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Conserved domains on  [gi|2081999175|emb|CAE8663257|]
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unnamed protein product [Apocalathium aciculiferum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM_2 smart01065
Starch binding domain;
182-264 2.14e-22

Starch binding domain;


:

Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 92.03  E-value: 2.14e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   182 TVTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGASFPVWSATAQIPVESPAAEWKLVICGPTGDTRWETCPN 261
Cdd:smart01065    2 SVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPLWKGTVSLPPAGTTIEYKYVKVDEDGSVTWESGPN 81


                    ...
gi 2081999175   262 RTT 264
Cdd:smart01065   82 RRL 84
CBM_2 smart01065
Starch binding domain;
21-92 8.05e-17

Starch binding domain;


:

Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 76.23  E-value: 8.05e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2081999175    21 PFGAQLLVVGSLDETGCWQPASGFSLKPSGKETPLWSASARFSPGAATLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:smart01065   13 QPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPLWKGTVSLPPAGTTIEYKYVKVDEDGSVTWESGPNRRL 84
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
 573-759 1.94e-08

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


:

Pssm-ID: 214625 [Multi-domain]  Cd Length: 252  Bit Score: 56.23  E-value: 1.94e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   573 CEDAYF------TSEHALGVADGvgcmvqfaKYGVNAAAYAADLM-SYASQAFSEGGVADENFAGSVEERAAAAVAFAEQ 645
Cdd:smart00332   23 MEDAHVitpdlsDSGGFFGVFDG--------HGGSEAAKFLSKNLpEILAEELIKEKDELEDVEEALRKAFLSTDEEILE 94

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   646 GADAYGASTITTMALDGSTAGCANLGDSGFLLLRKTQrgmaVVTRSEEqqHSWNCPYQLTRL----PKALACKFPNISLD 721
Cdd:smart00332   95 ELEALSGSTAVVALISGNKLYVANVGDSRAVLCRNGK----AVQLTED--HKPSNEDERARIeaagGFVINGRVNGVLAL 168

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2081999175   722 TAADCDRYRFQVRV-------------GDLVLLFTDGLRDNLHEREILHIV 759
Cdd:smart00332  169 SRAIGDFFLKPYVSaepdvtvveltekDDFLILASDGLWDVLSNQEVVDIV 219
 
Name Accession Description Interval E-value
CBM_2 smart01065
Starch binding domain;
182-264 2.14e-22

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 92.03  E-value: 2.14e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   182 TVTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGASFPVWSATAQIPVESPAAEWKLVICGPTGDTRWETCPN 261
Cdd:smart01065    2 SVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPLWKGTVSLPPAGTTIEYKYVKVDEDGSVTWESGPN 81


                    ...
gi 2081999175   262 RTT 264
Cdd:smart01065   82 RRL 84
CBM_20 pfam00686
Starch binding domain;
182-263 1.88e-18

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 81.18  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  182 TVTFEAHCRgTAPGDILRIVGSSPSFGSWNPKEGLRLSTSG-ASFPVWSATAQIPVeSPAAEWKLVICGPTGDTRWETCP 260
Cdd:pfam00686    2 SVTFNVNAT-TQYGQSVYIVGSIPELGNWNPKKAIALSASEySSYPLWSGTVSLPA-GTTIEYKYIKVDSDGSVTWESGP 79


                   ...
gi 2081999175  261 NRT 263
Cdd:pfam00686   80 NRS 82
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 183-263 5.65e-18

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 80.03  E-value: 5.65e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  183 VTFEAHCRgTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGaSFPVWSATAQIPV-ESPAAEWKLVICGPTGDTRWETCPN 261
Cdd:cd05467      2 VRFQVRCT-TQFGQSVYVVGSHPELGNWDPAKALRLNTSN-SYPLWTGEIPLPApEGQVIEYKYVIVDDDGNVQWESGSN 79


                   ..
gi 2081999175  262 RT 263
Cdd:cd05467     80 RV 81
CBM_2 smart01065
Starch binding domain;
21-92 8.05e-17

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 76.23  E-value: 8.05e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2081999175    21 PFGAQLLVVGSLDETGCWQPASGFSLKPSGKETPLWSASARFSPGAATLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:smart01065   13 QPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPLWKGTVSLPPAGTTIEYKYVKVDEDGSVTWESGPNRRL 84
CBM_20 pfam00686
Starch binding domain;
14-92 3.93e-16

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 74.63  E-value: 3.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   14 FSALVEPPFGAQLLVVGSLDETGCWQPASGFSLKPSGKET-PLWSASARFSPGAaTLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:pfam00686    5 FNVNATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYSSyPLWSGTVSLPAGT-TIEYKYIKVDSDGSVTWESGPNRSY 83
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 14-92 1.83e-14

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99883  Cd Length: 95  Bit Score: 69.70  E-value: 1.83e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2081999175   14 FSALVEPPFGAQLLVVGSLDETGCWQPASGFSLKPSGkeTPLWSASARFsPGAATLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:cd05808      5 FNVTATTVWGQNVYVVGNVPELGNWSPANAVALSAAT--YPVWSGTVDL-PAGTAIEYKYIKKDGSGTVTWESGPNRTA 80
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
 573-759 1.94e-08

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 214625 [Multi-domain]  Cd Length: 252  Bit Score: 56.23  E-value: 1.94e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   573 CEDAYF------TSEHALGVADGvgcmvqfaKYGVNAAAYAADLM-SYASQAFSEGGVADENFAGSVEERAAAAVAFAEQ 645
Cdd:smart00332   23 MEDAHVitpdlsDSGGFFGVFDG--------HGGSEAAKFLSKNLpEILAEELIKEKDELEDVEEALRKAFLSTDEEILE 94

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   646 GADAYGASTITTMALDGSTAGCANLGDSGFLLLRKTQrgmaVVTRSEEqqHSWNCPYQLTRL----PKALACKFPNISLD 721
Cdd:smart00332   95 ELEALSGSTAVVALISGNKLYVANVGDSRAVLCRNGK----AVQLTED--HKPSNEDERARIeaagGFVINGRVNGVLAL 168

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2081999175   722 TAADCDRYRFQVRV-------------GDLVLLFTDGLRDNLHEREILHIV 759
Cdd:smart00332  169 SRAIGDFFLKPYVSaepdvtvveltekDDFLILASDGLWDVLSNQEVVDIV 219
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
574-765 1.14e-07

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


Pssm-ID: 440396 [Multi-domain]  Cd Length: 247  Bit Score: 54.06  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  574 EDAYFTSEHA----LGVADGVGcmvqfakyGVNAAAYAADL-MSYASQAFSEGGVADEN-----FAGSVEE-----RAAA 638
Cdd:COG0631     17 EDAFLVALDPggglFVVADGMG--------GHAAGEVASRLaVETLAELFQEALAPDPEdleeaLREAIRAanraiLELA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  639 AVAFAEQGAdaygASTITTMALDGSTAGCANLGDSGFLLLRKTQ----------------RGMAvvTRSEEQQHSWNcpY 702
Cdd:COG0631     89 QEDPELAGM----GTTLVAALIAGGRLYIAHVGDSRAYLLRDGEleqltrdhslvqelvdAGRI--TPEEARTHPQR--N 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2081999175  703 QLTRlpkALackfpniSLDTAADCDRYRFQVRVGDLVLLFTDGLRDNLHEREILHIVDRALPP 765
Cdd:COG0631    161 VLTR---AL-------GTDDDVEPDISPLELEPGDRLLLCSDGLTDMVSDEEIAEILASAGDP 213
PLN02950 PLN02950
4-alpha-glucanotransferase
 23-103 2.49e-07

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 54.73  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   23 GAQLLVVGSLDETGCWQPASGFSLKPSGkeTPLWSASARFSPGAATLEYKFVQVLSGGAAVWEDGPNRVLRLDLGSGVPS 102
Cdd:PLN02950   167 GTSVYVTGSIAQLGNWQVDDGLKLNYTG--DSIWEADCLVPKSDFPIKYKYALQTAEGLVSLELGVNRELSLDSSSGKPP 244


                   .
gi 2081999175  103 S 103
Cdd:PLN02950   245 S 245
PLN02950 PLN02950
4-alpha-glucanotransferase
 170-298 7.73e-06

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 50.10  E-value: 7.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  170 DAASLSPSPGLGTVTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGASFpvWSATAQIPVESPAAEWKLVICG 249
Cdd:PLN02950   142 GALNKPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDDGLKLNYTGDSI--WEADCLVPKSDFPIKYKYALQT 219

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2081999175  250 PTGDTRWETCPNRTTRLPPPAPGVPPsewTVRLHwEGSCAEPDARGRGV 298
Cdd:PLN02950   220 AEGLVSLELGVNRELSLDSSSGKPPS---YIVAS-DGAFREMPWRGAGV 264
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
 574-759 4.39e-05

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083 [Multi-domain]  Cd Length: 254  Bit Score: 46.17  E-value: 4.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  574 EDAYF-------TSEHALGVADGVGcmvqfakyGVNAAAYAADLMSYA----------------SQAFSEG-GVADENFA 629
Cdd:cd00143     16 EDAVVikpnlnnEDGGLFGVFDGHG--------GHAAGEFASKLLVEElleeleetltlseediEEALRKAfLRADEEIL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  630 GSVEERAaaavafaeqgADAYGASTITTMALDGSTAGCANLGDSGFLLLRKTQrgMAVVTRseeqQHSWNCPYQL----- 704
Cdd:cd00143     88 EEAQDEP----------DDARSGTTAVVALIRGNKLYVANVGDSRAVLCRNGE--AVQLTK----DHKPVNEEEReriek 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2081999175  705 -------TRLPKALA--------CKFPNISL--DTaadcdryrFQVRV---GDLVLLFTDGLRDNLHEREILHIV 759
Cdd:cd00143    152 aggrvsnGRVPGVLAvtralgdfDLKPGVSAepDV--------TVVKLtedDDFLILASDGLWDVLSNQEAVDIV 218
PP2C_2 pfam13672
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
 573-754 6.94e-04

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 404547  Cd Length: 209  Bit Score: 41.92  E-value: 6.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  573 CEDAYFTSEHA----LGVADGVGCmvqfAKYGVNAAAYAADLM-SYASQAFSEGGVADENFAGSVEERAAAAVAFAEQGA 647
Cdd:pfam13672   12 CQDAFAVWVLDggwlIAVADGAGS----AKRSDVGARIAVEAAvEALADLLESEEELIEALLRAILNDWLALVKAEALAQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  648 DAYG---ASTITTMALDGSTAGCANLGDsgflllrktqrGMAVVTRSEEQQHSWNCP----Y--QLTRLPKALACKFPNI 718
Cdd:pfam13672   88 DLEPrdyATTLLAAVVTPGGIVFFQIGD-----------GAIVVRDRDGEVQVLSQPdsgeYanETTFLTSEDALDELRI 156

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2081999175  719 sldtaadcdrYRFQVRVGDLVLLFTDGLRDNLHERE 754
Cdd:pfam13672  157 ----------RRLPLEPGDALALMTDGLANSLRDEE 182
 
Name Accession Description Interval E-value
CBM_2 smart01065
Starch binding domain;
182-264 2.14e-22

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 92.03  E-value: 2.14e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   182 TVTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGASFPVWSATAQIPVESPAAEWKLVICGPTGDTRWETCPN 261
Cdd:smart01065    2 SVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPLWKGTVSLPPAGTTIEYKYVKVDEDGSVTWESGPN 81


                    ...
gi 2081999175   262 RTT 264
Cdd:smart01065   82 RRL 84
CBM_20 pfam00686
Starch binding domain;
182-263 1.88e-18

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 81.18  E-value: 1.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  182 TVTFEAHCRgTAPGDILRIVGSSPSFGSWNPKEGLRLSTSG-ASFPVWSATAQIPVeSPAAEWKLVICGPTGDTRWETCP 260
Cdd:pfam00686    2 SVTFNVNAT-TQYGQSVYIVGSIPELGNWNPKKAIALSASEySSYPLWSGTVSLPA-GTTIEYKYIKVDSDGSVTWESGP 79


                   ...
gi 2081999175  261 NRT 263
Cdd:pfam00686   80 NRS 82
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 183-263 5.65e-18

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 80.03  E-value: 5.65e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  183 VTFEAHCRgTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGaSFPVWSATAQIPV-ESPAAEWKLVICGPTGDTRWETCPN 261
Cdd:cd05467      2 VRFQVRCT-TQFGQSVYVVGSHPELGNWDPAKALRLNTSN-SYPLWTGEIPLPApEGQVIEYKYVIVDDDGNVQWESGSN 79


                   ..
gi 2081999175  262 RT 263
Cdd:cd05467     80 RV 81
CBM_2 smart01065
Starch binding domain;
21-92 8.05e-17

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 76.23  E-value: 8.05e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2081999175    21 PFGAQLLVVGSLDETGCWQPASGFSLKPSGKETPLWSASARFSPGAATLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:smart01065   13 QPGESVYVVGSVPELGNWNPKKAVPLSPDTDGYPLWKGTVSLPPAGTTIEYKYVKVDEDGSVTWESGPNRRL 84
CBM_20 pfam00686
Starch binding domain;
14-92 3.93e-16

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 74.63  E-value: 3.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   14 FSALVEPPFGAQLLVVGSLDETGCWQPASGFSLKPSGKET-PLWSASARFSPGAaTLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:pfam00686    5 FNVNATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYSSyPLWSGTVSLPAGT-TIEYKYIKVDSDGSVTWESGPNRSY 83
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 14-92 1.83e-14

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99883  Cd Length: 95  Bit Score: 69.70  E-value: 1.83e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2081999175   14 FSALVEPPFGAQLLVVGSLDETGCWQPASGFSLKPSGkeTPLWSASARFsPGAATLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:cd05808      5 FNVTATTVWGQNVYVVGNVPELGNWSPANAVALSAAT--YPVWSGTVDL-PAGTAIEYKYIKKDGSGTVTWESGPNRTA 80
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 182-263 2.11e-13

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99883  Cd Length: 95  Bit Score: 67.00  E-value: 2.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  182 TVTFEAHCRgTAPGDILRIVGSSPSFGSWNPKEGLRLSTsgASFPVWSATAQIPVeSPAAEWKLVICGPTGDTRWETCPN 261
Cdd:cd05808      2 AVTFNVTAT-TVWGQNVYVVGNVPELGNWSPANAVALSA--ATYPVWSGTVDLPA-GTAIEYKYIKKDGSGTVTWESGPN 77


                   ..
gi 2081999175  262 RT 263
Cdd:cd05808     78 RT 79
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 22-100 3.48e-13

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 66.17  E-value: 3.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   22 FGAQLLVVGSLDETGCWQPASGFSLKPSGKEtPLWSASARFSPGAA-TLEYKFVQVLSGGAAVWEDGPNRVLRLDLGSGV 100
Cdd:cd05467     12 FGQSVYVVGSHPELGNWDPAKALRLNTSNSY-PLWTGEIPLPAPEGqVIEYKYVIVDDDGNVQWESGSNRVLTVPSTSSL 90
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 13-103 1.75e-12

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 64.60  E-value: 1.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   13 VFSALVEPPFGAQLLVVGSLDETGCWQPASGFSLKPSG--KETPLWSASARFSPGAaTLEYKFVQVLSGGAAVWEDGPNR 90
Cdd:cd05811     10 TFNERVTTSYGENIKIVGSIPQLGNWDTSSAVALSASQytSSNPLWSVTIPLPAGT-SFEYKFIRKESDGSVTWESDPNR 88

                           90
                   ....*....|...
gi 2081999175   91 VLRldlgsgVPSS 103
Cdd:cd05811     89 SYT------VPSG 95
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 176-263 1.85e-12

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 64.60  E-value: 1.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  176 PSPGLGTVTFEAHCRgTAPGDILRIVGSSPSFGSWNPKEGLRLSTSG--ASFPVWSATAQIPVESpAAEWKLVICGPTGD 253
Cdd:cd05811      2 ATATTVAVTFNERVT-TSYGENIKIVGSIPQLGNWDTSSAVALSASQytSSNPLWSVTIPLPAGT-SFEYKFIRKESDGS 79

                           90
                   ....*....|
gi 2081999175  254 TRWETCPNRT 263
Cdd:cd05811     80 VTWESDPNRS 89
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 182-262 4.82e-11

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 60.42  E-value: 4.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  182 TVTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTsgASFPVWSATAQIPVESPAAEWKLVICG-PTGDTRWETCP 260
Cdd:cd05816      1 VVQFKILCPYVPKGQSVYVTGSSPELGNWDPQKALKLSD--VGFPIWEADIDISKDSFPFEYKYIIANkDSGVVSWENGP 78


                   ..
gi 2081999175  261 NR 262
Cdd:cd05816     79 NR 80
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
 573-759 1.94e-08

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 214625 [Multi-domain]  Cd Length: 252  Bit Score: 56.23  E-value: 1.94e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   573 CEDAYF------TSEHALGVADGvgcmvqfaKYGVNAAAYAADLM-SYASQAFSEGGVADENFAGSVEERAAAAVAFAEQ 645
Cdd:smart00332   23 MEDAHVitpdlsDSGGFFGVFDG--------HGGSEAAKFLSKNLpEILAEELIKEKDELEDVEEALRKAFLSTDEEILE 94

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   646 GADAYGASTITTMALDGSTAGCANLGDSGFLLLRKTQrgmaVVTRSEEqqHSWNCPYQLTRL----PKALACKFPNISLD 721
Cdd:smart00332   95 ELEALSGSTAVVALISGNKLYVANVGDSRAVLCRNGK----AVQLTED--HKPSNEDERARIeaagGFVINGRVNGVLAL 168

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2081999175   722 TAADCDRYRFQVRV-------------GDLVLLFTDGLRDNLHEREILHIV 759
Cdd:smart00332  169 SRAIGDFFLKPYVSaepdvtvveltekDDFLILASDGLWDVLSNQEVVDIV 219
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 183-265 3.97e-08

Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99891  Cd Length: 100  Bit Score: 52.09  E-value: 3.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  183 VTFEAHCRgTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGASfpVWSATAQIPVESpAAEWKLVICG--PTGDTRWETCP 260
Cdd:cd05817      2 VTFKIHYP-TQFGEAVYISGNCNQLGNWNPSKAKRMQWNEGD--LWTVDVGIPESV-YIEYKYFVSNydDPNTVLWESGP 77


                   ....*
gi 2081999175  261 NRTTR 265
Cdd:cd05817     78 NRVLR 82
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
 22-94 4.63e-08

Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99892  Cd Length: 92  Bit Score: 51.74  E-value: 4.63e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2081999175   22 FGAQLLVVGSLDETGCWQpasgfslkpsgKETPL-WSASARF----SPGAATLEYKFVQVLSGGAAVWEDGPNRVLRL 94
Cdd:cd05818     14 FGEHVAILGSTKELGSWK-----------KKVPMnWTENGWVcdleLDGGELVEYKFVIVKRDGSVIWEGGNNRVLEL 80
CBM20_genethonin_1 cd05813
Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 ...
 183-263 7.35e-08

Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 is a human skeletal muscle protein with no known function. It contains a C-terminal CBM20 domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99887  Cd Length: 95  Bit Score: 50.96  E-value: 7.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  183 VTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGasfpVWSATAQIPVESpAAEWKLVICGPTGDTRWETCPNR 262
Cdd:cd05813      3 VTFRVHYITHSDAQLVAVTGDHEELGSWHSYIPLQYVKDG----FWSASVSLPVDT-HVEWKFVLVENGQVTRWEECSNR 77


                   .
gi 2081999175  263 T 263
Cdd:cd05813     78 L 78
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
574-765 1.14e-07

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


Pssm-ID: 440396 [Multi-domain]  Cd Length: 247  Bit Score: 54.06  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  574 EDAYFTSEHA----LGVADGVGcmvqfakyGVNAAAYAADL-MSYASQAFSEGGVADEN-----FAGSVEE-----RAAA 638
Cdd:COG0631     17 EDAFLVALDPggglFVVADGMG--------GHAAGEVASRLaVETLAELFQEALAPDPEdleeaLREAIRAanraiLELA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  639 AVAFAEQGAdaygASTITTMALDGSTAGCANLGDSGFLLLRKTQ----------------RGMAvvTRSEEQQHSWNcpY 702
Cdd:COG0631     89 QEDPELAGM----GTTLVAALIAGGRLYIAHVGDSRAYLLRDGEleqltrdhslvqelvdAGRI--TPEEARTHPQR--N 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2081999175  703 QLTRlpkALackfpniSLDTAADCDRYRFQVRVGDLVLLFTDGLRDNLHEREILHIVDRALPP 765
Cdd:COG0631    161 VLTR---AL-------GTDDDVEPDISPLELEPGDRLLLCSDGLTDMVSDEEIAEILASAGDP 213
PLN02950 PLN02950
4-alpha-glucanotransferase
 23-103 2.49e-07

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 54.73  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   23 GAQLLVVGSLDETGCWQPASGFSLKPSGkeTPLWSASARFSPGAATLEYKFVQVLSGGAAVWEDGPNRVLRLDLGSGVPS 102
Cdd:PLN02950   167 GTSVYVTGSIAQLGNWQVDDGLKLNYTG--DSIWEADCLVPKSDFPIKYKYALQTAEGLVSLELGVNRELSLDSSSGKPP 244


                   .
gi 2081999175  103 S 103
Cdd:PLN02950   245 S 245
CBM20_laforin cd05806
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 12-88 1.05e-06

Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99881  Cd Length: 112  Bit Score: 48.28  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175   12 FVFSALVEPPFGA-QLLVVGSLDETGCWQPASGFSLKPSGK-----ETPLWSASARFSPG--AATLEYKFVQvLSGGAAV 83
Cdd:cd05806      3 FRFGVVLTFADRDtELLVLGSRPELGSWDPQRAVPMRPARKalspqEPSLWLGEVELSEPgsEDTFWYKFLK-REAGALI 81


                   ....*.
gi 2081999175   84 WE-DGP 88
Cdd:cd05806     82 WEgNGP 87
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 183-235 2.15e-06

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 47.70  E-value: 2.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2081999175  183 VTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGASFPVWSATAQIP 235
Cdd:cd05814      3 VTFRVFASELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDDDCNLWKASIELP 55
PLN02950 PLN02950
4-alpha-glucanotransferase
 170-298 7.73e-06

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 50.10  E-value: 7.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  170 DAASLSPSPGLGTVTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGASFpvWSATAQIPVESPAAEWKLVICG 249
Cdd:PLN02950   142 GALNKPPAPDEIVVRFKIACPRLEEGTSVYVTGSIAQLGNWQVDDGLKLNYTGDSI--WEADCLVPKSDFPIKYKYALQT 219

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2081999175  250 PTGDTRWETCPNRTTRLPPPAPGVPPsewTVRLHwEGSCAEPDARGRGV 298
Cdd:PLN02950   220 AEGLVSLELGVNRELSLDSSSGKPPS---YIVAS-DGAFREMPWRGAGV 264
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 182-257 1.32e-05

Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99885  Cd Length: 97  Bit Score: 44.71  E-value: 1.32e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2081999175  182 TVTFEAHCRGTAPGDILRIVGSSPSFGSWNPKEGLRLSTSGasFPVWSATAQIPVeSPAAEWKLVI---CGPTGDTRWE 257
Cdd:cd05810      2 SVTFSCNNGTTQLGQSVYVVGNVPQLGNWSPADAVKLDPTA--YPTWSGSISLPA-STNVEWKCLKrneTNPTAGVQWQ 77
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 28-92 1.38e-05

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 44.62  E-value: 1.38e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2081999175   28 VVGSLDETGCWQPASGFSLKPSGkeTPLWSASARFSPGAATLEYKFVQVLSG-GAAVWEDGPNRVL 92
Cdd:cd05816     19 VTGSSPELGNWDPQKALKLSDVG--FPIWEADIDISKDSFPFEYKYIIANKDsGVVSWENGPNREL 82
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
 574-759 4.39e-05

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083 [Multi-domain]  Cd Length: 254  Bit Score: 46.17  E-value: 4.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  574 EDAYF-------TSEHALGVADGVGcmvqfakyGVNAAAYAADLMSYA----------------SQAFSEG-GVADENFA 629
Cdd:cd00143     16 EDAVVikpnlnnEDGGLFGVFDGHG--------GHAAGEFASKLLVEElleeleetltlseediEEALRKAfLRADEEIL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  630 GSVEERAaaavafaeqgADAYGASTITTMALDGSTAGCANLGDSGFLLLRKTQrgMAVVTRseeqQHSWNCPYQL----- 704
Cdd:cd00143     88 EEAQDEP----------DDARSGTTAVVALIRGNKLYVANVGDSRAVLCRNGE--AVQLTK----DHKPVNEEEReriek 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2081999175  705 -------TRLPKALA--------CKFPNISL--DTaadcdryrFQVRV---GDLVLLFTDGLRDNLHEREILHIV 759
Cdd:cd00143    152 aggrvsnGRVPGVLAvtralgdfDLKPGVSAepDV--------TVVKLtedDDFLILASDGLWDVLSNQEAVDIV 218
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
 195-266 5.66e-04

Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99892  Cd Length: 92  Bit Score: 39.79  E-value: 5.66e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2081999175  195 GDILRIVGSSPSFGSWNPKEGLRLSTSGasfpvWSATAQIPVESpAAEWKLVICGPTGDTRWETCPNRTTRL 266
Cdd:cd05818     15 GEHVAILGSTKELGSWKKKVPMNWTENG-----WVCDLELDGGE-LVEYKFVIVKRDGSVIWEGGNNRVLEL 80
CBM20_novamyl cd05820
Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1, ...
 23-91 5.77e-04

Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1,4-alpha-maltohydrolase, and AcbD), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Novamyl has a five-domain structure similar to that of cyclodextrin glucanotransferase (CGTase). Novamyl has a substrate-binding surface with an open groove which can accommodate both cyclodextrins and linear substrates. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99893  Cd Length: 103  Bit Score: 40.28  E-value: 5.77e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2081999175   23 GAQLLVVGSLDETGCWQP----ASGFSLKPSgkeTPLWSASARFsPGAATLEYKFVQVLSGGAAVWEDGPNRV 91
Cdd:cd05820     18 GEFLYLTGSVPELGNWSTstdqAVGPLLCPN---WPDWFVVASV-PAGTYIEFKFLKAPADGTGTWEGGSNHA 86
PP2C_2 pfam13672
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
 573-754 6.94e-04

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 404547  Cd Length: 209  Bit Score: 41.92  E-value: 6.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  573 CEDAYFTSEHA----LGVADGVGCmvqfAKYGVNAAAYAADLM-SYASQAFSEGGVADENFAGSVEERAAAAVAFAEQGA 647
Cdd:pfam13672   12 CQDAFAVWVLDggwlIAVADGAGS----AKRSDVGARIAVEAAvEALADLLESEEELIEALLRAILNDWLALVKAEALAQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2081999175  648 DAYG---ASTITTMALDGSTAGCANLGDsgflllrktqrGMAVVTRSEEQQHSWNCP----Y--QLTRLPKALACKFPNI 718
Cdd:pfam13672   88 DLEPrdyATTLLAAVVTPGGIVFFQIGD-----------GAIVVRDRDGEVQVLSQPdsgeYanETTFLTSEDALDELRI 156

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2081999175  719 sldtaadcdrYRFQVRVGDLVLLFTDGLRDNLHERE 754
Cdd:pfam13672  157 ----------RRLPLEPGDALALMTDGLANSLRDEE 182
CBM20_genethonin_1 cd05813
Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 ...
 23-92 8.74e-04

Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 is a human skeletal muscle protein with no known function. It contains a C-terminal CBM20 domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99887  Cd Length: 95  Bit Score: 39.40  E-value: 8.74e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2081999175   23 GAQLL-VVGSLDETGCWQpasGFSLKPSGKETpLWSASArFSPGAATLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:cd05813     14 DAQLVaVTGDHEELGSWH---SYIPLQYVKDG-FWSASV-SLPVDTHVEWKFVLVENGQVTRWEECSNRLL 79
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 22-92 1.70e-03

Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99885  Cd Length: 97  Bit Score: 38.93  E-value: 1.70e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2081999175   22 FGAQLLVVGSLDETGCWQPASGFSLKPSGkeTPLWSASARFsPGAATLEYKFVQVLSGGAA---VWEDGPNRVL 92
Cdd:cd05810     14 LGQSVYVVGNVPQLGNWSPADAVKLDPTA--YPTWSGSISL-PASTNVEWKCLKRNETNPTagvQWQGGGNNQL 84
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 22-92 2.21e-03

CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99882 [Multi-domain]  Cd Length: 101  Bit Score: 38.70  E-value: 2.21e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2081999175   22 FGAQLLVVGSLDETGCWQPAsgfslKPSGK-------ETPLWSASARFsPGAATLEYKFVQVLSGGAAVWEDGPNRVL 92
Cdd:cd05807     16 LGENVYLVGNVHELGNWDPS-----KAIGPffnqvvyQYPNWYYDVSV-PAGTTIEFKFIKKNGDNTVTWESGSNHTY 87
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 22-93 3.81e-03

Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99891  Cd Length: 100  Bit Score: 37.84  E-value: 3.81e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2081999175   22 FGAQLLVVGSLDETGCWQPASGFSLKPSgkETPLWSASARFsPGAATLEYKFV--QVLSGGAAVWEDGPNRVLR 93
Cdd:cd05817     12 FGEAVYISGNCNQLGNWNPSKAKRMQWN--EGDLWTVDVGI-PESVYIEYKYFvsNYDDPNTVLWESGPNRVLR 82
CBM20_DPE2_repeat1 cd05815
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 195-266 5.87e-03

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 1. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 starch binding domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal carbohydrate-binding domains. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99889  Cd Length: 101  Bit Score: 37.42  E-value: 5.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2081999175  195 GDILRIVGSSPSFGSWNPKEGLRLS-TSGASFPVWSATAQIPvESPAAEWK--LVICGPTGdTRWETCPNRTTRL 266
Cdd:cd05815     13 GQSLLICGSDPLLGSWNVKKGLLLKpSHQGDVLVWSGSISVP-PGFSSEYNyyVVDDRKSV-LRSESGEKRKLVL 85
 
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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