: 50.33  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  374 DATPLFVMLAGEYYDRTADLDFIKEIWPNLEAAIGWIDNYgDLDNDGFVEYKhkaanGLANQ---GWkdSLDSVShedgq 450
Cdd:pfam04685  99 DLNPKFVLQVYRDYVFTGDKEFLKAMWPSVKAVMDYLLQF-DKDGDGLIENE-----GFPDQtydAW--SMTGPS----- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  451 ladppiALCevQGYVYAAKMHAAKLARILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQCYVLALDGNKQPCrvvssnag 530
Cdd:pfam04685 166 ------AYC--GGLWLAALQAAIEMAELLGDKADVAKYKEKLEKAKKVFEKKLWNGKYFNYDSSSSSYSNSI-------- 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  531 hvlftgIADHDKAEKVAKAMMAEDMFSEWGIRTLSTTAKRYNPMSYHNG----------------------SVWPHdval 588
Cdd:pfam04685 230 ------MADQLAGQWYLRACGLEPIVPEDKVRSALETIYELNVMKFKGGkmgavngmrpdggvdtssvqseEVWTG---- 299
                         250       260
                  ....*....|....*....|....*...
gi 441434730  589 ISYGLA----LYGMQNESAKILQGLFDA 612
Cdd:pfam04685 300 VTYALAatmiQEGMVEEGFKTAEGIYDT 327
SGA1 COG3387
Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and ...
465-518 8.18e-04

Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism];


Pssm-ID: 442614 [Multi-domain]  Cd Length: 585  Bit Score: 42.84  E-value: 8.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 441434730 465 VYAAKMHAAKLARILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQCYVLALDGN 518
Cdd:COG3387  404 CWVALDRAARLAELLGLPAPAERWRALADEIRAEILERGWDEERGAFVQAYGSD 457
Trehalase pfam01204
Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a ...
473-605 6.49e-03

Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.


Pssm-ID: 395961 [Multi-domain]  Cd Length: 509  Bit Score: 39.62  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441434730  473 AKLARILGRNDEAEEWEKQAGYLKEKFNKTFWDNELQCYvlaLDGN---KQPCRVVSSNAGHVLFTGIADHDKAEKVAKA 549
Cdd:pfam01204 319 AFFCDVLGDSETSAIWEERAEQRRLAIDKYLWNEEAGVW---FDYDlkkRKQTNYFSATNFWPLWAGLASPDQAKMVAKV 395
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 441434730  550 MMAEDMF----SEWGI-RTLSTTAKRYNpmsYHNGsvWPHDVALISYGLALYGMQNESAKI 605
Cdd:pfam01204 396 LPKLEESgllvFPGGRpTSLLDSGQQWD---YPNG--WAPLQWLAVEGLQRYGYDELAERL 451
 
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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