|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02316 |
PLN02316 |
synthase/transferase |
28-1130 |
0e+00 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 2084.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 28 MSNARPRGSSPKGFTPKTPVGtSTQNRDLENNGEKEGSITPKSSEIAEANKQTLETQVDEDEEQAIEHSgekkvdeekig 107
Cdd:PLN02316 1 MSTSKPKGSAPRGFAPRTTVE-SSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQVDFQHNSE----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 108 eevslmskkvavangnqvvkngsisrVGKDVTLSEDKIALEGSQNNDLKNDGIVKERSISIDARKTEDDSLQIKLKLEME 187
Cdd:PLN02316 69 --------------------------SAVEEVEAEDEIEVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 188 EklrkketdrlaeekLRKQEIERLAEENFSKGNRLFVYPQMVKPDEDIEVFLNRSLSTLSDEPDILIMGAFNDWRWKSFT 267
Cdd:PLN02316 123 N--------------LRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYLNRSLSTLANEPDVLIMGAFNGWRWKSFT 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 268 FRLSKTHLNGDWWSCQVHVPKEAYKMDFVFFNGQDVYDNNDKKDFYILVEGGMDAFAFDDFLLEEKRRELEKLAKEQAVK 347
Cdd:PLN02316 189 ERLEKTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGGMDEHSFEDFLLEEKRRELEKLAKEEAER 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 348 ERLAEEQRRREEEKAASEADRAQARAEIEKRRTTLQELMKKAARSFNNVCHIEPSEFKGEDMIKLYYNKSSGPLAHANDL 427
Cdd:PLN02316 269 ERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYIEPSEFKAGDTVKLYYNRSSGPLAHSTEI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 428 WVHGGHNNWKDGLSIVERLVSSDKKDGDWWYANVVVPDRAFVLDWVFADGPPQSAAVYDNNHRQDFHAIVPSGIPEELYW 507
Cdd:PLN02316 349 WIHGGYNNWIDGLSIVEKLVKSEEKDGDWWYAEVVVPERALVLDWVFADGPPGNARNYDNNGRQDFHAIVPNNIPEELYW 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 508 VEEEHKIYRKLQEERRLREDAIRAKAEKTARIKAETKEQTLKRFLLSQKHIVYTEPLDVQAGSTVTVFYNPANTILNGKP 587
Cdd:PLN02316 429 VEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLSQKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKP 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 588 EVWFRGSFNRWTHRKGPLPPQKMLPADNGSHVKATVKVPLDAYMMDFVFSEKEDGGIFDNREGMDYHIPVSGGIAKEPPM 667
Cdd:PLN02316 509 EVWFRGSFNRWTHRLGPLPPQKMVPADNGSHLKATVKVPLDAYMMDFVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPM 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 668 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKISHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVY 747
Cdd:PLN02316 589 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVY 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 748 FLEPQNGMFWAGCVYGCKNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSKSRVVFTIHNL 827
Cdd:PLN02316 669 FLEPQNGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNL 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 828 EFGANNIGKAMAYSDKATTVSPTYSREISGNPLIASHLHKFHGILNGIDPDIWDPYNDTYIPVPYTSENVVEGKRAAKEA 907
Cdd:PLN02316 749 EFGANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEA 828
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 908 LQQRLGLKKADLPLVGIITRLTHQKGIHLIKHAIWRTLERGGQvlfypiscfsnslliVVLLGSAPDPRVQNDFVNLANH 987
Cdd:PLN02316 829 LQQRLGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQ---------------VVLLGSAPDPRIQNDFVNLANQ 893
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 988 LHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKERAKAQGL 1067
Cdd:PLN02316 894 LHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFDVDHDKERAQAQGL 973
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050351180 1068 EPNGFSFDGADPAGVDYALNRAISAWYDGRDWFNSLCKKVMEQDWSWNKPALDYLELYHSARK 1130
Cdd:PLN02316 974 EPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSARK 1036
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
668-1127 |
0e+00 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 547.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 668 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKISHVKDLHYQRSYS---WGGTEIKVWFGKVEGL 744
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVkvgGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 745 SVYFLEP-----QNGMFwAGCVYGCKNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSKSR 819
Cdd:cd03791 81 DYYFLDNpeffdRPGLP-GPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 820 VVFTIHNLEF---------------------------GANNIGKA-MAYSDKATTVSPTYSREI-------SGNPLIASH 864
Cdd:cd03791 160 TVFTIHNLAYqglfpldtlaelglppelfhidglefyGQINFLKAgIVYADRVTTVSPTYAKEIltpeygeGLDGVLRAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 865 LHKFHGILNGIDPDIWDPYNDTYIPVPYtSENVVEGKRAAKEALQQRLGLK-KADLPLVGIITRLTHQKGIHLIKHAIWR 943
Cdd:cd03791 240 AGKLSGILNGIDYDEWNPATDKLIPANY-SANDLEGKAENKAALQKELGLPvDPDAPLFGFVGRLTEQKGVDLILDALPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 944 TLERGGQVlfypiscfsnsllivVLLGSApDPRVQNDFVNLANHlhssHHDRARLCLTYDEPLSHLIYAGADFILVPSIF 1023
Cdd:cd03791 319 LLEEGGQL---------------VVLGSG-DPEYEQAFRELAER----YPGKVAVVIGFDEALAHRIYAGADFFLMPSRF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1024 EPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKErakaqglEPNGFSFDGADPAGVDYALNRAISAWYDgRDWFNSL 1103
Cdd:cd03791 379 EPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKL 450
|
490 500
....*....|....*....|....
gi 2050351180 1104 CKKVMEQDWSWNKPALDYLELYHS 1127
Cdd:cd03791 451 QKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
667-1128 |
1.10e-176 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 526.58 E-value: 1.10e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 667 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKiSHVKDLHYQRSYS--WGGTEIK--VWFGKVE 742
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSID-DKLKDLEVVASLEvpLGGRTYYarVLEGPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 743 GLSVYFLEpQNGMFWAGCVYGCKN-----DGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSK 817
Cdd:COG0297 80 GVPVYFID-NPELFDRPGPYGDPDrdypdNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 818 SRVVFTIHNLE----FGANNIGK------------------------AMAYSDKATTVSPTYSREI----SGN---PLIA 862
Cdd:COG0297 159 IKTVFTIHNLAyqgiFPAEILELlglppelftpdglefygqinflkaGIVYADRVTTVSPTYAREIqtpeFGEgldGLLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 863 SHLHKFHGILNGIDPDIWDPYNDTYIPVPYTSENVvEGKRAAKEALQQRLGLK-KADLPLVGIITRLTHQKGIHLIKHAI 941
Cdd:COG0297 239 ARSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPvDPDAPLIGMVSRLTEQKGLDLLLEAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 942 WRTLERGGQVlfypiscfsnsllivVLLGSApDPRVQNDFVNLANHlhssHHDRARLCLTYDEPLSHLIYAGADFILVPS 1021
Cdd:COG0297 318 DELLEEDVQL---------------VVLGSG-DPEYEEAFRELAAR----YPGRVAVYIGYDEALAHRIYAGADFFLMPS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1022 IFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKERAkaqglepNGFSFDGADPAGVDYALNRAISAWYDGRDWfN 1101
Cdd:COG0297 378 RFEPCGLNQMYALRYGTVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-R 449
|
490 500
....*....|....*....|....*..
gi 2050351180 1102 SLCKKVMEQDWSWNKPALDYLELYHSA 1128
Cdd:COG0297 450 KLQRNAMKQDFSWEKSAKEYLELYREL 476
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
667-1128 |
9.75e-158 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 477.14 E-value: 9.75e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 667 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKISHVK----DLHYQRSYSWGGTEIKVWFGKVE 742
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDqvkvVELVDLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 743 GLSVYFLEPQNGMFWAGCVYGC--KNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYmhyGLSKSRV 820
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPGGIYGDdyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVY---RPNPIKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 821 VFTIHNLEF---------------------------GANNIGKA-MAYSDKATTVSPTYSREI----SG---NPLIASHL 865
Cdd:TIGR02095 158 VFTIHNLAYqgvfpaddfselglppeyfhmeglefyGRVNFLKGgIVYADRVTTVSPTYAREIltpeFGyglDGVLKARS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 866 HKFHGILNGIDPDIWDPYNDTYIPVPYTSENVvEGKRAAKEALQQRLGLK-KADLPLVGIITRLTHQKGIHLIKHAIWRT 944
Cdd:TIGR02095 238 GKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPvDDDVPLFGVISRLTQQKGVDLLLAALPEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 945 LERGGQVlfypiscfsnsllivVLLGSApDPRVQNDFVNLAnhlhSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFE 1024
Cdd:TIGR02095 317 LELGGQL---------------VVLGTG-DPELEEALRELA----ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1025 PCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKERAkaqglepNGFSFDGADPAGVDYALNRAISAWYDGRDWFNSLC 1104
Cdd:TIGR02095 377 PCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQ 449
|
490 500
....*....|....*....|....
gi 2050351180 1105 KKVMEQDWSWNKPALDYLELYHSA 1128
Cdd:TIGR02095 450 KNAMSQDFSWDKSAKQYVELYRSL 473
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
669-855 |
8.98e-60 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 204.87 E-value: 8.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 669 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMK-----ISHVKDLHYQRSYSWGGTEIKVWFGKVEG 743
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPeernqLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 744 LSVYFLEPQNgMFWAGCVYGCKN-----DGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSKS 818
Cdd:pfam08323 81 VDVYFLDNPD-YFDRPGLYGDDGrdyedNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050351180 819 RVVFTIHNLEF---------------------------GANNIGKA-MAYSDKATTVSPTYSREI 855
Cdd:pfam08323 160 KTVFTIHNLAYqgrfpadlldllglppedfnldglefyGQINFLKAgIVYADAVTTVSPTYAEEI 224
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
232-316 |
7.18e-19 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 82.02 E-value: 7.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 232 DEDIEVFLNRSLSTLSDEPDILIMGaFNDWRWKSFTFRLSKTHLNGdWWSCQVHVpKEAYKMDFVFFNGQDVYDNNDKKD 311
Cdd:smart01066 1 GNTVTVYYNGLLATSGAKNVYLHYG-FGENNWTDVPDVRMEKTGEG-WVKATIPV-KEAYKLNFCFKDGAGNWDNNGGAN 77
|
....*
gi 2050351180 312 FYILV 316
Cdd:smart01066 78 YHFEI 82
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02316 |
PLN02316 |
synthase/transferase |
28-1130 |
0e+00 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 2084.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 28 MSNARPRGSSPKGFTPKTPVGtSTQNRDLENNGEKEGSITPKSSEIAEANKQTLETQVDEDEEQAIEHSgekkvdeekig 107
Cdd:PLN02316 1 MSTSKPKGSAPRGFAPRTTVE-SSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQVDFQHNSE----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 108 eevslmskkvavangnqvvkngsisrVGKDVTLSEDKIALEGSQNNDLKNDGIVKERSISIDARKTEDDSLQIKLKLEME 187
Cdd:PLN02316 69 --------------------------SAVEEVEAEDEIEVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 188 EklrkketdrlaeekLRKQEIERLAEENFSKGNRLFVYPQMVKPDEDIEVFLNRSLSTLSDEPDILIMGAFNDWRWKSFT 267
Cdd:PLN02316 123 N--------------LRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYLNRSLSTLANEPDVLIMGAFNGWRWKSFT 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 268 FRLSKTHLNGDWWSCQVHVPKEAYKMDFVFFNGQDVYDNNDKKDFYILVEGGMDAFAFDDFLLEEKRRELEKLAKEQAVK 347
Cdd:PLN02316 189 ERLEKTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGGMDEHSFEDFLLEEKRRELEKLAKEEAER 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 348 ERLAEEQRRREEEKAASEADRAQARAEIEKRRTTLQELMKKAARSFNNVCHIEPSEFKGEDMIKLYYNKSSGPLAHANDL 427
Cdd:PLN02316 269 ERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYIEPSEFKAGDTVKLYYNRSSGPLAHSTEI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 428 WVHGGHNNWKDGLSIVERLVSSDKKDGDWWYANVVVPDRAFVLDWVFADGPPQSAAVYDNNHRQDFHAIVPSGIPEELYW 507
Cdd:PLN02316 349 WIHGGYNNWIDGLSIVEKLVKSEEKDGDWWYAEVVVPERALVLDWVFADGPPGNARNYDNNGRQDFHAIVPNNIPEELYW 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 508 VEEEHKIYRKLQEERRLREDAIRAKAEKTARIKAETKEQTLKRFLLSQKHIVYTEPLDVQAGSTVTVFYNPANTILNGKP 587
Cdd:PLN02316 429 VEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLSQKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKP 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 588 EVWFRGSFNRWTHRKGPLPPQKMLPADNGSHVKATVKVPLDAYMMDFVFSEKEDGGIFDNREGMDYHIPVSGGIAKEPPM 667
Cdd:PLN02316 509 EVWFRGSFNRWTHRLGPLPPQKMVPADNGSHLKATVKVPLDAYMMDFVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPM 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 668 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKISHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVY 747
Cdd:PLN02316 589 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVY 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 748 FLEPQNGMFWAGCVYGCKNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSKSRVVFTIHNL 827
Cdd:PLN02316 669 FLEPQNGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNL 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 828 EFGANNIGKAMAYSDKATTVSPTYSREISGNPLIASHLHKFHGILNGIDPDIWDPYNDTYIPVPYTSENVVEGKRAAKEA 907
Cdd:PLN02316 749 EFGANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEA 828
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 908 LQQRLGLKKADLPLVGIITRLTHQKGIHLIKHAIWRTLERGGQvlfypiscfsnslliVVLLGSAPDPRVQNDFVNLANH 987
Cdd:PLN02316 829 LQQRLGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQ---------------VVLLGSAPDPRIQNDFVNLANQ 893
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 988 LHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKERAKAQGL 1067
Cdd:PLN02316 894 LHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFDVDHDKERAQAQGL 973
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050351180 1068 EPNGFSFDGADPAGVDYALNRAISAWYDGRDWFNSLCKKVMEQDWSWNKPALDYLELYHSARK 1130
Cdd:PLN02316 974 EPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSARK 1036
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
668-1127 |
0e+00 |
|
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
Pssm-ID: 340822 [Multi-domain] Cd Length: 474 Bit Score: 547.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 668 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKISHVKDLHYQRSYS---WGGTEIKVWFGKVEGL 744
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLEVkvgGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 745 SVYFLEP-----QNGMFwAGCVYGCKNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSKSR 819
Cdd:cd03791 81 DYYFLDNpeffdRPGLP-GPPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 820 VVFTIHNLEF---------------------------GANNIGKA-MAYSDKATTVSPTYSREI-------SGNPLIASH 864
Cdd:cd03791 160 TVFTIHNLAYqglfpldtlaelglppelfhidglefyGQINFLKAgIVYADRVTTVSPTYAKEIltpeygeGLDGVLRAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 865 LHKFHGILNGIDPDIWDPYNDTYIPVPYtSENVVEGKRAAKEALQQRLGLK-KADLPLVGIITRLTHQKGIHLIKHAIWR 943
Cdd:cd03791 240 AGKLSGILNGIDYDEWNPATDKLIPANY-SANDLEGKAENKAALQKELGLPvDPDAPLFGFVGRLTEQKGVDLILDALPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 944 TLERGGQVlfypiscfsnsllivVLLGSApDPRVQNDFVNLANHlhssHHDRARLCLTYDEPLSHLIYAGADFILVPSIF 1023
Cdd:cd03791 319 LLEEGGQL---------------VVLGSG-DPEYEQAFRELAER----YPGKVAVVIGFDEALAHRIYAGADFFLMPSRF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1024 EPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKErakaqglEPNGFSFDGADPAGVDYALNRAISAWYDgRDWFNSL 1103
Cdd:cd03791 379 EPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKL 450
|
490 500
....*....|....*....|....
gi 2050351180 1104 CKKVMEQDWSWNKPALDYLELYHS 1127
Cdd:cd03791 451 QKNAMKQDFSWDKSAKEYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
667-1128 |
1.10e-176 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 526.58 E-value: 1.10e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 667 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKiSHVKDLHYQRSYS--WGGTEIK--VWFGKVE 742
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSID-DKLKDLEVVASLEvpLGGRTYYarVLEGPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 743 GLSVYFLEpQNGMFWAGCVYGCKN-----DGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSK 817
Cdd:COG0297 80 GVPVYFID-NPELFDRPGPYGDPDrdypdNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 818 SRVVFTIHNLE----FGANNIGK------------------------AMAYSDKATTVSPTYSREI----SGN---PLIA 862
Cdd:COG0297 159 IKTVFTIHNLAyqgiFPAEILELlglppelftpdglefygqinflkaGIVYADRVTTVSPTYAREIqtpeFGEgldGLLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 863 SHLHKFHGILNGIDPDIWDPYNDTYIPVPYTSENVvEGKRAAKEALQQRLGLK-KADLPLVGIITRLTHQKGIHLIKHAI 941
Cdd:COG0297 239 ARSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPvDPDAPLIGMVSRLTEQKGLDLLLEAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 942 WRTLERGGQVlfypiscfsnsllivVLLGSApDPRVQNDFVNLANHlhssHHDRARLCLTYDEPLSHLIYAGADFILVPS 1021
Cdd:COG0297 318 DELLEEDVQL---------------VVLGSG-DPEYEEAFRELAAR----YPGRVAVYIGYDEALAHRIYAGADFFLMPS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1022 IFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKERAkaqglepNGFSFDGADPAGVDYALNRAISAWYDGRDWfN 1101
Cdd:COG0297 378 RFEPCGLNQMYALRYGTVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-R 449
|
490 500
....*....|....*....|....*..
gi 2050351180 1102 SLCKKVMEQDWSWNKPALDYLELYHSA 1128
Cdd:COG0297 450 KLQRNAMKQDFSWEKSAKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
667-1130 |
4.09e-174 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 519.29 E-value: 4.09e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 667 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKishVKDLHYQRSYSWGGteIKVWFGKVE--GL 744
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIR---EKLRDAQVVGRLDL--FTVLFGHLEgdGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 745 SVYFLEPQNgMFWAGCVYGCKNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYmHYGLSKSRVVFTI 824
Cdd:PRK00654 76 PVYLIDAPH-LFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGLIPALLKEKY-WRGYPDIKTVFTI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 825 HNLE----FGANNIG-----------------------KA-MAYSDKATTVSPTYSREI----SG---NPLIASHLHKFH 869
Cdd:PRK00654 154 HNLAyqglFPAEILGelglpaeafhleglefygqisflKAgLYYADRVTTVSPTYAREIttpeFGyglEGLLRARSGKLS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 870 GILNGIDPDIWDPYNDTYIPVPYTSENVvEGKRAAKEALQQRLGLKKADLPLVGIITRLTHQKGIHLIKHAIWRTLERGG 949
Cdd:PRK00654 234 GILNGIDYDIWNPETDPLLAANYSADDL-EGKAENKRALQERFGLPDDDAPLFAMVSRLTEQKGLDLVLEALPELLEQGG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 950 QVlfypiscfsnsllivVLLGSaPDPRVQNDFVNLANHlhssHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLT 1029
Cdd:PRK00654 313 QL---------------VLLGT-GDPELEEAFRALAAR----YPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1030 QLTAMRYGSIAVVRKTGGLFDTVFDVDHDKERAkaqglepNGFSFDGADPAGVDYALNRAISAWYDGRDWfNSLCKKVME 1109
Cdd:PRK00654 373 QLYALRYGTLPIVRRTGGLADTVIDYNPEDGEA-------TGFVFDDFNAEDLLRALRRALELYRQPPLW-RALQRQAMA 444
|
490 500
....*....|....*....|.
gi 2050351180 1110 QDWSWNKPALDYLELYHSARK 1130
Cdd:PRK00654 445 QDFSWDKSAEEYLELYRRLLG 465
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
667-1128 |
9.75e-158 |
|
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273969 [Multi-domain] Cd Length: 473 Bit Score: 477.14 E-value: 9.75e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 667 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKISHVK----DLHYQRSYSWGGTEIKVWFGKVE 742
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDqvkvVELVDLSVGPRTLYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 743 GLSVYFLEPQNGMFWAGCVYGC--KNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYmhyGLSKSRV 820
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPGGIYGDdyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVY---RPNPIKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 821 VFTIHNLEF---------------------------GANNIGKA-MAYSDKATTVSPTYSREI----SG---NPLIASHL 865
Cdd:TIGR02095 158 VFTIHNLAYqgvfpaddfselglppeyfhmeglefyGRVNFLKGgIVYADRVTTVSPTYAREIltpeFGyglDGVLKARS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 866 HKFHGILNGIDPDIWDPYNDTYIPVPYTSENVvEGKRAAKEALQQRLGLK-KADLPLVGIITRLTHQKGIHLIKHAIWRT 944
Cdd:TIGR02095 238 GKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPvDDDVPLFGVISRLTQQKGVDLLLAALPEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 945 LERGGQVlfypiscfsnsllivVLLGSApDPRVQNDFVNLAnhlhSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFE 1024
Cdd:TIGR02095 317 LELGGQL---------------VVLGTG-DPELEEALRELA----ERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1025 PCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKERAkaqglepNGFSFDGADPAGVDYALNRAISAWYDGRDWFNSLC 1104
Cdd:TIGR02095 377 PCGLTQLYAMRYGTVPIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQ 449
|
490 500
....*....|....*....|....
gi 2050351180 1105 KKVMEQDWSWNKPALDYLELYHSA 1128
Cdd:TIGR02095 450 KNAMSQDFSWDKSAKQYVELYRSL 473
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
667-1128 |
1.28e-149 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 473.23 E-value: 1.28e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 667 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMKISHVKDLHYQ----RSYSWGGT-EIKVWFGKV 741
Cdd:PLN02939 482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKVLdvvvESYFDGNLfKNKIWTGTV 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 742 EGLSVYFLEPQN--GMFWAGCVYGCKNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSKSR 819
Cdd:PLN02939 562 EGLPVYFIEPQHpsKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKGFNSAR 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 820 VVFTIHNLEF------------------------------GANNIGK-AMAYSDKATTVSPTYSREI---SGNPL---IA 862
Cdd:PLN02939 642 ICFTCHNFEYqgtapasdlascgldvhqldrpdrmqdnahGRINVVKgAIVYSNIVTTVSPTYAQEVrseGGRGLqdtLK 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 863 SHLHKFHGILNGIDPDIWDPYNDTYIPVPYtSENVVEGKRAAKEALQQRLGLKKADL--PLVGIITRLTHQKGIHLIKHA 940
Cdd:PLN02939 722 FHSKKFVGILNGIDTDTWNPSTDRFLKVQY-NANDLQGKAANKAALRKQLGLSSADAsqPLVGCITRLVPQKGVHLIRHA 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 941 IWRTLERGGQVlfypiscfsnsllivVLLGSAPDPRVQNDFVNLANHLHSSHHdrARLCLTYDEPLSHLIYAGADFILVP 1020
Cdd:PLN02939 801 IYKTAELGGQF---------------VLLGSSPVPHIQREFEGIADQFQSNNN--IRLILKYDEALSHSIYAASDMFIIP 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1021 SIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKERAKAQglepNGFSFDGADPAGVDYALNRAISAWYDGRDWF 1100
Cdd:PLN02939 864 SMFEPCGLTQMIAMRYGSVPIVRKTGGLNDSVFDFDDETIPVELR----NGFTFLTPDEQGLNSALERAFNYYKRKPEVW 939
|
490 500
....*....|....*....|....*...
gi 2050351180 1101 NSLCKKVMEQDWSWNKPALDYLELYHSA 1128
Cdd:PLN02939 940 KQLVQKDMNIDFSWDSSASQYEELYQRA 967
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
666-1127 |
3.23e-75 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 257.34 E-value: 3.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 666 PMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKY-DCMK-ISHVKDLHYQRSYsWGGTEiKVWFGKVEG 743
Cdd:PRK14099 3 PLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYpAVLAgIEDAEQVHSFPDL-FGGPA-RLLAARAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 744 LSVYFLE-------PQN------GMFWAgcvygckNDGERFGFFCHAALEFLQQS--GFHPDIIHCHDWSSAPVAwlfkd 808
Cdd:PRK14099 81 LDLFVLDaphlydrPGNpyvgpdGKDWP-------DNAQRFAALARAAAAIGQGLvpGFVPDIVHAHDWQAGLAP----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 809 HYMHY-GLSKSRVVFTIHNLEF---------GA----------------NNIG--KA-MAYSDKATTVSPTYSREISGNP 859
Cdd:PRK14099 149 AYLHYsGRPAPGTVFTIHNLAFqgqfprellGAlglppsafsldgveyyGGIGylKAgLQLADRITTVSPTYALEIQGPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 860 -------LIASHLHKFHGILNGIDPDIWDPYNDTYIPVPYTSENVvEGKRAAKEALQQRLGLKKA-DLPLVGIITRLTHQ 931
Cdd:PRK14099 229 agmgldgLLRQRADRLSGILNGIDTAVWNPATDELIAATYDVETL-AARAANKAALQARFGLDPDpDALLLGVISRLSWQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 932 KGIHLIKHAIwRTLERGGQVLfypiscfsnsllivVLLGSApDPRVQNDFVNLANHlhssHHDRARLCLTYDEPLSHLIY 1011
Cdd:PRK14099 308 KGLDLLLEAL-PTLLGEGAQL--------------ALLGSG-DAELEARFRAAAQA----YPGQIGVVIGYDEALAHLIQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1012 AGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDhdkERAKAQGLePNGFSFDGADPAGVDYALNRAIS 1091
Cdd:PRK14099 368 AGADALLVPSRFEPCGLTQLCALRYGAVPVVARVGGLADTVVDAN---EMAIATGV-ATGVQFSPVTADALAAALRKTAA 443
|
490 500 510
....*....|....*....|....*....|....*.
gi 2050351180 1092 AWYDGRDWFNsLCKKVMEQDWSWNKPALDYLELYHS 1127
Cdd:PRK14099 444 LFADPVAWRR-LQRNGMTTDVSWRNPAQHYAALYRS 478
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
669-855 |
8.98e-60 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 204.87 E-value: 8.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 669 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKYDCMK-----ISHVKDLHYQRSYSWGGTEIKVWFGKVEG 743
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPeernqLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 744 LSVYFLEPQNgMFWAGCVYGCKN-----DGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKDHYMHYGLSKS 818
Cdd:pfam08323 81 VDVYFLDNPD-YFDRPGLYGDDGrdyedNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050351180 819 RVVFTIHNLEF---------------------------GANNIGKA-MAYSDKATTVSPTYSREI 855
Cdd:pfam08323 160 KTVFTIHNLAYqgrfpadlldllglppedfnldglefyGQINFLKAgIVYADAVTTVSPTYAEEI 224
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
669-1125 |
4.49e-53 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 194.18 E-value: 4.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 669 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHSVDIILPKY-----------DCMKIS----HVKD----LHyqrsysw 729
Cdd:PRK14098 8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYgtindrkfrlhDVLRLSdievPLKEktdlLH------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 730 ggteIKVWFGKVEGLSVYFLE-----PQNGMFWAGCVYG-CKNDGERFGFFCHAALEFLQQSGFHPDIIHCHDWSSAPVA 803
Cdd:PRK14098 81 ----VKVTALPSSKIQTYFLYnekyfKRNGLFTDMSLGGdLKGSAEKVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 804 WLFKDHYM-HYGLSKSRVVFTIHN------LEFGA--------------------NNIGKAMAYSDKATTVSPTYSREIS 856
Cdd:PRK14098 157 LLLKTVYAdHEFFKDIKTVLTIHNvyrqgvLPFKVfqkllpeevcsglhregdevNMLYTGVEHADLLTTTSPRYAEEIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 857 GNPLIASHLHK--------FHGILNGIDPDIWDPYNDTYIPVPYTSENVvEGKRAAKEALQQRLGLK-KADLPLVGIITR 927
Cdd:PRK14098 237 GDGEEAFGLDKvleerkmrLHGILNGIDTRQWNPSTDKLIKKRYSIERL-DGKLENKKALLEEVGLPfDEETPLVGVIIN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 928 LTHQKGIHLIKHAIWRTLERGGQVlfypiscfsnsllivVLLGSApDPRVQNDFVNLANhlhsSHHDRARLCLTYDEPLS 1007
Cdd:PRK14098 316 FDDFQGAELLAESLEKLVELDIQL---------------VICGSG-DKEYEKRFQDFAE----EHPEQVSVQTEFTDAFF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1008 HLIYAGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDHDKErakaqglepNGFSFDGADPAGVDYALN 1087
Cdd:PRK14098 376 HLAIAGLDMLLMPGKIESCGMLQMFAMSYGTIPVAYAGGGIVETIEEVSEDKG---------SGFIFHDYTPEALVAKLG 446
|
490 500 510
....*....|....*....|....*....|....*...
gi 2050351180 1088 RAISAWYDGRDWfNSLCKKVMEQDWSWNKPALDYLELY 1125
Cdd:PRK14098 447 EALALYHDEERW-EELVLEAMERDFSWKNSAEEYAQLY 483
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
573-656 |
2.04e-21 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 89.27 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 573 TVFYNPANtilngKPEVWFRGSFNRWTHRKGpLPPQKMLPADNGSHVKATVKVPLDAYMMDFVFseKEDGGIFDNREGMD 652
Cdd:pfam16760 1 NIYYNGSL-----AKEVYIHGGFNGWKNVQD-VPMEKLPPTGGGDWFSATVPVPEDAYVLDFVF--KDGAGNWDNNNGQN 72
|
....
gi 2050351180 653 YHIP 656
Cdd:pfam16760 73 YHIP 76
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
411-496 |
1.26e-20 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 86.96 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 411 KLYYNKSSgplahANDLWVHGGHNNWKDGLSI-VERLvsSDKKDGDWWYANVVVPDRAFVLDWVFADGppqsAAVYDNNH 489
Cdd:pfam16760 1 NIYYNGSL-----AKEVYIHGGFNGWKNVQDVpMEKL--PPTGGGDWFSATVPVPEDAYVLDFVFKDG----AGNWDNNN 69
|
....*..
gi 2050351180 490 RQDFHAI 496
Cdd:pfam16760 70 GQNYHIP 76
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
237-314 |
3.15e-20 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 85.81 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 237 VFLNRSLStlsdePDILIMGAFNDWRWKSFTfRLSKTH--LNGDWWSCQVHVPKEAYKMDFVFFNGQDVYDNNDKKDFYI 314
Cdd:pfam16760 2 IYYNGSLA-----KEVYIHGGFNGWKNVQDV-PMEKLPptGGGDWFSATVPVPEDAYVLDFVFKDGAGNWDNNNGQNYHI 75
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
232-316 |
7.18e-19 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 82.02 E-value: 7.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 232 DEDIEVFLNRSLSTLSDEPDILIMGaFNDWRWKSFTFRLSKTHLNGdWWSCQVHVpKEAYKMDFVFFNGQDVYDNNDKKD 311
Cdd:smart01066 1 GNTVTVYYNGLLATSGAKNVYLHYG-FGENNWTDVPDVRMEKTGEG-WVKATIPV-KEAYKLNFCFKDGAGNWDNNGGAN 77
|
....*
gi 2050351180 312 FYILV 316
Cdd:smart01066 78 YHFEI 82
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
787-1126 |
8.96e-19 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 89.52 E-value: 8.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 787 FHPDIIHCHDWSSAPVAWLFKdhymhyGLSKSRVVFTIHNLEFGANN------------IGKAMAYSDKATTVSPTYSRE 854
Cdd:cd03801 81 RKFDVVHAHGLLAALLAALLA------LLLGAPLVVTLHGAEPGRLLlllaaerrllarAEALLRRADAVIAVSEALRDE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 855 ISGnpLIASHLHKFHGILNGIDPDIWDPyndtyipvpytsenvvegkraakeALQQRLGLKKADlPLVGIITRLTHQKGI 934
Cdd:cd03801 155 LRA--LGGIPPEKIVVIPNGVDLERFSP------------------------PLRRKLGIPPDR-PVLLFVGRLSPRKGV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 935 HLIKHAIWRTLERGGQVLFypiscfsnsllivVLLGSAPD--PRVQNDFVNLANHLH----SSHHDRARLcltydeplsh 1008
Cdd:cd03801 208 DLLLEALAKLLRRGPDVRL-------------VIVGGDGPlrAELEELELGLGDRVRflgfVPDEELPAL---------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1009 liYAGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDVDhdkerakaqglepNGFSFDGADPAgvdyALNR 1088
Cdd:cd03801 265 --YAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGE-------------GGLVVPPDDVE----ALAD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2050351180 1089 AISAWYDGRDWFNSLCK---KVMEQDWSWNKPALDYLELYH 1126
Cdd:cd03801 326 ALLRLLADPELRARLGRaarERVAERFSWERVAERLLDLYR 366
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
569-658 |
8.94e-18 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 78.94 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 569 GSTVTVFYNPANTIlNGKPEVWFRGSF--NRWTHrkgpLPPQKMLPADNGsHVKATVKVpLDAYMMDFVFseKEDGGIFD 646
Cdd:smart01066 1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTD----VPDVRMEKTGEG-WVKATIPV-KEAYKLNFCF--KDGAGNWD 71
|
90
....*....|..
gi 2050351180 647 NREGMDYHIPVS 658
Cdd:smart01066 72 NNGGANYHFEIG 83
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
774-1122 |
1.96e-11 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 67.27 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 774 FCHAALEFLQQSGFHPDIIHCHDWSSAPVAWLFKD-------HYMH-YGLSKSRVVFTIHNLEFGANNIGK--AMAYSDK 843
Cdd:cd03800 87 FADGLLRFIAREGGRYDLIHSHYWDSGLVGALLARrlgvplvHTFHsLGRVKYRHLGAQDTYHPSLRITAEeqILEAADR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 844 ATTVSPtysREISGnpLIASHLH---KFHGILNGIDPDIWDPYNDtyipvpytsenvvegkraaKEALQQRLGLKkADLP 920
Cdd:cd03800 167 VIASTP---QEADE--LISLYGAdpsRINVVPPGVDLERFFPVDR-------------------AEARRARLLLP-PDKP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 921 LVGIITRLTHQKGIHLIKHAIWRTLERGGQVLfypiscfsnsllIVVLLGSAPDPRVQNDF--VNLANHLHSShhDRARL 998
Cdd:cd03800 222 VVLALGRLDPRKGIDTLVRAFAQLPELRELAN------------LVLVGGPSDDPLSMDREelAELAEELGLI--DRVRF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 999 CLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDvdhdkerakaqglEPNGFSFDGAD 1078
Cdd:cd03800 288 PGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRD-------------GRTGLLVDPHD 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2050351180 1079 PAgvdyALNRAISAWYDGRDWFNSLCKKVME---QDWSWNKPALDYL 1122
Cdd:cd03800 355 PE----ALAAALRRLLDDPALWQRLSRAGLErarAHYTWESVADQLL 397
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
787-1052 |
6.31e-11 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 65.45 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 787 FHPDIIHCHDWSSAPVAWLFKdhymhyGLSKSRVVFTIHNLEFgANNIGKA-----MAYSDKATTVS-PTYSREISGNPL 860
Cdd:cd03819 75 ERIDLIHAHSRAPAWLGWLAS------RLTGVPLVTTVHGSYL-ATYHPKDfalavRARGDRVIAVSeLVRDHLIEALGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 861 IAShlhKFHGILNGIDPDIWDPyndtyipvpytsenvvegkraAKEALQQRLGLKKADLPLVGIITRLTHQKGIHLIKHA 940
Cdd:cd03819 148 DPE---RIRVIPNGVDTDRFPP---------------------EAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 941 IWRtLERGGQVLFypiscfsnslLIVvllGSAPdprvQNDFVnlaNHLHSSHHDRARLCLT-YDEPLSHLiYAGADFILV 1019
Cdd:cd03819 204 AAE-LKDEPDFRL----------LVA---GDGP----ERDEI---RRLVERLGLRDRVTFTgFREDVPAA-LAASDVVVL 261
|
250 260 270
....*....|....*....|....*....|...
gi 2050351180 1020 PSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTV 1052
Cdd:cd03819 262 PSLHEEFGRVALEAMACGTPVVATDVGGAREIV 294
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
406-498 |
2.61e-10 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 57.75 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 406 GEDmIKLYYNKSSGPLAhANDLWVHGG--HNNWKDglsiVERLVSsdKKDGDWWYANVVVPDRAFVLDWVFADGppqsAA 483
Cdd:smart01066 1 GNT-VTVYYNGLLATSG-AKNVYLHYGfgENNWTD----VPDVRM--EKTGEGWVKATIPVKEAYKLNFCFKDG----AG 68
|
90
....*....|....*
gi 2050351180 484 VYDNNHRQDFHAIVP 498
Cdd:smart01066 69 NWDNNGGANYHFEIG 83
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
1008-1130 |
4.09e-09 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 55.77 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 1008 HLIYAGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFDvdhdkerakaqglEPNGFSFDGADPAgvdyALN 1087
Cdd:COG0438 15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED-------------GETGLLVPPGDPE----ALA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2050351180 1088 RAISAWYDGRDWFNSL---CKKVMEQDWSWNKPALDYLELYHSARK 1130
Cdd:COG0438 78 EAILRLLEDPELRRRLgeaARERAEERFSWEAIAERLLALYEELLA 123
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
683-878 |
7.96e-06 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 47.53 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 683 GGLGDVVTSLSRAVQDLNHSVDIILPKYDcmkishvkdlhyqrsyswGGTEIKVWFGKVEGLSVYFLEPQNGMFWAgcvy 762
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGP------------------GPLAEEVVRVVRVPRVPLPLPPRLLRSLA---- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 763 gckndgerfgfFCHAALEFLQQsgFHPDIIHCHDWSSAPVAWLFKDHYMHYglsksRVVFTIHNLEFGANNIG------- 835
Cdd:pfam13439 59 -----------FLRRLRRLLRR--ERPDVVHAHSPFPLGLAALAARLRLGI-----PLVVTYHGLFPDYKRLGarlsplr 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2050351180 836 --------KAMAYSDKATTVSPTysreisgnplIASHLHKFHG--------ILNGIDPD 878
Cdd:pfam13439 121 rllrrlerRLLRRADRVIAVSEA----------VADELRRLYGvppekirvIPNGVDLE 169
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
860-1054 |
9.80e-06 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 48.17 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 860 LIASHLHKFHGILNGIDPDIW---DPYNDTY----------IPVPYT--SENVVEGKRAAKEAL-QQRLGLKKADLPLVG 923
Cdd:cd01635 38 LLLLALRRILKKLLELKPDVVhahSPHAAALaallaarllgIPIVVTvhGPDSLESTRSELLALaRLLVSLPLADKVSVG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 924 iitRLTHQKGIHLIKHAIwrtlerggqvLFYPISCFSNSLLIVVllgsaPDPRVQNDFVNLANHLHSSHHDRARLCltYD 1003
Cdd:cd01635 118 ---RLVPEKGIDLLLEAL----------ALLKARLPDLVLVLVG-----GGGEREEEEALAAALGLLERVVIIGGL--VD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2050351180 1004 EPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVFD 1054
Cdd:cd01635 178 DEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
683-829 |
9.49e-04 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 41.23 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 683 GGLGDVVTSLSRAVQDLNHSVDIILPkydcmkishvkdlhyqrSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWagcvy 762
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTP-----------------GGPPGRPELVGDGVRVHRLPVPPRPSPLADLA----- 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050351180 763 gckndgerfgfFCHAALEFLQQsgFHPDIIHCHDWSSAPVAWLFKDhymhygLSKSRVVFTIHNLEF 829
Cdd:pfam13579 59 -----------ALRRLRRLLRA--ERPDVVHAHSPTAGLAARLARR------RRGVPLVVTVHGLAL 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-218 |
1.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 74 AEANKQTLETQVDEDEEQAIEhsgEKKVDEEKIGEEVslmsKKVAVANGNQVVKNGSISRVGKDVTLSEDKIALEGSQNN 153
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADE---AKKAEEAKKADEA----KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050351180 154 DLKNDGIVKERSisiDARKTEDDSLQIKLKLEMEEKLRKKETDRLAEEKLRKQEIERLAEENFSK 218
Cdd:PTZ00121 1579 ALRKAEEAKKAE---EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
81-206 |
2.74e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 81 LETQVDEDEEQAIEHSGEKKVDEEKIGEEVSLMSKKVAVANGNQVVKNGSISRVGKdvtLSEDKIALEGSQNNDLKNDGI 160
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKK---LEEDILLLEDQNSKLSKERKL 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2050351180 161 VKERSISIDARKTEDD----SLQiKLKL-------EMEEKLRKKETDRLAEEKLRKQ 206
Cdd:pfam01576 157 LEERISEFTSNLAEEEekakSLS-KLKNkheamisDLEERLKKEEKGRQELEKAKRK 212
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
918-1098 |
2.77e-03 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 39.56 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 918 DLPLVGIITRLTHQKGIHLIKHAIWRTLERGGQVLFypiscfsnsllivVLLGSAPDP---RVQNDFVNLANHLHSSHHd 994
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKL-------------VIAGDGEEEkrlKKLAEKLGLGDNVIFLGF- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050351180 995 rarlclTYDEPLSHLiYAGADFILVPSIFEPCGLTQLTAMRYGSIAVVRKTGGLFDTVfdVDHDkerakaqglepNGFSF 1074
Cdd:pfam00534 67 ------VSDEDLPEL-LKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV--KDGE-----------TGFLV 126
|
170 180
....*....|....*....|....
gi 2050351180 1075 DGADPAgvdyALNRAISAWYDGRD 1098
Cdd:pfam00534 127 KPNNAE----ALAEAIDKLLEDEE 146
|
|
|