NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|302200897|gb|ADL08467|]
View 

Amylo-alpha-16-glucosidase [Thermosediminibacter oceani DSM 16646]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
231-617 3.10e-158

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


:

Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 460.11  E-value: 3.10e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 231 NLYKRSLADLRMLLSdfGEGPMAVAGIPWFAVPFGRDSIITGIQALLANTEIARGTLGTMARYQgqkldpwsdEEPGKIM 310
Cdd:COG3408    2 RALRRAADQLRTNTP--GDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQ---------EEPGKIP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 311 HELRQGElvntkevpfGPYYGTLDATPLFLILLSEYYNWTGDKKFFMELFPAAEKALKWMEQyGDRDGDSFLEYIREkeg 390
Cdd:COG3408   71 HEVRDGE---------EPYYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 391 GLVNQGWKDSKDSVVFSdgrladPPIALAEIQGYAYDALMRMARIYGELGKKEKANGLLRKAAHLKERFHRAFWMEDKKY 470
Cdd:COG3408  138 GLDNQTWMDSKVDSVTP------RSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELGY 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 471 FAEALDGEKRKVDSITSNP--GHCLWSGMLEYEKAVLVADRLLSDELFSGWGIRTMSCREAAYNPASYHNGSVWPHDNSL 548
Cdd:COG3408  212 LADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNGL 291
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302200897 549 IALGLARYGFKDHLKKLISGMIAASEYFEYCRLPELFCGFSredggpvRYPVACSPQAWAAATPIALLQ 617
Cdd:COG3408  292 YAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGFD-------GYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
5-185 4.27e-52

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: 178.55  E-value: 4.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897    5 IKEDGVFVETCESGDIE---ESTLGMFYQDTRYLSKYELKINGKRPVFLSASAEKNYFKEVYL-----------ADEKNE 70
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPpggGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDltnpdleddggGLPDGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897   71 VLISRKSCIyKNTFNERIRLTNYGLRTSELYLTIELDADFKHMFEVRGFAgRKGTGKKLAPVVEPRKIILRYTGSDNILR 150
Cdd:pfam14742  81 LHIRRERFL-GGGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGR-RARRGRLLPPVVEGDELRLAYRGLDGVLR 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 302200897  151 STVITFSRNITSFKDGRLGFSVELGPKESFDLCVC 185
Cdd:pfam14742 159 ETRIRFDPAPDELDGGRATFRVELAPGESWTLTLR 193
 
Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
231-617 3.10e-158

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


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 460.11  E-value: 3.10e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 231 NLYKRSLADLRMLLSdfGEGPMAVAGIPWFAVPFGRDSIITGIQALLANTEIARGTLGTMARYQgqkldpwsdEEPGKIM 310
Cdd:COG3408    2 RALRRAADQLRTNTP--GDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQ---------EEPGKIP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 311 HELRQGElvntkevpfGPYYGTLDATPLFLILLSEYYNWTGDKKFFMELFPAAEKALKWMEQyGDRDGDSFLEYIREkeg 390
Cdd:COG3408   71 HEVRDGE---------EPYYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 391 GLVNQGWKDSKDSVVFSdgrladPPIALAEIQGYAYDALMRMARIYGELGKKEKANGLLRKAAHLKERFHRAFWMEDKKY 470
Cdd:COG3408  138 GLDNQTWMDSKVDSVTP------RSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELGY 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 471 FAEALDGEKRKVDSITSNP--GHCLWSGMLEYEKAVLVADRLLSDELFSGWGIRTMSCREAAYNPASYHNGSVWPHDNSL 548
Cdd:COG3408  212 LADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNGL 291
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302200897 549 IALGLARYGFKDHLKKLISGMIAASEYFEYCRLPELFCGFSredggpvRYPVACSPQAWAAATPIALLQ 617
Cdd:COG3408  292 YAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGFD-------GYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
5-185 4.27e-52

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: 178.55  E-value: 4.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897    5 IKEDGVFVETCESGDIE---ESTLGMFYQDTRYLSKYELKINGKRPVFLSASAEKNYFKEVYL-----------ADEKNE 70
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPpggGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDltnpdleddggGLPDGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897   71 VLISRKSCIyKNTFNERIRLTNYGLRTSELYLTIELDADFKHMFEVRGFAgRKGTGKKLAPVVEPRKIILRYTGSDNILR 150
Cdd:pfam14742  81 LHIRRERFL-GGGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGR-RARRGRLLPPVVEGDELRLAYRGLDGVLR 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 302200897  151 STVITFSRNITSFKDGRLGFSVELGPKESFDLCVC 185
Cdd:pfam14742 159 ETRIRFDPAPDELDGGRATFRVELAPGESWTLTLR 193
GDE_C pfam06202
Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. ...
250-611 9.47e-26

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: 109.73  E-value: 9.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  250 GPMAVAGIPWFAvPFGRDSIITgIQALLANT---EIARGTLGTMARYqgqkldpwsdeepgkimheLRQGELVNTKEVPF 326
Cdd:pfam06202  18 GPSIIAGYHWFS-DWGRDTFIA-LPGLLLVTgrfEEARDIILTFAGY-------------------LRHGLIPNLFPAGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  327 GPYYGTLDATPLFLILLSEYYNWTGDKKFFMELFPAAEKALKWMEQygdrdGDSFLEYIREkEGGLVNQG-------WKD 399
Cdd:pfam06202  77 EPRYNTVDASLWFIYAVQKYLEYAPDAEFLRRIFPTIQEILGAYFK-----GTDFNIGLDP-EDGLIHGGsrgnqltWMD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  400 SKdsvvfSDGRLADPPIALA-EIQGYAYDALMRMARIyGELGKKEKANGLLRKAAHLKERFHRAFWMEDKKYFAEALDGE 478
Cdd:pfam06202 151 AK-----VGGWPVTPRDGKAvEINALWYNALRFASRL-ANKILGEDKSSYKELAEKIKDNFEKKFWNNKRGILYDVIDPS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  479 KRKVDSITSNPghcLWsgmleyekAVLVADRLLSDE------------LFSGWGIRTMSCREAAYNP----------ASY 536
Cdd:pfam06202 225 LPKDYQLRPNF---LI--------ALSLAPTLLSPEkakkaldlaeeeLLTPYGLRTLDPDDPDYLGtyrgdqdsrdMAY 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  537 HNGSVWP-------------HDNSLIALGLARYGFKDHLKKLISGMIAaseyfeycRLPELFcgfsrEDGGPVRyPVACS 603
Cdd:pfam06202 294 HQGTVWPwligyflraklkfGDDSKLALDLVAPLLEGHYKHLQEAGWG--------GIPELF-----DGDGPYC-PRGCI 359

                  ....*...
gi 302200897  604 PQAWAAAT 611
Cdd:pfam06202 360 AQAWSVAE 367
 
Name Accession Description Interval E-value
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
231-617 3.10e-158

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


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 460.11  E-value: 3.10e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 231 NLYKRSLADLRMLLSdfGEGPMAVAGIPWFAVPFGRDSIITGIQALLANTEIARGTLGTMARYQgqkldpwsdEEPGKIM 310
Cdd:COG3408    2 RALRRAADQLRTNTP--GDGPTVIAGYPWFSTDWGRDTLIALPGLLLLDPELARGILRTLARYQ---------EEPGKIP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 311 HELRQGElvntkevpfGPYYGTLDATPLFLILLSEYYNWTGDKKFFMELFPAAEKALKWMEQyGDRDGDSFLEYIREkeg 390
Cdd:COG3408   71 HEVRDGE---------EPYYGTVDATPWFIIALGEYYRWTGDLAFLRELLPALEAALDWILR-GDRDGDGLLEYGRS--- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 391 GLVNQGWKDSKDSVVFSdgrladPPIALAEIQGYAYDALMRMARIYGELGKKEKANGLLRKAAHLKERFHRAFWMEDKKY 470
Cdd:COG3408  138 GLDNQTWMDSKVDSVTP------RSGALVEVQALWYNALRALAELARALGDPELAARWRELAERLKESFNERFWNEELGY 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 471 FAEALDGEKRKVDSITSNP--GHCLWSGMLEYEKAVLVADRLLSDELFSGWGIRTMSCREAAYNPASYHNGSVWPHDNSL 548
Cdd:COG3408  212 LADALDGDGRPDDSIRPNQlfAHALPTGILDPERARAVLRRLVSPELLTPWGLRTLSPGDPAYNPMAYHNGSVWPWLNGL 291
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302200897 549 IALGLARYGFKDHLKKLISGMIAASEYFEYCRLPELFCGFSredggpvRYPVACSPQAWAAATPIALLQ 617
Cdd:COG3408  292 YAEGLLRYGFREEARRLLEGLLDALEEFGLGRLPELFDGFD-------GYPRGCIPQAWSAAEVLRLLQ 353
GDE_N_bis pfam14742
N-terminal domain of (some) glycogen debranching enzymes; This domain is found on the ...
5-185 4.27e-52

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: 178.55  E-value: 4.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897    5 IKEDGVFVETCESGDIE---ESTLGMFYQDTRYLSKYELKINGKRPVFLSASAEKNYFKEVYL-----------ADEKNE 70
Cdd:pfam14742   1 LKEGDTFLVTDRDGDIPpggGGPQGLFHRDTRFLSRLELTINGRRPELLSSTARGDNYALSVDltnpdleddggGLPDGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897   71 VLISRKSCIyKNTFNERIRLTNYGLRTSELYLTIELDADFKHMFEVRGFAgRKGTGKKLAPVVEPRKIILRYTGSDNILR 150
Cdd:pfam14742  81 LHIRRERFL-GGGLYERLTLTNYGTEPVELTLTLEFDADFADLFEVRGGR-RARRGRLLPPVVEGDELRLAYRGLDGVLR 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 302200897  151 STVITFSRNITSFKDGRLGFSVELGPKESFDLCVC 185
Cdd:pfam14742 159 ETRIRFDPAPDELDGGRATFRVELAPGESWTLTLR 193
GDE_C pfam06202
Amylo-alpha-1,6-glucosidase; This family includes human glycogen branching enzyme Swiss:P35573. ...
250-611 9.47e-26

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: 109.73  E-value: 9.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  250 GPMAVAGIPWFAvPFGRDSIITgIQALLANT---EIARGTLGTMARYqgqkldpwsdeepgkimheLRQGELVNTKEVPF 326
Cdd:pfam06202  18 GPSIIAGYHWFS-DWGRDTFIA-LPGLLLVTgrfEEARDIILTFAGY-------------------LRHGLIPNLFPAGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  327 GPYYGTLDATPLFLILLSEYYNWTGDKKFFMELFPAAEKALKWMEQygdrdGDSFLEYIREkEGGLVNQG-------WKD 399
Cdd:pfam06202  77 EPRYNTVDASLWFIYAVQKYLEYAPDAEFLRRIFPTIQEILGAYFK-----GTDFNIGLDP-EDGLIHGGsrgnqltWMD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  400 SKdsvvfSDGRLADPPIALA-EIQGYAYDALMRMARIyGELGKKEKANGLLRKAAHLKERFHRAFWMEDKKYFAEALDGE 478
Cdd:pfam06202 151 AK-----VGGWPVTPRDGKAvEINALWYNALRFASRL-ANKILGEDKSSYKELAEKIKDNFEKKFWNNKRGILYDVIDPS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  479 KRKVDSITSNPghcLWsgmleyekAVLVADRLLSDE------------LFSGWGIRTMSCREAAYNP----------ASY 536
Cdd:pfam06202 225 LPKDYQLRPNF---LI--------ALSLAPTLLSPEkakkaldlaeeeLLTPYGLRTLDPDDPDYLGtyrgdqdsrdMAY 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  537 HNGSVWP-------------HDNSLIALGLARYGFKDHLKKLISGMIAaseyfeycRLPELFcgfsrEDGGPVRyPVACS 603
Cdd:pfam06202 294 HQGTVWPwligyflraklkfGDDSKLALDLVAPLLEGHYKHLQEAGWG--------GIPELF-----DGDGPYC-PRGCI 359

                  ....*...
gi 302200897  604 PQAWAAAT 611
Cdd:pfam06202 360 AQAWSVAE 367
Bac_rhamnosid6H pfam17389
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain; This family consists of bacterial ...
325-488 9.19e-09

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: 57.71  E-value: 9.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  325 PFGPYYGTLDATPLFLILLSEYYNWTGDKKFFMELFPAAEKALKWMEQYGDRDGDSFLEYirekegGLVNQGWKDSKDSV 404
Cdd:pfam17389  89 VRGPGSPGPEWGDAIVIVPWALYRNYGDTRILQDQYPSMKRWLDYLLQRSDDGLWGLSGW------GLGDWLDPDGRPGD 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897  405 VFSDGRLadppIALAeiqgYAYDALMRMARIYGELGKKEKANGLLRKAAHLKERFHRAFWMEDKKYFAealdgekrkVDS 484
Cdd:pfam17389 163 APTPGDL----VATA----YYYRSLGLMAKMAELLGKDEDAKRYAALAEELKAAFNKKYLDTETGSYA---------NDT 225

                  ....
gi 302200897  485 ITSN 488
Cdd:pfam17389 226 QTAN 229
TreA COG1626
Neutral trehalase [Carbohydrate transport and metabolism];
433-565 5.10e-04

Neutral trehalase [Carbohydrate transport and metabolism];


Pssm-ID: 441233  Cd Length: 438  Bit Score: 42.91  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302200897 433 ARIYGELGKKEKANGLLRKAAHLKERFHRAFWMEDKKYFAEA--LDGEKRKVDSITS-NPghcLWSGMLEYEKAVLVADR 509
Cdd:COG1626  252 AKAYALAGDPAKAAEYRARAERRKEAINRYLWDEERGFYFDYdfVTGKQTAVLSAAAfYP---LFAGIATPEQAARVAET 328
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302200897 510 LLSDELFSGwGIRTmscreaaynpASYHNGSVWPHDN-----SLIAL-GLARYGFKDHLKKL 565
Cdd:COG1626  329 LEPQLLKPG-GLVT----------TLVNSGQQWDAPNgwaplQWMAVkGLRNYGYDDLAREI 379
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH