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Conserved domains on  [gi|1000956291|ref|XP_015577567|]
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4-alpha-glucanotransferase DPE2 [Ricinus communis]

Protein Classification

PLN02950 family protein( domain architecture ID 11477311)

PLN02950 family protein

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN02950 PLN02950
4-alpha-glucanotransferase
 8-913 0e+00

4-alpha-glucanotransferase


:

Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 1912.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291   8 SGTESVKSVNLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPVHEGEELIWYGTVSIPSAFSCEYSYYVVDDERN 87
Cdd:PLN02950    1 SGKKSLKSVTLSFRIPYYTQWGQSLLVCGSEPLLGSWNVKKGLLLSPVHQGDELVWEGSVSVPEGFSCEYSYYVVDDNKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  88 VLRWEMGKKRKLLLPECVNDGETAELHDLWQ-SGGDAILFRSAFKDVIFRKSWNLNIERPLEVQNKLEKEDGIVVHFKIC 166
Cdd:PLN02950   81 VLRWEAGKKRKLVLPEGLQGGELVELHDLWQkSGPEALFFRSAFKDVIFRHSWGVNTERPLGALNKPPAPDEIVVRFKIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 167 CPNVEEETSVYVIGSTSKLGQWKVQNGLKLSYAGDLIWQADLLMPRSDFPIKYRYCKYNKAGTISLETGQNRELSLD-SS 245
Cdd:PLN02950  161 CPRLEEGTSVYVTGSIAQLGNWQVDDGLKLNYTGDSIWEADCLVPKSDFPIKYKYALQTAEGLVSLELGVNRELSLDsSS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 246 KVPPRHIFLSDGMLRGMPWRGAGVAIPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSVHGMWWDSYPY 325
Cdd:PLN02950  241 GKPPSYIVASDGAFREMPWRGAGVAVPVFSIRSEEDVGVGEFLDLKLLVDWAVKSGLHLVQLLPVNDTSVHGMWWDSYPY 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 326 SSLSVFALHPLYLTVHALSENLPEDVKREIQGAKERLDGKDVDYEATLATKLSIAKQVFALEKDLILNSGSFQKYFSENE 405
Cdd:PLN02950  321 SSLSVFALHPLYLRVQALSERLPEDLKAEIQKARKQLDKKDVDYEATLATKLSIAKKVFDLEKDLTLNSSSFKKFFSENE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 406 EWLKPYAAFCFLRDFFETSDHSQWGRFSQYSNEKLVKLVSKDSLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGD 485
Cdd:PLN02950  401 HWLKPYAAFCFLRDFFETSDHSQWGRFSDFSDEKLEKLVSPGSLHYDTICFHYYIQYHLHSQLSEAAEYARKKGVVLKGD 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 486 LPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFF 565
Cdd:PLN02950  481 LPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFF 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 566 RIWELPEHAMTGLIGKFRPSIPLSQEELEKDGIWDFDRLSRPYIRQEFLQEKLGASWTFIAANFLNEHQKGRYEFKEDCN 645
Cdd:PLN02950  561 RIWELPAHAVTGLVGKFRPSIPLSQEELEQEGIWDFDRLSRPYIRQEFLQEKFGDRWTEIASNFLNEYQKGCYEFKEDCN 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 646 TEKKITSKLKTLAEKSMF-ESEDKIRHGLFDLLKNIVLIRDPEDARKFYPRFNLEDTSSFEDLDDHSKNVLKRLYYDYYF 724
Cdd:PLN02950  641 TEKKIAAKLKRLAEKSWLlEEEEKIRRGLFDLLQNVVLIRDPEDPRKFYPRFNLEDTSSFQDLDDHSKNVLKRLYYDYYF 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 725 NRQENLWRKNAMKTLPVLLNSSDMLACGEDLGLIPACVHPVMQELGLIGLRIQRMPSEPDLEFGIPSKYSYMTVCAPSCH 804
Cdd:PLN02950  721 HRQEDLWRENALKTLPALLNSSDMLACGEDLGLVPACVHPVMQELGLLGLRIQRMPSEPGLEFGIPSQYSYMTVCAPSCH 800

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 805 DCSTFRAWWEEDEERRLRFFKIVVGSDILPPSQCTPDVACFIIRQHVEAPSMWAIFPLQDLLALKKEYMTRPATEETIND 884
Cdd:PLN02950  801 DCSTLRAWWEEDEERRERFYKHVLGSDGPPPSQCVPDVAHFILQQHVEAPSMWAIFPLQDLLALKEEYTTRPANEETIND 880

                         890       900
                  ....*....|....*....|....*....
gi 1000956291 885 PTNPKHYWRYRVHVTLESLMKDKELKSTL 913
Cdd:PLN02950  881 PTNPKHYWRFRVHVTLESLLADKDLLATI 909
 
Name Accession Description Interval E-value
PLN02950 PLN02950
4-alpha-glucanotransferase
 8-913 0e+00

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 1912.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291   8 SGTESVKSVNLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPVHEGEELIWYGTVSIPSAFSCEYSYYVVDDERN 87
Cdd:PLN02950    1 SGKKSLKSVTLSFRIPYYTQWGQSLLVCGSEPLLGSWNVKKGLLLSPVHQGDELVWEGSVSVPEGFSCEYSYYVVDDNKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  88 VLRWEMGKKRKLLLPECVNDGETAELHDLWQ-SGGDAILFRSAFKDVIFRKSWNLNIERPLEVQNKLEKEDGIVVHFKIC 166
Cdd:PLN02950   81 VLRWEAGKKRKLVLPEGLQGGELVELHDLWQkSGPEALFFRSAFKDVIFRHSWGVNTERPLGALNKPPAPDEIVVRFKIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 167 CPNVEEETSVYVIGSTSKLGQWKVQNGLKLSYAGDLIWQADLLMPRSDFPIKYRYCKYNKAGTISLETGQNRELSLD-SS 245
Cdd:PLN02950  161 CPRLEEGTSVYVTGSIAQLGNWQVDDGLKLNYTGDSIWEADCLVPKSDFPIKYKYALQTAEGLVSLELGVNRELSLDsSS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 246 KVPPRHIFLSDGMLRGMPWRGAGVAIPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSVHGMWWDSYPY 325
Cdd:PLN02950  241 GKPPSYIVASDGAFREMPWRGAGVAVPVFSIRSEEDVGVGEFLDLKLLVDWAVKSGLHLVQLLPVNDTSVHGMWWDSYPY 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 326 SSLSVFALHPLYLTVHALSENLPEDVKREIQGAKERLDGKDVDYEATLATKLSIAKQVFALEKDLILNSGSFQKYFSENE 405
Cdd:PLN02950  321 SSLSVFALHPLYLRVQALSERLPEDLKAEIQKARKQLDKKDVDYEATLATKLSIAKKVFDLEKDLTLNSSSFKKFFSENE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 406 EWLKPYAAFCFLRDFFETSDHSQWGRFSQYSNEKLVKLVSKDSLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGD 485
Cdd:PLN02950  401 HWLKPYAAFCFLRDFFETSDHSQWGRFSDFSDEKLEKLVSPGSLHYDTICFHYYIQYHLHSQLSEAAEYARKKGVVLKGD 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 486 LPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFF 565
Cdd:PLN02950  481 LPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFF 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 566 RIWELPEHAMTGLIGKFRPSIPLSQEELEKDGIWDFDRLSRPYIRQEFLQEKLGASWTFIAANFLNEHQKGRYEFKEDCN 645
Cdd:PLN02950  561 RIWELPAHAVTGLVGKFRPSIPLSQEELEQEGIWDFDRLSRPYIRQEFLQEKFGDRWTEIASNFLNEYQKGCYEFKEDCN 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 646 TEKKITSKLKTLAEKSMF-ESEDKIRHGLFDLLKNIVLIRDPEDARKFYPRFNLEDTSSFEDLDDHSKNVLKRLYYDYYF 724
Cdd:PLN02950  641 TEKKIAAKLKRLAEKSWLlEEEEKIRRGLFDLLQNVVLIRDPEDPRKFYPRFNLEDTSSFQDLDDHSKNVLKRLYYDYYF 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 725 NRQENLWRKNAMKTLPVLLNSSDMLACGEDLGLIPACVHPVMQELGLIGLRIQRMPSEPDLEFGIPSKYSYMTVCAPSCH 804
Cdd:PLN02950  721 HRQEDLWRENALKTLPALLNSSDMLACGEDLGLVPACVHPVMQELGLLGLRIQRMPSEPGLEFGIPSQYSYMTVCAPSCH 800

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 805 DCSTFRAWWEEDEERRLRFFKIVVGSDILPPSQCTPDVACFIIRQHVEAPSMWAIFPLQDLLALKKEYMTRPATEETIND 884
Cdd:PLN02950  801 DCSTLRAWWEEDEERRERFYKHVLGSDGPPPSQCVPDVAHFILQQHVEAPSMWAIFPLQDLLALKEEYTTRPANEETIND 880

                         890       900
                  ....*....|....*....|....*....
gi 1000956291 885 PTNPKHYWRYRVHVTLESLMKDKELKSTL 913
Cdd:PLN02950  881 PTNPKHYWRFRVHVTLESLLADKDLLATI 909
Glyco_hydro_77 pfam02446
4-alpha-glucanotransferase; These enzymes EC:2.4.1.25 transfer a segment of a (1,4) ...
 271-899 5.33e-173

4-alpha-glucanotransferase; These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.


Pssm-ID: 460560  Cd Length: 458  Bit Score: 511.60  E-value: 5.33e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 271 IPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSvhgmwWDSYPYSSLSVFALHPLYLTvhalsenlPED 350
Cdd:pfam02446   1 LPLYSLPSPRSYGIGDFGDLYEFVDFLAEAGQSYWQILPLGPTT-----EDTSPYSSFSAFAGNPLYID--------LEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 351 VKREIQGAKERLDGKD-VDYEATLATKLSIAKQVFALEKDLILN--SGSFQKYFSENEEWLKPYAAFCFLRDFFETSDHS 427
Cdd:pfam02446  68 LQEEGLLLREELNALErVDYEAVYALKLALLRKAFERFKAKALAgrRAEFEAFCEENGEWLEDYALFMALKDGFGGASWR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 428 QWGR-FSQYSNEKLVKLvskDSLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGDLPIGVDRNSVDTWVYPNLFRM 506
Cdd:pfam02446 148 EWPEeLRDRDPEALAAF---REELADEIEFHKFLQYLFFRQWAALKAYANEKGIKIIGDLPIGVARDSADVWANPELFAL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 507 NTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRIWELPEHAMTGLIGkfrpsi 586
Cdd:pfam02446 225 DESAGAPPDYFSATGQNWGNPLYNWDALEKDGYAWWIDRLRANLKLFDALRIDHFRGFFRYWEIPAGEKTAFNG------ 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 587 plsqeelekdgiwdfdrlsrpyirqeflqeklgaswtfiaanflnehqkgryefkedcntekkitsklktlaeksmfese 666
Cdd:pfam02446     --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 667 dkirhglfdllknivlirdpedarkfyprfnledtssfedlddhsknvlkrLYYDYYFNRQENLWRKNAMKTlpvllnss 746
Cdd:pfam02446 299 ---------------------------------------------------LWVKYPGEDLFAALALELQRG-------- 319

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 747 DMLACGEDLGLIPACVHPVMQELGLIGLRIQRMPSEPDLE-FGIPSKYSYMTVCAPSCHDCSTFRAWWEEDEERrlRFFK 825
Cdd:pfam02446 320 DLLVIAEDLGTVPPEVRELLDELGIPGMKVLQFAFDDDDEnFYLPHNYPYNSVVYTGTHDNPTLRGWWDRAREK--EFLL 397

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1000956291 826 IVVGsdilPPSQCTPDVACFIIRQHVEAPSMWAIFPLQDLLalkkeymtrPATEETINDPTNPKHYWRYRVHVT 899
Cdd:pfam02446 398 DYLG----APSESEEEIVWALIRLALASVADLAIIPLQDLL---------LGEEARMNIPGTVGGNWRWRLHLT 458
MalQ COG1640
4-alpha-glucanotransferase [Carbohydrate transport and metabolism];
265-922 1.26e-91

4-alpha-glucanotransferase [Carbohydrate transport and metabolism];


Pssm-ID: 441247  Cd Length: 505  Bit Score: 300.52  E-value: 1.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 265 RGAGVAIPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSVHGmwWDSyPYSSLSVFALHPLYLTVHALS 344
Cdd:COG1640     1 RAWGILLHLYSLPSARNWGIGDFGDLYRFVDFLAEAGQDFWQILPLHATFPPY--GDS-PYSPSSRFAGNPLYIDLEALP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 345 E--NLPEDvkrEIQGAKERLDGKDVDYEATLATKLSIAKQVFA--LEKDLILNSGSFQKYFSENEEWLKPYAAFCFLRDF 420
Cdd:COG1640    78 EfgLLSAA---DLAALAPLRDADRVDYDAVAALKLAALRLAFErfRARADAERRAAFEAFCAEEGEWLEDYALFMALKEH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 421 FETSDHSQWGR-FSQYSNEKLVKLVSKdslHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGDLPIGVDRNSVDTWV 499
Cdd:COG1640   155 FGGRGWREWPEeLRDRDPPAVAAFRAE---LADEIEFHKFLQWLFFRQWAALKAYANAAGIGLIGDLPIGVAPDSADVWA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 500 YPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRIWELPEHAMTGLI 579
Cdd:COG1640   232 NPELFALDAVAGAPPDYFSPTGQLWGNPPYDWDALAETGYAWWIDRLRANLRLADALRIDHFRGLERLWWIPAGEETAAN 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 580 GKFRPSiplsqeelekdgiwDFDRLsrpyirqeflqeklgaswtfiaanflnehqkgryefkedcntekkitskLKTLAE 659
Cdd:COG1640   312 GAWVKY--------------PGEDL-------------------------------------------------FGILAL 328

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 660 KsmfesedkiRHGlfdllknivlirdpedarkfyprfnledtssfedlddhsknvlkrlyydyyfnrqenlwrknamktL 739
Cdd:COG1640   329 E---------RGR------------------------------------------------------------------L 333

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 740 PVLlnssdmlacGEDLGLIPACVHPVMQELGLIGLRI----QRMPSEPDLefgiPSKYSYMTVCAPSCHDCSTFRAWWE- 814
Cdd:COG1640   334 PVI---------AEDLGTVPPEVRELLDRFGLPGMKVlqfeFDDPDGPFL----PHNYPRNAVAYTGTHDNPTLAGWWEg 400

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 815 ----------EDEERRLRFFKIVVGSDILPPSQCTPDVACFIIRqhveAPSMWAIFPLQDLLALkkeymtrpatEETIND 884
Cdd:COG1640   401 ldldlreeraEREEERAALLRYLGRDPEDMEEELVWALIRLLAA----SVAALAIVPLQDLLGL----------EARMNL 466

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 1000956291 885 P-TNPKHYWRYRVHVTLESLMKDKELKSTLKGLIHGSGR 922
Cdd:COG1640   467 PgTVDGYNWRWRLPVDLEDLFADPEARRLLAALTELYGR 505
CBM20_DPE2_repeat1 cd05815
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 17-117 1.30e-54

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: 184.57  E-value: 1.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  17 NLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPVHEGEELIWYGTVSIPSAFSCEYSYYVVDDERNVLRWEMGKK 96
Cdd:cd05815     1 TLSFKLPYYTQWGQSLLICGSDPLLGSWNVKKGLLLKPSHQGDVLVWSGSISVPPGFSSEYNYYVVDDRKSVLRSESGEK 80

                          90       100
                  ....*....|....*....|.
gi 1000956291  97 RKLLLPECVNDGETAELHDLW 117
Cdd:cd05815    81 RKLVLPEGLQGGESVELRDLW 101
malQ TIGR00217
4-alpha-glucanotransferase; This enzyme is known as amylomaltase and disproportionating enzyme. ...
 265-585 2.61e-48

4-alpha-glucanotransferase; This enzyme is known as amylomaltase and disproportionating enzyme. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 129321 [Multi-domain]  Cd Length: 513  Bit Score: 180.44  E-value: 2.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 265 RGAGVAIPMFSVRSEndLGVGEFLDLK-LLVDWAVESGFHLVQLL---PINDTSvhgmwwdSYPYSSLSVFALHPLYLTV 340
Cdd:TIGR00217  14 RKSGILLQLYSLPSE--WGIGDLGDGAyKFIDFLKAGSQSVWQIHalyPADFTR-------SPPYSISSARALNVYYIDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 341 HALSE-NLPEDVKREIQGAKerlDGKDVDYEATLATKLSIAKQVFA--LEKDLILNSGSFQKYFSENEEWLKPYAAFCFL 417
Cdd:TIGR00217  85 EALDEfIDLPLSLLKEAELR---ESDRVDYSKKIALKDTALKEAFLnfINRASADEVRSFAEFKKKQSDWLADFASFVAQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 418 RDFF----ETSDHSQWGRFSQYSNEKLVKLVSKdsLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGDLPIGVDRN 493
Cdd:TIGR00217 162 KEAFfkesKNAGWVLWDKGIQKRNEPELFKLRN--ILSKEIKFQEWLQWLFFSQFQALKRYANDMGIGLYGDLPVFVAYD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 494 SVDTWVYPNLFRMNTSTGAP------PDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRI 567
Cdd:TIGR00217 240 SADVWADPELFCLRASAGAPkpaglgPDYFLEQGQNWGLPPYDWNVLKARGYEWWIKRLGANMQYADILRIDHFRGFVSL 319

                         330
                  ....*....|....*...
gi 1000956291 568 WELPEHAMTGLIGKFRPS 585
Cdd:TIGR00217 320 WWVPAGESTAFNGAWVHY 337
CBM_2 smart01065
Starch binding domain;
16-103 8.22e-20

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 84.71  E-value: 8.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291   16 VNLSFRIPY-YTQWGQSLLVCGSKPILGSWNVKKGLLLSPVhEGEELIWYGTVSIPSA-FSCEYSYYVVDDERNVlRWEM 93
Cdd:smart01065   1 VSVTFKVRNgYTQPGESVYVVGSVPELGNWNPKKAVPLSPD-TDGYPLWKGTVSLPPAgTTIEYKYVKVDEDGSV-TWES 78

                           90
                   ....*....|
gi 1000956291   94 GKKRKLLLPE 103
Cdd:smart01065  79 GPNRRLTVPE 88
 
Name Accession Description Interval E-value
PLN02950 PLN02950
4-alpha-glucanotransferase
 8-913 0e+00

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 1912.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291   8 SGTESVKSVNLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPVHEGEELIWYGTVSIPSAFSCEYSYYVVDDERN 87
Cdd:PLN02950    1 SGKKSLKSVTLSFRIPYYTQWGQSLLVCGSEPLLGSWNVKKGLLLSPVHQGDELVWEGSVSVPEGFSCEYSYYVVDDNKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  88 VLRWEMGKKRKLLLPECVNDGETAELHDLWQ-SGGDAILFRSAFKDVIFRKSWNLNIERPLEVQNKLEKEDGIVVHFKIC 166
Cdd:PLN02950   81 VLRWEAGKKRKLVLPEGLQGGELVELHDLWQkSGPEALFFRSAFKDVIFRHSWGVNTERPLGALNKPPAPDEIVVRFKIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 167 CPNVEEETSVYVIGSTSKLGQWKVQNGLKLSYAGDLIWQADLLMPRSDFPIKYRYCKYNKAGTISLETGQNRELSLD-SS 245
Cdd:PLN02950  161 CPRLEEGTSVYVTGSIAQLGNWQVDDGLKLNYTGDSIWEADCLVPKSDFPIKYKYALQTAEGLVSLELGVNRELSLDsSS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 246 KVPPRHIFLSDGMLRGMPWRGAGVAIPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSVHGMWWDSYPY 325
Cdd:PLN02950  241 GKPPSYIVASDGAFREMPWRGAGVAVPVFSIRSEEDVGVGEFLDLKLLVDWAVKSGLHLVQLLPVNDTSVHGMWWDSYPY 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 326 SSLSVFALHPLYLTVHALSENLPEDVKREIQGAKERLDGKDVDYEATLATKLSIAKQVFALEKDLILNSGSFQKYFSENE 405
Cdd:PLN02950  321 SSLSVFALHPLYLRVQALSERLPEDLKAEIQKARKQLDKKDVDYEATLATKLSIAKKVFDLEKDLTLNSSSFKKFFSENE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 406 EWLKPYAAFCFLRDFFETSDHSQWGRFSQYSNEKLVKLVSKDSLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGD 485
Cdd:PLN02950  401 HWLKPYAAFCFLRDFFETSDHSQWGRFSDFSDEKLEKLVSPGSLHYDTICFHYYIQYHLHSQLSEAAEYARKKGVVLKGD 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 486 LPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFF 565
Cdd:PLN02950  481 LPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFF 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 566 RIWELPEHAMTGLIGKFRPSIPLSQEELEKDGIWDFDRLSRPYIRQEFLQEKLGASWTFIAANFLNEHQKGRYEFKEDCN 645
Cdd:PLN02950  561 RIWELPAHAVTGLVGKFRPSIPLSQEELEQEGIWDFDRLSRPYIRQEFLQEKFGDRWTEIASNFLNEYQKGCYEFKEDCN 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 646 TEKKITSKLKTLAEKSMF-ESEDKIRHGLFDLLKNIVLIRDPEDARKFYPRFNLEDTSSFEDLDDHSKNVLKRLYYDYYF 724
Cdd:PLN02950  641 TEKKIAAKLKRLAEKSWLlEEEEKIRRGLFDLLQNVVLIRDPEDPRKFYPRFNLEDTSSFQDLDDHSKNVLKRLYYDYYF 720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 725 NRQENLWRKNAMKTLPVLLNSSDMLACGEDLGLIPACVHPVMQELGLIGLRIQRMPSEPDLEFGIPSKYSYMTVCAPSCH 804
Cdd:PLN02950  721 HRQEDLWRENALKTLPALLNSSDMLACGEDLGLVPACVHPVMQELGLLGLRIQRMPSEPGLEFGIPSQYSYMTVCAPSCH 800

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 805 DCSTFRAWWEEDEERRLRFFKIVVGSDILPPSQCTPDVACFIIRQHVEAPSMWAIFPLQDLLALKKEYMTRPATEETIND 884
Cdd:PLN02950  801 DCSTLRAWWEEDEERRERFYKHVLGSDGPPPSQCVPDVAHFILQQHVEAPSMWAIFPLQDLLALKEEYTTRPANEETIND 880

                         890       900
                  ....*....|....*....|....*....
gi 1000956291 885 PTNPKHYWRYRVHVTLESLMKDKELKSTL 913
Cdd:PLN02950  881 PTNPKHYWRFRVHVTLESLLADKDLLATI 909
PLN03236 PLN03236
4-alpha-glucanotransferase; Provisional
 249-923 0e+00

4-alpha-glucanotransferase; Provisional


Pssm-ID: 178774  Cd Length: 745  Bit Score: 864.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 249 PRHIFLSDGMLR-GMPWRGAGVAIPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSVHGMWWDSYPYSS 327
Cdd:PLN03236   43 ERRIIHRDGHFRhGGAWKGSGMALPVFSLRSAESVGAGDFGDLEALVDFAAEAGMSVVQLLPVNDTCVHGTFWDSYPYSS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 328 LSVFALHPLYLTVHALSENLPE------------DVKREIQGAKERLDGKDVDYEATLATKLSIAKQVFALEKDLILNSG 395
Cdd:PLN03236  123 LSVHALHPLYLKLKELVEEAANaaaagpdagrlaALAAEIDAAKHALDLKEIDYEATMKEKLMFAKRAFEADGAKFLASD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 396 SFQKYFSENEEWLKPYAAFCFLRDFFETSDHSQWGR-FSQYSNEKLVKLVSKDSLHYEMICFHYYIQFHLHLQLSEAAEY 474
Cdd:PLN03236  203 ACERFVKANASWLKPYAVFCALRDLFGTAEHWRWGDlFATFAAAILAKIDCPGGDLYESTRFFFYLQYHLDRQLRRAAAH 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 475 ARKKGVILKGDLPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFT 554
Cdd:PLN03236  283 AAAKGVILKGDLPIGVDKASVDTWMHPKLFRMDTSTGAPPDAFDANGQNWGFPTYDWEEMAEDDYAWWRARMQHLEQFFS 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 555 AYRIDHILGFFRIWELPEHAMTGLIGKFRPSIPLSQEELEKDGIWDFDRLSRPYIRQEFLQEKLGASWTFIAANFLNE-- 632
Cdd:PLN03236  363 AIRIDHILGFFRIWELPAHAKTGRLGRFRPSLPIRKDELAARGLWDLDRLCEPWIQSEELEALFGDNDGEAAGRFFEEtd 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 633 -------HQKGRYEFKEDCNTEKKITSKLKTLAEKS----MFESEDKIRHGLFDLLKNIVLIRDPEDARKFYPRFNLEDT 701
Cdd:PLN03236  443 aetkpdgTTRGLWKFRKEFDTEQAIFASEALKPRDDfpdhLNDEQEELRAGLMQLFQNRCLLRDPDDADAFYPRFEFEET 522

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 702 SSFEDLDDHSKNVLKRLYYDYYFNRQENLWRKNAMKTLPVLLNSSDMLACGEDLGLIPACVHPVMQELGLIGLRIQRMPS 781
Cdd:PLN03236  523 TSFQALDDWARDALRDLSDDYFFARQDATWRENARKTLPALLKCTEMLVCGEDLGFTPMCVPPVLDELGILGLRIQRMPH 602

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 782 EPDL-EFGIPSKYSYMTVCAPSCHDCSTFRAWWEEDEERRLRFFKIVVGSDilpPSQCTPDVACFIIRQHVEAPSMWAIF 860
Cdd:PLN03236  603 DGESgEFGRPERYPYETVCSPSCHDTMTTRAWWEADAARRARYAELFQAGN---DDACEPHVMRAILRQHIASPSSIAIF 679

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1000956291 861 PLQDLLALKKEYMTRPATEETINDPTNPKHYWRYRVHVTLESLMKDKELKSTLKGLIHGSGRS 923
Cdd:PLN03236  680 PAQDLLALDEEYAKRPAEEETINDPTNPKHYWRFRIHVACEDLLANAAFLGEIKDLVREGGQM 742
Glyco_hydro_77 pfam02446
4-alpha-glucanotransferase; These enzymes EC:2.4.1.25 transfer a segment of a (1,4) ...
 271-899 5.33e-173

4-alpha-glucanotransferase; These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.


Pssm-ID: 460560  Cd Length: 458  Bit Score: 511.60  E-value: 5.33e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 271 IPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSvhgmwWDSYPYSSLSVFALHPLYLTvhalsenlPED 350
Cdd:pfam02446   1 LPLYSLPSPRSYGIGDFGDLYEFVDFLAEAGQSYWQILPLGPTT-----EDTSPYSSFSAFAGNPLYID--------LEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 351 VKREIQGAKERLDGKD-VDYEATLATKLSIAKQVFALEKDLILN--SGSFQKYFSENEEWLKPYAAFCFLRDFFETSDHS 427
Cdd:pfam02446  68 LQEEGLLLREELNALErVDYEAVYALKLALLRKAFERFKAKALAgrRAEFEAFCEENGEWLEDYALFMALKDGFGGASWR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 428 QWGR-FSQYSNEKLVKLvskDSLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGDLPIGVDRNSVDTWVYPNLFRM 506
Cdd:pfam02446 148 EWPEeLRDRDPEALAAF---REELADEIEFHKFLQYLFFRQWAALKAYANEKGIKIIGDLPIGVARDSADVWANPELFAL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 507 NTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRIWELPEHAMTGLIGkfrpsi 586
Cdd:pfam02446 225 DESAGAPPDYFSATGQNWGNPLYNWDALEKDGYAWWIDRLRANLKLFDALRIDHFRGFFRYWEIPAGEKTAFNG------ 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 587 plsqeelekdgiwdfdrlsrpyirqeflqeklgaswtfiaanflnehqkgryefkedcntekkitsklktlaeksmfese 666
Cdd:pfam02446     --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 667 dkirhglfdllknivlirdpedarkfyprfnledtssfedlddhsknvlkrLYYDYYFNRQENLWRKNAMKTlpvllnss 746
Cdd:pfam02446 299 ---------------------------------------------------LWVKYPGEDLFAALALELQRG-------- 319

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 747 DMLACGEDLGLIPACVHPVMQELGLIGLRIQRMPSEPDLE-FGIPSKYSYMTVCAPSCHDCSTFRAWWEEDEERrlRFFK 825
Cdd:pfam02446 320 DLLVIAEDLGTVPPEVRELLDELGIPGMKVLQFAFDDDDEnFYLPHNYPYNSVVYTGTHDNPTLRGWWDRAREK--EFLL 397

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1000956291 826 IVVGsdilPPSQCTPDVACFIIRQHVEAPSMWAIFPLQDLLalkkeymtrPATEETINDPTNPKHYWRYRVHVT 899
Cdd:pfam02446 398 DYLG----APSESEEEIVWALIRLALASVADLAIIPLQDLL---------LGEEARMNIPGTVGGNWRWRLHLT 458
MalQ COG1640
4-alpha-glucanotransferase [Carbohydrate transport and metabolism];
265-922 1.26e-91

4-alpha-glucanotransferase [Carbohydrate transport and metabolism];


Pssm-ID: 441247  Cd Length: 505  Bit Score: 300.52  E-value: 1.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 265 RGAGVAIPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSVHGmwWDSyPYSSLSVFALHPLYLTVHALS 344
Cdd:COG1640     1 RAWGILLHLYSLPSARNWGIGDFGDLYRFVDFLAEAGQDFWQILPLHATFPPY--GDS-PYSPSSRFAGNPLYIDLEALP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 345 E--NLPEDvkrEIQGAKERLDGKDVDYEATLATKLSIAKQVFA--LEKDLILNSGSFQKYFSENEEWLKPYAAFCFLRDF 420
Cdd:COG1640    78 EfgLLSAA---DLAALAPLRDADRVDYDAVAALKLAALRLAFErfRARADAERRAAFEAFCAEEGEWLEDYALFMALKEH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 421 FETSDHSQWGR-FSQYSNEKLVKLVSKdslHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGDLPIGVDRNSVDTWV 499
Cdd:COG1640   155 FGGRGWREWPEeLRDRDPPAVAAFRAE---LADEIEFHKFLQWLFFRQWAALKAYANAAGIGLIGDLPIGVAPDSADVWA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 500 YPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRIWELPEHAMTGLI 579
Cdd:COG1640   232 NPELFALDAVAGAPPDYFSPTGQLWGNPPYDWDALAETGYAWWIDRLRANLRLADALRIDHFRGLERLWWIPAGEETAAN 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 580 GKFRPSiplsqeelekdgiwDFDRLsrpyirqeflqeklgaswtfiaanflnehqkgryefkedcntekkitskLKTLAE 659
Cdd:COG1640   312 GAWVKY--------------PGEDL-------------------------------------------------FGILAL 328

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 660 KsmfesedkiRHGlfdllknivlirdpedarkfyprfnledtssfedlddhsknvlkrlyydyyfnrqenlwrknamktL 739
Cdd:COG1640   329 E---------RGR------------------------------------------------------------------L 333

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 740 PVLlnssdmlacGEDLGLIPACVHPVMQELGLIGLRI----QRMPSEPDLefgiPSKYSYMTVCAPSCHDCSTFRAWWE- 814
Cdd:COG1640   334 PVI---------AEDLGTVPPEVRELLDRFGLPGMKVlqfeFDDPDGPFL----PHNYPRNAVAYTGTHDNPTLAGWWEg 400

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 815 ----------EDEERRLRFFKIVVGSDILPPSQCTPDVACFIIRqhveAPSMWAIFPLQDLLALkkeymtrpatEETIND 884
Cdd:COG1640   401 ldldlreeraEREEERAALLRYLGRDPEDMEEELVWALIRLLAA----SVAALAIVPLQDLLGL----------EARMNL 466

                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 1000956291 885 P-TNPKHYWRYRVHVTLESLMKDKELKSTLKGLIHGSGR 922
Cdd:COG1640   467 PgTVDGYNWRWRLPVDLEDLFADPEARRLLAALTELYGR 505
PRK14508 PRK14508
4-alpha-glucanotransferase; Provisional
 265-585 4.73e-74

4-alpha-glucanotransferase; Provisional


Pssm-ID: 237738  Cd Length: 497  Bit Score: 252.81  E-value: 4.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 265 RGAGVAIPMFSVRSenDLGVGEF-LDLKLLVDWAVESGFHLVQLLPINDTSvHGmwwDSyPYSSLSVFALHPLYLTVHAL 343
Cdd:PRK14508    5 RKSGILLHITSLPG--SYGIGDFgKGAYEFIDFLAEAGQSYWQILPLGPTG-YG---DS-PYQSFSAFAGNPLLIDLEAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 344 SE--NLPEDvkrEIQGAKERLDGKDVDYEATLATKLSIAKQVFA-LEKDLILNSGSFQKYFSENEEWLKPYAAFCFLRDF 420
Cdd:PRK14508   78 VDdgLLDES---DLEGLPFGSNPERVDYDLVREAKRPLLRKAFErFLRASLERAEAFEAFCEEEAYWLDDYALFMALKEH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 421 FETSDHSQWGRFSQYSNEKLVKLVSKDslHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGDLPIGVDRNSVDTWVY 500
Cdd:PRK14508  155 FGGLPWNEWPEPLRKRDPEALAKAREE--LADEILYHKFLQYLFFRQWKALKAYANDKGIEIIGDLPIYVAYDSADVWAN 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 501 PNLFRMNTST------GAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRIWELPEHA 574
Cdd:PRK14508  233 PELFKLDEDGkptvvaGVPPDYFSETGQLWGNPVYNWDALRKDGYRWWIERLRRSFKLYDIVRIDHFRGFEAYWEIPAGE 312

                         330
                  ....*....|.
gi 1000956291 575 MTGLIGKFRPS 585
Cdd:PRK14508  313 KTAINGRWVPG 323
PRK14510 PRK14510
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;
265-922 1.81e-59

bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase;


Pssm-ID: 237739 [Multi-domain]  Cd Length: 1221  Bit Score: 222.07  E-value: 1.81e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  265 RGAGVAIPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPINDTSVHGMWWDSyPYSSLSVFALHPLYLTVHALS 344
Cdd:PRK14510   723 RACGILMHLYSLRSQRPWGIGDFEELYALVDFLAEGGQSLWGVNPLHPLGLGDPERAS-PYQPSSRRAGNPLLISLDLLP 801

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  345 EN--LPEDVKREIQGAKERLDGKD---VDYEATLATKLSIAKQVFA------LEKDLILNSGSFQKYFSENEEWLKPYAA 413
Cdd:PRK14510   802 EAglLTENEAALGSAGPELAKLSAlgsVDYAWVEALKEKLLRAAYEafrdklPRYPLDLSSPEFDRFIEEGGDWLRRYAI 881

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  414 FCFLRDFFETSDHSQWGrfSQYSNEKLVKLVSKDSLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILK--GDLPIGVD 491
Cdd:PRK14510   882 FKALKAKFPGKGWHQWP--EEYRLRKPPALEAFAEKYAEEVNYAKFLQYIADRQWQAAKDYAQEQGLSIGfyGDLAIGVA 959

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  492 RNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRIWELP 571
Cdd:PRK14510   960 PDGADAWAERSCFALDVSIGAPPDYFNPEGQNWGLPPYDPRALRRDGYRWFIERIRANMRHAGALRIDHVRGLERLFEVP 1039

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  572 EHAMTgligkfrpsiplsqeeleKDGIWDfdrlsrpyirqeflqeklgaswtfiaanflnehqkgRYEFKEdcntekkit 651
Cdd:PRK14510  1040 QGASA------------------KEGAYL------------------------------------KGPGEE--------- 1056

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  652 sklktLAEKSMFESEDkirhglfdllknivlirdpedarkfyprfnledtssfedlddhsknvlkrlyydyyfnrqenlw 731
Cdd:PRK14510  1057 -----LFGQVALESQR---------------------------------------------------------------- 1067

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  732 rknamktlpvllnsSDMLACGEDLGLIPACVHPVMQELGLIGLRIQRMPSEPDLEFGIPSKYSYMTVCAPSCHDCSTFRA 811
Cdd:PRK14510  1068 --------------AQCPVIGEDLGTIPSGVRELLAILGILSYRVLQFERLGEGNFLPPPLYNALAAAYVGTHDLPTLAG 1133

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  812 WWEedeerrlrffkivvGSDILPPSQCtpDVACFIIRQHVEAPSMWAIFPLQDLLAlKKEYMTRPAteeTINDptNPKhy 891
Cdd:PRK14510  1134 WWE--------------GVDLSEKEQL--GAAEAVIEMLARSPAILVIIQLQDLLG-SNVRMNLPG---TIRE--NPN-- 1189

                          650       660       670
                   ....*....|....*....|....*....|.
gi 1000956291  892 WRYRVHVTLESLMKDKELKSTLKGLIHGSGR 922
Cdd:PRK14510  1190 WRRKLSAPVERLTLTQRACARLRGLAEKRGR 1220
CBM20_DPE2_repeat1 cd05815
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 17-117 1.30e-54

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: 184.57  E-value: 1.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  17 NLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPVHEGEELIWYGTVSIPSAFSCEYSYYVVDDERNVLRWEMGKK 96
Cdd:cd05815     1 TLSFKLPYYTQWGQSLLICGSDPLLGSWNVKKGLLLKPSHQGDVLVWSGSISVPPGFSSEYNYYVVDDRKSVLRSESGEK 80

                          90       100
                  ....*....|....*....|.
gi 1000956291  97 RKLLLPECVNDGETAELHDLW 117
Cdd:cd05815    81 RKLVLPEGLQGGESVELRDLW 101
malQ TIGR00217
4-alpha-glucanotransferase; This enzyme is known as amylomaltase and disproportionating enzyme. ...
 265-585 2.61e-48

4-alpha-glucanotransferase; This enzyme is known as amylomaltase and disproportionating enzyme. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 129321 [Multi-domain]  Cd Length: 513  Bit Score: 180.44  E-value: 2.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 265 RGAGVAIPMFSVRSEndLGVGEFLDLK-LLVDWAVESGFHLVQLL---PINDTSvhgmwwdSYPYSSLSVFALHPLYLTV 340
Cdd:TIGR00217  14 RKSGILLQLYSLPSE--WGIGDLGDGAyKFIDFLKAGSQSVWQIHalyPADFTR-------SPPYSISSARALNVYYIDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 341 HALSE-NLPEDVKREIQGAKerlDGKDVDYEATLATKLSIAKQVFA--LEKDLILNSGSFQKYFSENEEWLKPYAAFCFL 417
Cdd:TIGR00217  85 EALDEfIDLPLSLLKEAELR---ESDRVDYSKKIALKDTALKEAFLnfINRASADEVRSFAEFKKKQSDWLADFASFVAQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 418 RDFF----ETSDHSQWGRFSQYSNEKLVKLVSKdsLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGDLPIGVDRN 493
Cdd:TIGR00217 162 KEAFfkesKNAGWVLWDKGIQKRNEPELFKLRN--ILSKEIKFQEWLQWLFFSQFQALKRYANDMGIGLYGDLPVFVAYD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 494 SVDTWVYPNLFRMNTSTGAP------PDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRI 567
Cdd:TIGR00217 240 SADVWADPELFCLRASAGAPkpaglgPDYFLEQGQNWGLPPYDWNVLKARGYEWWIKRLGANMQYADILRIDHFRGFVSL 319

                         330
                  ....*....|....*...
gi 1000956291 568 WELPEHAMTGLIGKFRPS 585
Cdd:TIGR00217 320 WWVPAGESTAFNGAWVHY 337
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 160-257 8.77e-38

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: 136.30  E-value: 8.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 160 VVHFKICCPNVEEETSVYVIGSTSKLGQWKVQNGLKLSYAGDLIWQADLLMPRSDFPIKYRYCKYNKA-GTISLETGQNR 238
Cdd:cd05816     1 VVQFKILCPYVPKGQSVYVTGSSPELGNWDPQKALKLSDVGFPIWEADIDISKDSFPFEYKYIIANKDsGVVSWENGPNR 80

                          90
                  ....*....|....*....
gi 1000956291 239 ELSLDSSKVPPRHIFLSDG 257
Cdd:cd05816    81 ELSAPSLKGESSTLIVSDG 99
PRK14507 PRK14507
malto-oligosyltrehalose synthase;
268-571 2.16e-37

malto-oligosyltrehalose synthase;


Pssm-ID: 237737 [Multi-domain]  Cd Length: 1693  Bit Score: 152.95  E-value: 2.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  268 GVAIPMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPindtsVHGMWWD----SYPYSSLSVFALHPLYLTVHAL 343
Cdd:PRK14507   174 GLAAQLYGLRSARNWGIGDFGDLGRLVRDAALRGASFLGLSP-----LHALFPTdpakASPYSPSSRLFLNTLYIDVEAV 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  344 SENLPEDVKREIQGAKE---RLDG----KDVDYEATLATKLSIAKQVFA--LEKDLILNSG---SFQKYFSENEEWLKPY 411
Cdd:PRK14507   249 PDFAECEAARLLVHAPEfqaRLEAlraaELVDYAGVAEAKFEVLEALWRhfRARHLERNTGrdaGFRAFRAEGGESLRSH 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  412 AAFCFLRDFFETSDHSQWGRFS-----QYSNEKLVKLVSKDslHYEMICFHYYIQFHLHLQLSEAAEYARKKG--VILKG 484
Cdd:PRK14507   329 ALFEALQEHFRAEDAHWWGWPDwpeayRDPGTPAVRAFAEE--HAERVEYHEYLQWLADLQLAAAGERAQALGmrLGLYR 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  485 DLPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGF 564
Cdd:PRK14507   407 DLAVGVDRGGSETWSHPELFANGASIGAPPDELNPKGQDWGLPPFDPLELERDGYAPFRALLRANMRHAGALRIDHVMQL 486


                   ....*..
gi 1000956291  565 FRIWELP 571
Cdd:PRK14507   487 MRLFWIP 493
PLN02635 PLN02635
disproportionating enzyme
 265-583 1.52e-34

disproportionating enzyme


Pssm-ID: 215341  Cd Length: 538  Bit Score: 139.89  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 265 RGAGVAIPMFSVRSENdlGVGEFLD-LKLLVDWAVESGFHLVQLLP-INDTSVHGMWWDsyPYSSLSVFALHPLYLTVha 342
Cdd:PLN02635   28 RRAGILLHPTSLPGPY--GIGDLGDeAFRFLDWLASTGCSVWQVLPlVPPGRKGGEDGS--PYSGQDANCGNTLLISL-- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 343 lsENLPEDVKREIQGAKERLDGKDVDYEATLATKLS-IAKqvfALEKdLILNSGSFQKY---FSENEE---WLKPYAAFC 415
Cdd:PLN02635  102 --EELVKDGLLEEDELPEPVPVGKVDFSAVAELKDPlIAK---AAER-LLLSDGELKEEledFRKDPEissWLEDAALFA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 416 FLRDFFETSDHSQWGrfSQYSNEKLVKLVSKDSLHYEMICFHYYIQFHLHLQLSEAAEYARKKGVILKGDLPIGVDRNSV 495
Cdd:PLN02635  176 AIDNTLNAKAWWDWP--EPLRDRHPAALEAIRQSHKDFIDEFIAQQFLFQRQWQAVRSYANEKGISIIGDMPIYVGGHSA 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 496 DTWVYPNLFRMNTS------TGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMAKYFTAYRIDHILGFFRIWE 569
Cdd:PLN02635  254 DVWANRKLFLLNKTgfpllvSGVPPDAFSETGQLWGSPLYDWKAMAKDGYSWWAGRMRRALELYDEFRIDHFRGFAGYWA 333

                         330
                  ....*....|....
gi 1000956291 570 LPEHAMTGLIGKFR 583
Cdd:PLN02635  334 VPADAKTAMNGRWK 347
CBM_20 pfam00686
Starch binding domain;
16-110 2.30e-26

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 103.91  E-value: 2.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  16 VNLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPVHEGEELIWYGTVSIPSAFSCEYSYYVVDDERNVlRWEMGK 95
Cdd:pfam00686   1 VSVTFNVNATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYSSYPLWSGTVSLPAGTTIEYKYIKVDSDGSV-TWESGP 79

                          90
                  ....*....|....*
gi 1000956291  96 KRKLLLPECVNDGET 110
Cdd:pfam00686  80 NRSYTVPASGASTTT 94
malQ PRK11052
4-alpha-glucanotransferase; Provisional
 247-571 1.47e-25

4-alpha-glucanotransferase; Provisional


Pssm-ID: 236831 [Multi-domain]  Cd Length: 695  Bit Score: 113.44  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 247 VPPRHIFLSDGMLRGMPWRGAGVAipMFSVRSENDLGVGEFLDLKLLVDWAVESGFHLVQLLPIndtsvHGMwwdsYP-- 324
Cdd:PRK11052  126 VAPKRCYEPQALLQGKKLWGACVQ--LYTLRSEHNWGIGDFGDLKQMLEDVAKRGGDFIGLNPI-----HAL----YPan 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 325 ------YSSLSVFALHPLYLTVHALSE-NLPEDVKR-----EIQGAKERLDGKD-VDYEATLATKLSI---AKQVFALEK 388
Cdd:PRK11052  195 pesaspYSPSSRRWLNVIYIDVNAVEDfQQSEEAQAwwqsaETQQRLQQARAAEwVDYSTVTALKLTAlrlAFKQFAQRD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 389 DLILNSGSFQKYFSENEEWLKPYAAFCFLRDFFETSDHSQWG------RFSQYSNEKlVKLVSKDslHYEMICFHYYIQF 462
Cdd:PRK11052  275 KDDEQMQAFRQFVAEGGESLLWQAAFDALHAHLVKEDEMRWGwpvwpeEYQDVDSPA-VQQFCEE--HADEVDFYLWLQW 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 463 HLHLQLSEAAEYARKKG--VILKGDLPIGVDRNSVDTWVYPNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYA 540
Cdd:PRK11052  352 LADSQFAACWQLSQQLGmpIGLYRDLAVGVAEGGAETWCDRELYCLKASVGAPPDILGPLGQNWGLPPMDPHVLQARAYQ 431

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1000956291 541 WW----RArltQMaKYFTAYRIDHILGFFRIWELP 571
Cdd:PRK11052  432 PFidllRA---NM-QHCGALRIDHVMSLLRLWWIP 462
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 19-117 7.23e-22

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: 90.82  E-value: 7.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  19 SFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPvhEGEELIWYGTVSIPSA--FSCEYSYYVVDDERNVlRWEMGKK 96
Cdd:cd05467     3 RFQVRCTTQFGQSVYVVGSHPELGNWDPAKALRLNT--SNSYPLWTGEIPLPAPegQVIEYKYVIVDDDGNV-QWESGSN 79

                          90       100
                  ....*....|....*....|.
gi 1000956291  97 RKLLLPEcvndGETAELHDLW 117
Cdd:cd05467    80 RVLTVPS----TSSLIVVDDW 96
CBM_2 smart01065
Starch binding domain;
16-103 8.22e-20

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 84.71  E-value: 8.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291   16 VNLSFRIPY-YTQWGQSLLVCGSKPILGSWNVKKGLLLSPVhEGEELIWYGTVSIPSA-FSCEYSYYVVDDERNVlRWEM 93
Cdd:smart01065   1 VSVTFKVRNgYTQPGESVYVVGSVPELGNWNPKKAVPLSPD-TDGYPLWKGTVSLPPAgTTIEYKYVKVDEDGSV-TWES 78

                           90
                   ....*....|
gi 1000956291   94 GKKRKLLLPE 103
Cdd:smart01065  79 GPNRRLTVPE 88
CBM_2 smart01065
Starch binding domain;
159-244 6.10e-17

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 76.62  E-value: 6.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  159 IVVHFKICCPNVEEETSVYVIGSTSKLGQWKVQNGLKLSYAGD--LIWQADLLMPRSDFPIKYRYCKYNKAGTISLETGQ 236
Cdd:smart01065   1 VSVTFKVRNGYTQPGESVYVVGSVPELGNWNPKKAVPLSPDTDgyPLWKGTVSLPPAGTTIEYKYVKVDEDGSVTWESGP 80


                   ....*...
gi 1000956291  237 NRELSLDS 244
Cdd:smart01065  81 NRRLTVPE 88
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 161-247 1.94e-16

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: 75.41  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 161 VHFKICCPNVEEEtSVYVIGSTSKLGQWKVQNGLKLSYAG-DLIWQADL-LMPRSDFPIKYRYCKYNKAGTISLETGQNR 238
Cdd:cd05467     2 VRFQVRCTTQFGQ-SVYVVGSHPELGNWDPAKALRLNTSNsYPLWTGEIpLPAPEGQVIEYKYVIVDDDGNVQWESGSNR 80


                  ....*....
gi 1000956291 239 ELSLDSSKV 247
Cdd:cd05467    81 VLTVPSTSS 89
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 16-117 2.05e-15

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: 72.40  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  16 VNLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPVHEGeelIWYGTVSIPSAFSCEYSYYVVDDERNVLrWEMGK 95
Cdd:cd05808     1 VAVTFNVTATTVWGQNVYVVGNVPELGNWSPANAVALSAATYP---VWSGTVDLPAGTAIEYKYIKKDGSGTVT-WESGP 76

                          90       100
                  ....*....|....*....|..
gi 1000956291  96 KRKLLLPecvnDGETAELHDLW 117
Cdd:cd05808    77 NRTATTP----ASGTLTLNDTW 94
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 29-115 1.54e-14

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: 70.05  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  29 GQSLLVCGSKPILGSWNVKKGLLLSPVHegeELIWYGTVSIP-SAFSCEYSYYVVDDERNVLRWEMGKKRKLLLPECVND 107
Cdd:cd05816    14 GQSVYVTGSSPELGNWDPQKALKLSDVG---FPIWEADIDISkDSFPFEYKYIIANKDSGVVSWENGPNRELSAPSLKGE 90


                  ....*...
gi 1000956291 108 GETAELHD 115
Cdd:cd05816    91 SSTLIVSD 98
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 15-117 1.03e-11

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: 62.29  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  15 SVNLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSPV-HEGEELIWYGTVSIPSAFSCEYSYYVVDDERNVLrWEM 93
Cdd:cd05811     6 TVAVTFNERVTTSYGENIKIVGSIPQLGNWDTSSAVALSASqYTSSNPLWSVTIPLPAGTSFEYKFIRKESDGSVT-WES 84

                          90       100
                  ....*....|....*....|....
gi 1000956291  94 GKKRKLLLPECVndGETAELHDLW 117
Cdd:cd05811    85 DPNRSYTVPSGC--GTTATVDDSW 106
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 17-97 4.67e-11

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: 60.18  E-value: 4.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  17 NLSFRIPYYTQWGQSLLVCGSKPILGSWNVKKGLLLSpVHEGEelIWYGTVSIPSAFSCEYSYYVVDDER-NVLRWEMGK 95
Cdd:cd05817     1 MVTFKIHYPTQFGEAVYISGNCNQLGNWNPSKAKRMQ-WNEGD--LWTVDVGIPESVYIEYKYFVSNYDDpNTVLWESGP 77


                  ..
gi 1000956291  96 KR 97
Cdd:cd05817    78 NR 79
CBM_20 pfam00686
Starch binding domain;
161-245 4.45e-09

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 54.60  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 161 VHFKICCPNVEEEtSVYVIGSTSKLGQWKVQNGLKLS---YAGDLIWQADLLMPrSDFPIKYRYCKYNKAGTISLETGQN 237
Cdd:pfam00686   3 VTFNVNATTQYGQ-SVYIVGSIPELGNWNPKKAIALSaseYSSYPLWSGTVSLP-AGTTIEYKYIKVDSDGSVTWESGPN 80


                  ....*...
gi 1000956291 238 RELSLDSS 245
Cdd:pfam00686  81 RSYTVPAS 88
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 176-245 4.74e-09

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: 54.29  E-value: 4.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291 176 VYVIGSTSKLGQWKVQNGLKLSYAGDLIWQADLLMPrSDFPIKYRYCKYNKAGTISLETGQNRELSLDSS 245
Cdd:cd05808    17 VYVVGNVPELGNWSPANAVALSAATYPVWSGTVDLP-AGTAIEYKYIKKDGSGTVTWESGPNRTATTPAS 85
CBM20_genethonin_1 cd05813
Genethonin-1, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Genethonin-1 ...
 16-99 9.61e-09

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: 53.66  E-value: 9.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  16 VNLSFRIPYYTQWGQSLL-VCGSKPILGSWNVkkgllLSPVHEGEELIWYGTVSIPSAFSCEYSYYVVDDERnVLRWEMG 94
Cdd:cd05813     1 VNVTFRVHYITHSDAQLVaVTGDHEELGSWHS-----YIPLQYVKDGFWSASVSLPVDTHVEWKFVLVENGQ-VTRWEEC 74


                  ....*
gi 1000956291  95 KKRKL 99
Cdd:cd05813    75 SNRLL 79
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 29-92 7.95e-08

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: 51.55  E-value: 7.95e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1000956291  29 GQSLLVCGSKPILGSWNVKKGLLLSPVHEGEELiWYGTVSIPSAFSCEYSYYVV----DDERN---VLRWE 92
Cdd:cd05814    15 GEVVAVVGSLPVLGNWQPEKAVPLEKEDDDCNL-WKASIELPRGVDFQYRYFVAvvlnDSGPCqviVRKWE 84
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 25-129 8.49e-07

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: 48.17  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  25 YTQWGQSLLVCGSKPILGSWNVKKGLLLSPVHEGeelIWYGTVSIPSAFSCEysyyvvddernvlrWemgkkrklllpEC 104
Cdd:cd05810    11 TTQLGQSVYVVGNVPQLGNWSPADAVKLDPTAYP---TWSGSISLPASTNVE--------------W-----------KC 62

                          90       100
                  ....*....|....*....|....*.
gi 1000956291 105 VNDGET-AELHDLWQSGGDAILFRSA 129
Cdd:cd05810    63 LKRNETnPTAGVQWQGGGNNQLTTGN 88
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 160-224 1.20e-05

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: 45.39  E-value: 1.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1000956291 160 VVHFKICCPNVEEETSVYVIGSTSKLGQWKVQNGLKLSYAGD--LIWQADLLMPRsDFPIKYRYCKY 224
Cdd:cd05814     2 RVTFRVFASELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDDdcNLWKASIELPR-GVDFQYRYFVA 67
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 175-238 3.05e-05

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: 43.80  E-value: 3.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1000956291 175 SVYVIGSTSKLGQWKVQNGLKLS---Y-AGDLIWQADLLMPRSDfPIKYRYCKYNKAGTISLETGQNR 238
Cdd:cd05811    22 NIKIVGSIPQLGNWDTSSAVALSasqYtSSNPLWSVTIPLPAGT-SFEYKFIRKESDGSVTWESDPNR 88
CBM20_CGTase cd05807
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ...
 25-103 5.24e-05

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: 43.32  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000956291  25 YTQWGQSLLVCGSKPILGSWNVKK--GLLLSPVHEgEELIWYGTVSIPSAFSCEYSYYVVDDERNVLrWEMGKKRKLLLP 102
Cdd:cd05807    13 TTQLGENVYLVGNVHELGNWDPSKaiGPFFNQVVY-QYPNWYYDVSVPAGTTIEFKFIKKNGDNTVT-WESGSNHTYTAP 90


                  .
gi 1000956291 103 E 103
Cdd:cd05807    91 S 91
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 161-238 2.51e-04

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: 41.31  E-value: 2.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1000956291 161 VHFKICCPnVEEETSVYVIGSTSKLGQWKVQNGLKLSYAGDLIWQADLLMPRS-DFPIKYRYCKYNKAGTISLETGQNR 238
Cdd:cd05817     2 VTFKIHYP-TQFGEAVYISGNCNQLGNWNPSKAKRMQWNEGDLWTVDVGIPESvYIEYKYFVSNYDDPNTVLWESGPNR 79
CBM20_water_dikinase cd05818
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ...
 176-242 5.87e-03

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: 37.10  E-value: 5.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1000956291 176 VYVIGSTSKLGQWKVQNGLKLSYAGdliWQADLLMPrSDFPIKYRYCKYNKAGTISLETGQNRELSL 242
Cdd:cd05818    18 VAILGSTKELGSWKKKVPMNWTENG---WVCDLELD-GGELVEYKFVIVKRDGSVIWEGGNNRVLEL 80
 
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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