|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02316 |
PLN02316 |
synthase/transferase |
679-1673 |
0e+00 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 1885.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 679 EEQKSIAMNEEQTIVTEEDIPMAKVEIGIDKAKFLHLLSEEESSWDENEVGIIEADE-QYEVDETSMSTEQDIQESPNDD 757
Cdd:PLN02316 33 DKEDSSTSTSSLSVSAVEKTSNAKEEIQVDFQHNSESAVEEVEAEDEIEVEQNQSDVlKSSSIVKEESISTDMDGIDDDS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 758 LD-------PQALWSMLQELAEKNYSLGNKLFTYPDVLKADSTIDLYFNRDLSAVANEPDVLIKGAFNGWKWRFFTEKLH 830
Cdd:PLN02316 113 LDrklklerENLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYLNRSLSTLANEPDVLIMGAFNGWRWKSFTERLE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 831 KSELAGDWWCCKLYIPKQAYRMDFVFFNGHTVYENNNNNDFVIQIESTMDENLFEDFLAEEKQRELENLANEEAERRRQT 910
Cdd:PLN02316 193 KTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGGMDEHSFEDFLLEEKRRELEKLAKEEAERERQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 911 DEQRRMEEERAADKADRVQAKVEVETKKNKLCNVLGLARAPVDNLWYIEPITTGQEATVRLYYNINSRPLVHSTEIWMHG 990
Cdd:PLN02316 273 EEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYIEPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 991 GYNNWIDGLSFAERLVHHHDKDCDWWFADVVVPERTYVLDWVFADGPPGSARNYDNNGGHDFHATLPNNMTEEEYWMEEE 1070
Cdd:PLN02316 353 GYNNWIDGLSIVEKLVKSEEKDGDWWYAEVVVPERALVLDWVFADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1071 QRIYTRLQQERREREEAIKRKAERNAKMKAEMKEKTMRMFLVSQKHIVYTEPLEIHAGTTIDVLYNPSNTVLTGKPEVWF 1150
Cdd:PLN02316 433 HQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLSQKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWF 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1151 RCSFNRWMYPGGVLPPQKMVQAENGSHLKATVYVPRDAYMMDFVFSESEEGGIYDNRNGLDYHIPVFGSIAKEPPMHIVH 1230
Cdd:PLN02316 513 RGSFNRWTHRLGPLPPQKMVPADNGSHLKATVKVPLDAYMMDFVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVH 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1231 IAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLHIHQSFSWGGSEIKVWRGLVEGLCVYFLEP 1310
Cdd:PLN02316 593 IAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEP 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1311 QNGMFGVGYVYG-RDDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANARVVFTIHNLEFGA 1389
Cdd:PLN02316 673 QNGMFWAGCVYGcRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGA 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1390 HHIGKAMRYCDKATTVSNTYSKEVSGHGAIVPHLGKFYGILNGIDPDIWDPYNDNFIPVHYTCENVVEGKRAAKRALQQK 1469
Cdd:PLN02316 753 NHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQR 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1470 FGLQQIDVPVVGIVTRLTAQKGIHLIKHAIHRTLERNGQVVLLGSAPDSRIQADFVNLANKLHGVNHGQVRLSLTYDEPL 1549
Cdd:PLN02316 833 LGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPL 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1550 SHLIYAGSDFILVPSIFEPCGLTQLVAMRYGTIPIVRKTGGLFDTVFDVDNDKERARDRGLEPNGFSFDGADSNGVDYAL 1629
Cdd:PLN02316 913 SHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYAL 992
|
970 980 990 1000
....*....|....*....|....*....|....*....|....
gi 1162503518 1630 NRAISAWFDARSWFHSLCKRVMEQDWSWNRPALDYIELYRSASK 1673
Cdd:PLN02316 993 NRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSARK 1036
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
1227-1670 |
3.46e-178 |
|
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: 543.70 E-value: 3.46e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1227 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLH---IHQSFSWGGSEIKVWRGLVEGL 1303
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRvlgLEVKVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1304 CVYFLEPQNgMFGVGYVYGR------DDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANAR 1377
Cdd:cd03791 81 DYYFLDNPE-FFDRPGLPGPpgydypDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1378 VVFTIHNLE----FGAHHIGK------------------------AMRYCDKATTVSNTYSKEV-------SGHGAIVPH 1422
Cdd:cd03791 160 TVFTIHNLAyqglFPLDTLAElglppelfhidglefygqinflkaGIVYADRVTTVSPTYAKEIltpeygeGLDGVLRAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1423 LGKFYGILNGIDPDIWDPYNDNFIPVHYTcENVVEGKRAAKRALQQKFGLQQ-IDVPVVGIVTRLTAQKGIHLIKHAIHR 1501
Cdd:cd03791 240 AGKLSGILNGIDYDEWNPATDKLIPANYS-ANDLEGKAENKAALQKELGLPVdPDAPLFGFVGRLTEQKGVDLILDALPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1502 TLERNGQVVLLGSApDSRIQADFVNLANKlhgvNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGT 1581
Cdd:cd03791 319 LLEEGGQLVVLGSG-DPEYEQAFRELAER----YPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1582 IPIVRKTGGLFDTVFDVDNDKErardrglEPNGFSFDGADSNGVDYALNRAISAWFDaRSWFHSLCKRVMEQDWSWNRPA 1661
Cdd:cd03791 394 LPIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKNAMKQDFSWDKSA 465
|
....*....
gi 1162503518 1662 LDYIELYRS 1670
Cdd:cd03791 466 KEYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1226-1671 |
3.11e-172 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 527.74 E-value: 3.11e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1226 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCL--NLSNVKNL-HIHQSFSWGGSEIKVWRGLVEG 1302
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIddKLKDLEVVaSLEVPLGGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1303 LCVYFLEpQNGMFGVGYVYGR------DDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANA 1376
Cdd:COG0297 81 VPVYFID-NPELFDRPGPYGDpdrdypDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1377 RVVFTIHNLE----FGAHHIGK------------------------AMRYCDKATTVSNTYSKEV----SGHG---AIVP 1421
Cdd:COG0297 160 KTVFTIHNLAyqgiFPAEILELlglppelftpdglefygqinflkaGIVYADRVTTVSPTYAREIqtpeFGEGldgLLRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1422 HLGKFYGILNGIDPDIWDPYNDNFIPVHYTCENVvEGKRAAKRALQQKFGL-QQIDVPVVGIVTRLTAQKGIHLIKHAIH 1500
Cdd:COG0297 240 RSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLpVDPDAPLIGMVSRLTEQKGLDLLLEALD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1501 RTLERNGQVVLLGSApDSRIQADFVNLANKlhgvNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYG 1580
Cdd:COG0297 319 ELLEEDVQLVVLGSG-DPEYEEAFRELAAR----YPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1581 TIPIVRKTGGLFDTVFDVDNDKERArdrglepNGFSFDGADSNGVDYALNRAISAWFDARSWfHSLCKRVMEQDWSWNRP 1660
Cdd:COG0297 394 TVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-RKLQRNAMKQDFSWEKS 465
|
490
....*....|.
gi 1162503518 1661 ALDYIELYRSA 1671
Cdd:COG0297 466 AKEYLELYREL 476
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1226-1671 |
1.66e-155 |
|
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: 483.31 E-value: 1.66e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1226 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLHI--HQSFSWGGS--EIKVWRGLVE 1301
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVveLVDLSVGPRtlYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1302 GLCVYFLEPQNGMFGVGYVYG---RDDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSslaNARV 1378
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPGGIYGddyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRPN---PIKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1379 VFTIHNLE----FGAHHIGK------------------------AMRYCDKATTVSNTYSKEV----SG---HGAIVPHL 1423
Cdd:TIGR02095 158 VFTIHNLAyqgvFPADDFSElglppeyfhmeglefygrvnflkgGIVYADRVTTVSPTYAREIltpeFGyglDGVLKARS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1424 GKFYGILNGIDPDIWDPYNDNFIPVHYTCENVvEGKRAAKRALQQKFGLQQI-DVPVVGIVTRLTAQKGIHLIKHAIHRT 1502
Cdd:TIGR02095 238 GKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPVDdDVPLFGVISRLTQQKGVDLLLAALPEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1503 LERNGQVVLLGSApDSRIQADFVNLANKlhgvNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGTI 1582
Cdd:TIGR02095 317 LELGGQLVVLGTG-DPELEEALRELAER----YPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1583 PIVRKTGGLFDTVFDVDNDKERArdrglepNGFSFDGADSNGVDYALNRAISAWFDARSWFHSLCKRVMEQDWSWNRPAL 1662
Cdd:TIGR02095 392 PIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAK 464
|
....*....
gi 1162503518 1663 DYIELYRSA 1671
Cdd:TIGR02095 465 QYVELYRSL 473
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
1228-1413 |
1.67e-59 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 204.87 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1228 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLN-----LSNVKNLHIHQSFSWGGSEIKVWRGLVEG 1302
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPeernqLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1303 LCVYFLEPQNgMFGVGYVYGR------DDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANA 1376
Cdd:pfam08323 81 VDVYFLDNPD-YFDRPGLYGDdgrdyeDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162503518 1377 RVVFTIHNLE----FGAHHIGK------------------------AMRYCDKATTVSNTYSKEV 1413
Cdd:pfam08323 160 KTVFTIHNLAyqgrFPADLLDLlglppedfnldglefygqinflkaGIVYADAVTTVSPTYAEEI 224
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
1128-1216 |
1.90e-14 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 70.08 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1128 GTTIDVLYNPSNTVlTGKPEVWFRCSF--NRWMYpggvLPPQKMVQAENGsHLKATVYVpRDAYMMDFVFSEseEGGIYD 1205
Cdd:smart01066 1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTD----VPDVRMEKTGEG-WVKATIPV-KEAYKLNFCFKD--GAGNWD 71
|
90
....*....|.
gi 1162503518 1206 NRNGLDYHIPV 1216
Cdd:smart01066 72 NNGGANYHFEI 82
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
63-189 |
2.21e-10 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 65.66 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 63 TASPNVKVAAYSNYAPRLLVESSSKKSEHhdSSRHREETIDTYNGLSGSDAAElTSNRDVEIEVDLQHISEEelpgkvsi 142
Cdd:PLN02316 1 MSTSKPKGSAPRGFAPRTTVESSQKRIQQ--NNGDKEDSSTSTSSLSVSAVEK-TSNAKEEIQVDFQHNSES-------- 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1162503518 143 naSLGEMETVDEAEVEEDKFEVDTSGIVLRNVAVREVDPKDEHNAKD 189
Cdd:PLN02316 70 --AVEEVEAEDEIEVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLD 114
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02316 |
PLN02316 |
synthase/transferase |
679-1673 |
0e+00 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 1885.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 679 EEQKSIAMNEEQTIVTEEDIPMAKVEIGIDKAKFLHLLSEEESSWDENEVGIIEADE-QYEVDETSMSTEQDIQESPNDD 757
Cdd:PLN02316 33 DKEDSSTSTSSLSVSAVEKTSNAKEEIQVDFQHNSESAVEEVEAEDEIEVEQNQSDVlKSSSIVKEESISTDMDGIDDDS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 758 LD-------PQALWSMLQELAEKNYSLGNKLFTYPDVLKADSTIDLYFNRDLSAVANEPDVLIKGAFNGWKWRFFTEKLH 830
Cdd:PLN02316 113 LDrklklerENLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYLNRSLSTLANEPDVLIMGAFNGWRWKSFTERLE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 831 KSELAGDWWCCKLYIPKQAYRMDFVFFNGHTVYENNNNNDFVIQIESTMDENLFEDFLAEEKQRELENLANEEAERRRQT 910
Cdd:PLN02316 193 KTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGGMDEHSFEDFLLEEKRRELEKLAKEEAERERQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 911 DEQRRMEEERAADKADRVQAKVEVETKKNKLCNVLGLARAPVDNLWYIEPITTGQEATVRLYYNINSRPLVHSTEIWMHG 990
Cdd:PLN02316 273 EEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYIEPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 991 GYNNWIDGLSFAERLVHHHDKDCDWWFADVVVPERTYVLDWVFADGPPGSARNYDNNGGHDFHATLPNNMTEEEYWMEEE 1070
Cdd:PLN02316 353 GYNNWIDGLSIVEKLVKSEEKDGDWWYAEVVVPERALVLDWVFADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1071 QRIYTRLQQERREREEAIKRKAERNAKMKAEMKEKTMRMFLVSQKHIVYTEPLEIHAGTTIDVLYNPSNTVLTGKPEVWF 1150
Cdd:PLN02316 433 HQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLSQKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWF 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1151 RCSFNRWMYPGGVLPPQKMVQAENGSHLKATVYVPRDAYMMDFVFSESEEGGIYDNRNGLDYHIPVFGSIAKEPPMHIVH 1230
Cdd:PLN02316 513 RGSFNRWTHRLGPLPPQKMVPADNGSHLKATVKVPLDAYMMDFVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVH 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1231 IAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLHIHQSFSWGGSEIKVWRGLVEGLCVYFLEP 1310
Cdd:PLN02316 593 IAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCLNLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEP 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1311 QNGMFGVGYVYG-RDDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANARVVFTIHNLEFGA 1389
Cdd:PLN02316 673 QNGMFWAGCVYGcRNDGERFGFFCHAALEFLLQSGFHPDIIHCHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGA 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1390 HHIGKAMRYCDKATTVSNTYSKEVSGHGAIVPHLGKFYGILNGIDPDIWDPYNDNFIPVHYTCENVVEGKRAAKRALQQK 1469
Cdd:PLN02316 753 NHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQR 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1470 FGLQQIDVPVVGIVTRLTAQKGIHLIKHAIHRTLERNGQVVLLGSAPDSRIQADFVNLANKLHGVNHGQVRLSLTYDEPL 1549
Cdd:PLN02316 833 LGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPL 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1550 SHLIYAGSDFILVPSIFEPCGLTQLVAMRYGTIPIVRKTGGLFDTVFDVDNDKERARDRGLEPNGFSFDGADSNGVDYAL 1629
Cdd:PLN02316 913 SHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGLFDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYAL 992
|
970 980 990 1000
....*....|....*....|....*....|....*....|....
gi 1162503518 1630 NRAISAWFDARSWFHSLCKRVMEQDWSWNRPALDYIELYRSASK 1673
Cdd:PLN02316 993 NRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSARK 1036
|
|
| GT5_Glycogen_synthase_DULL1-like |
cd03791 |
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ... |
1227-1670 |
3.46e-178 |
|
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: 543.70 E-value: 3.46e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1227 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLH---IHQSFSWGGSEIKVWRGLVEGL 1303
Cdd:cd03791 1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRvlgLEVKVGGRGEEVGVFELPVDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1304 CVYFLEPQNgMFGVGYVYGR------DDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANAR 1377
Cdd:cd03791 81 DYYFLDNPE-FFDRPGLPGPpgydypDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1378 VVFTIHNLE----FGAHHIGK------------------------AMRYCDKATTVSNTYSKEV-------SGHGAIVPH 1422
Cdd:cd03791 160 TVFTIHNLAyqglFPLDTLAElglppelfhidglefygqinflkaGIVYADRVTTVSPTYAKEIltpeygeGLDGVLRAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1423 LGKFYGILNGIDPDIWDPYNDNFIPVHYTcENVVEGKRAAKRALQQKFGLQQ-IDVPVVGIVTRLTAQKGIHLIKHAIHR 1501
Cdd:cd03791 240 AGKLSGILNGIDYDEWNPATDKLIPANYS-ANDLEGKAENKAALQKELGLPVdPDAPLFGFVGRLTEQKGVDLILDALPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1502 TLERNGQVVLLGSApDSRIQADFVNLANKlhgvNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGT 1581
Cdd:cd03791 319 LLEEGGQLVVLGSG-DPEYEQAFRELAER----YPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1582 IPIVRKTGGLFDTVFDVDNDKErardrglEPNGFSFDGADSNGVDYALNRAISAWFDaRSWFHSLCKRVMEQDWSWNRPA 1661
Cdd:cd03791 394 LPIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKNAMKQDFSWDKSA 465
|
....*....
gi 1162503518 1662 LDYIELYRS 1670
Cdd:cd03791 466 KEYLELYRS 474
|
|
| GlgA |
COG0297 |
Glycogen synthase [Carbohydrate transport and metabolism]; |
1226-1671 |
3.11e-172 |
|
Glycogen synthase [Carbohydrate transport and metabolism];
Pssm-ID: 440066 [Multi-domain] Cd Length: 476 Bit Score: 527.74 E-value: 3.11e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1226 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCL--NLSNVKNL-HIHQSFSWGGSEIKVWRGLVEG 1302
Cdd:COG0297 1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIddKLKDLEVVaSLEVPLGGRTYYARVLEGPDDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1303 LCVYFLEpQNGMFGVGYVYGR------DDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANA 1376
Cdd:COG0297 81 VPVYFID-NPELFDRPGPYGDpdrdypDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1377 RVVFTIHNLE----FGAHHIGK------------------------AMRYCDKATTVSNTYSKEV----SGHG---AIVP 1421
Cdd:COG0297 160 KTVFTIHNLAyqgiFPAEILELlglppelftpdglefygqinflkaGIVYADRVTTVSPTYAREIqtpeFGEGldgLLRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1422 HLGKFYGILNGIDPDIWDPYNDNFIPVHYTCENVvEGKRAAKRALQQKFGL-QQIDVPVVGIVTRLTAQKGIHLIKHAIH 1500
Cdd:COG0297 240 RSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLpVDPDAPLIGMVSRLTEQKGLDLLLEALD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1501 RTLERNGQVVLLGSApDSRIQADFVNLANKlhgvNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYG 1580
Cdd:COG0297 319 ELLEEDVQLVVLGSG-DPEYEEAFRELAAR----YPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1581 TIPIVRKTGGLFDTVFDVDNDKERArdrglepNGFSFDGADSNGVDYALNRAISAWFDARSWfHSLCKRVMEQDWSWNRP 1660
Cdd:COG0297 394 TVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-RKLQRNAMKQDFSWEKS 465
|
490
....*....|.
gi 1162503518 1661 ALDYIELYRSA 1671
Cdd:COG0297 466 AKEYLELYREL 476
|
|
| glgA |
PRK00654 |
glycogen synthase GlgA; |
1226-1671 |
5.30e-165 |
|
glycogen synthase GlgA;
Pssm-ID: 234809 [Multi-domain] Cd Length: 466 Bit Score: 508.12 E-value: 5.30e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1226 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLHIhqsfsWGGSEIKVWRGLVE--GL 1303
Cdd:PRK00654 1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVV-----GRLDLFTVLFGHLEgdGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1304 CVYFLEPQNgMFGVGYVYG-RDDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSA--PVaWLHKENYAKssLANARVVF 1380
Cdd:PRK00654 76 PVYLIDAPH-LFDRPSGYGyPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGliPA-LLKEKYWRG--YPDIKTVF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1381 TIHNLE----FGAHHIG-----------------------KA-MRYCDKATTVSNTYSKEV----SGHG---AIVPHLGK 1425
Cdd:PRK00654 152 TIHNLAyqglFPAEILGelglpaeafhleglefygqisflKAgLYYADRVTTVSPTYAREIttpeFGYGlegLLRARSGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1426 FYGILNGIDPDIWDPYNDNFIPVHYTCENVvEGKRAAKRALQQKFGLQQIDVPVVGIVTRLTAQKGIHLIKHAIHRTLER 1505
Cdd:PRK00654 232 LSGILNGIDYDIWNPETDPLLAANYSADDL-EGKAENKRALQERFGLPDDDAPLFAMVSRLTEQKGLDLVLEALPELLEQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1506 NGQVVLLGSaPDSRIQADFVNLANKLHGvnhgQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGTIPIV 1585
Cdd:PRK00654 311 GGQLVLLGT-GDPELEEAFRALAARYPG----KVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1586 RKTGGLFDTVFDVDNDKERArdrglepNGFSFDGADSNGVDYALNRAISAWFDARSWfHSLCKRVMEQDWSWNRPALDYI 1665
Cdd:PRK00654 386 RRTGGLADTVIDYNPEDGEA-------TGFVFDDFNAEDLLRALRRALELYRQPPLW-RALQRQAMAQDFSWDKSAEEYL 457
|
....*.
gi 1162503518 1666 ELYRSA 1671
Cdd:PRK00654 458 ELYRRL 463
|
|
| glgA |
TIGR02095 |
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ... |
1226-1671 |
1.66e-155 |
|
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: 483.31 E-value: 1.66e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1226 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLHI--HQSFSWGGS--EIKVWRGLVE 1301
Cdd:TIGR02095 1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVveLVDLSVGPRtlYVKVFEGVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1302 GLCVYFLEPQNGMFGVGYVYG---RDDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSslaNARV 1378
Cdd:TIGR02095 81 GVPVYFIDNPSLFDRPGGIYGddyPDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRPN---PIKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1379 VFTIHNLE----FGAHHIGK------------------------AMRYCDKATTVSNTYSKEV----SG---HGAIVPHL 1423
Cdd:TIGR02095 158 VFTIHNLAyqgvFPADDFSElglppeyfhmeglefygrvnflkgGIVYADRVTTVSPTYAREIltpeFGyglDGVLKARS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1424 GKFYGILNGIDPDIWDPYNDNFIPVHYTCENVvEGKRAAKRALQQKFGLQQI-DVPVVGIVTRLTAQKGIHLIKHAIHRT 1502
Cdd:TIGR02095 238 GKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPVDdDVPLFGVISRLTQQKGVDLLLAALPEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1503 LERNGQVVLLGSApDSRIQADFVNLANKlhgvNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGTI 1582
Cdd:TIGR02095 317 LELGGQLVVLGTG-DPELEEALRELAER----YPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1583 PIVRKTGGLFDTVFDVDNDKERArdrglepNGFSFDGADSNGVDYALNRAISAWFDARSWFHSLCKRVMEQDWSWNRPAL 1662
Cdd:TIGR02095 392 PIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSAK 464
|
....*....
gi 1162503518 1663 DYIELYRSA 1671
Cdd:TIGR02095 465 QYVELYRSL 473
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1226-1671 |
1.37e-142 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 465.92 E-value: 1.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1226 MHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLH-----IHQSFSWGGSEIKVWRGLV 1300
Cdd:PLN02939 482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKvldvvVESYFDGNLFKNKIWTGTV 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1301 EGLCVYFLEPQN--GMFGVGYVYGRDDD-RRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANAR 1377
Cdd:PLN02939 562 EGLPVYFIEPQHpsKFFWRAQYYGEHDDfKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKGFNSAR 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1378 VVFTIHNLEF--------------GAHHIGKAMRYCDKA-----------------TTVSNTYSKEVSGHG------AIV 1420
Cdd:PLN02939 642 ICFTCHNFEYqgtapasdlascglDVHQLDRPDRMQDNAhgrinvvkgaivysnivTTVSPTYAQEVRSEGgrglqdTLK 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1421 PHLGKFYGILNGIDPDIWDPYNDNFIPVHYTCeNVVEGKRAAKRALQQKFGLQQIDV--PVVGIVTRLTAQKGIHLIKHA 1498
Cdd:PLN02939 722 FHSKKFVGILNGIDTDTWNPSTDRFLKVQYNA-NDLQGKAANKAALRKQLGLSSADAsqPLVGCITRLVPQKGVHLIRHA 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1499 IHRTLERNGQVVLLGSAPDSRIQADFVNLANklHGVNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMR 1578
Cdd:PLN02939 801 IYKTAELGGQFVLLGSSPVPHIQREFEGIAD--QFQSNNNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMR 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1579 YGTIPIVRKTGGLFDTVFDVDNDKERARDRglepNGFSFDGADSNGVDYALNRAISAWFDARSWFHSLCKRVMEQDWSWN 1658
Cdd:PLN02939 879 YGSVPIVRKTGGLNDSVFDFDDETIPVELR----NGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWD 954
|
490
....*....|...
gi 1162503518 1659 RPALDYIELYRSA 1671
Cdd:PLN02939 955 SSASQYEELYQRA 967
|
|
| PRK14099 |
PRK14099 |
glycogen synthase GlgA; |
1225-1670 |
1.02e-77 |
|
glycogen synthase GlgA;
Pssm-ID: 237610 [Multi-domain] Cd Length: 485 Bit Score: 266.58 E-value: 1.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1225 PMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVqdLGHNVEV--ILPKYGCL--NLSNVKNLHIHQSFsWGGSEiKVWRGLV 1300
Cdd:PRK14099 3 PLRVLSVASEIFPLIKTGGLADVAGALPAAL--KAHGVEVrtLVPGYPAVlaGIEDAEQVHSFPDL-FGGPA-RLLAARA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1301 EGLCVYFLE-------PQNGMFGVGYVYGRDDDRRFGFFCR--SALEFLLQSGSSPNIIHCHDWSSAPV-AWLHKENYAK 1370
Cdd:PRK14099 79 GGLDLFVLDaphlydrPGNPYVGPDGKDWPDNAQRFAALARaaAAIGQGLVPGFVPDIVHAHDWQAGLApAYLHYSGRPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1371 SSlanarVVFTIHNL----EFGAHHIG-----------------------KA-MRYCDKATTVSNTYSKEVSG--HGAIV 1420
Cdd:PRK14099 159 PG-----TVFTIHNLafqgQFPRELLGalglppsafsldgveyyggigylKAgLQLADRITTVSPTYALEIQGpeAGMGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1421 PHL-----GKFYGILNGIDPDIWDPYNDNFIPVHYTCENvVEGKRAAKRALQQKFGLQ-QIDVPVVGIVTRLTAQKGIHL 1494
Cdd:PRK14099 234 DGLlrqraDRLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDpDPDALLLGVISRLSWQKGLDL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1495 IKHAIHrTLERNG-QVVLLGSApDSRIQADFVNLANKlhgvNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQ 1573
Cdd:PRK14099 313 LLEALP-TLLGEGaQLALLGSG-DAELEARFRAAAQA----YPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1574 LVAMRYGTIPIVRKTGGLFDTVFDVDndkERARDRGLePNGFSFDGADSNGVDYALNRAISAWFDARSWfHSLCKRVMEQ 1653
Cdd:PRK14099 387 LCALRYGAVPVVARVGGLADTVVDAN---EMAIATGV-ATGVQFSPVTADALAAALRKTAALFADPVAW-RRLQRNGMTT 461
|
490
....*....|....*..
gi 1162503518 1654 DWSWNRPALDYIELYRS 1670
Cdd:PRK14099 462 DVSWRNPAQHYAALYRS 478
|
|
| Glyco_transf_5 |
pfam08323 |
Starch synthase catalytic domain; |
1228-1413 |
1.67e-59 |
|
Starch synthase catalytic domain;
Pssm-ID: 400563 [Multi-domain] Cd Length: 239 Bit Score: 204.87 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1228 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLN-----LSNVKNLHIHQSFSWGGSEIKVWRGLVEG 1302
Cdd:pfam08323 1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPeernqLEDVIRLSVAAGVPVRPLTVGVARLELDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1303 LCVYFLEPQNgMFGVGYVYGR------DDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLHKENYAKSSLANA 1376
Cdd:pfam08323 81 VDVYFLDNPD-YFDRPGLYGDdgrdyeDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162503518 1377 RVVFTIHNLE----FGAHHIGK------------------------AMRYCDKATTVSNTYSKEV 1413
Cdd:pfam08323 160 KTVFTIHNLAyqgrFPADLLDLlglppedfnldglefygqinflkaGIVYADAVTTVSPTYAEEI 224
|
|
| PRK14098 |
PRK14098 |
starch synthase; |
1228-1669 |
6.06e-57 |
|
starch synthase;
Pssm-ID: 172588 [Multi-domain] Cd Length: 489 Bit Score: 206.12 E-value: 6.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1228 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLGHNVEVILPKYGCLN-----LSNVKNLhihqsfswggSEIKV-WRGLVE 1301
Cdd:PRK14098 8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTINdrkfrLHDVLRL----------SDIEVpLKEKTD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1302 GLCV------------YFLE-----PQNGMFGVGYVYG--RDDDRRFGFFCRSALEFLLQSGSSPNIIHCHDWSSAPVAW 1362
Cdd:PRK14098 78 LLHVkvtalpsskiqtYFLYnekyfKRNGLFTDMSLGGdlKGSAEKVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1363 LHKENYAKSSL-ANARVVFTIHNLE------------------FGAHHIGK--------AMRYCDKATTVSNTYSKEVSG 1415
Cdd:PRK14098 158 LLKTVYADHEFfKDIKTVLTIHNVYrqgvlpfkvfqkllpeevCSGLHREGdevnmlytGVEHADLLTTTSPRYAEEIAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1416 HGAIVPHLGK--------FYGILNGIDPDIWDPYNDNFIPVHYTCENVvEGKRAAKRALQQKFGLQ-QIDVPVVGIVTRL 1486
Cdd:PRK14098 238 DGEEAFGLDKvleerkmrLHGILNGIDTRQWNPSTDKLIKKRYSIERL-DGKLENKKALLEEVGLPfDEETPLVGVIINF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1487 TAQKGIHLIKHAIHRTLERNGQVVLLGSApDSRIQADFVNLANKlhgvNHGQVRLSLTYDEPLSHLIYAGSDFILVPSIF 1566
Cdd:PRK14098 317 DDFQGAELLAESLEKLVELDIQLVICGSG-DKEYEKRFQDFAEE----HPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1567 EPCGLTQLVAMRYGTIPIVRKTGGLFDTVFDVDNDKErardrglepNGFSFDGADSNGVDYALNRAISAWFDARSWfHSL 1646
Cdd:PRK14098 392 ESCGMLQMFAMSYGTIPVAYAGGGIVETIEEVSEDKG---------SGFIFHDYTPEALVAKLGEALALYHDEERW-EEL 461
|
490 500
....*....|....*....|...
gi 1162503518 1647 CKRVMEQDWSWNRPALDYIELYR 1669
Cdd:PRK14098 462 VLEAMERDFSWKNSAEEYAQLYR 484
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
1133-1215 |
1.61e-20 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 86.96 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1133 VLYNPSNtvltgKPEVWFRCSFNRWMYPGGVlPPQKMVQAENGSHLKATVYVPRDAYMMDFVFSESeeGGIYDNRNGLDY 1212
Cdd:pfam16760 2 IYYNGSL-----AKEVYIHGGFNGWKNVQDV-PMEKLPPTGGGDWFSATVPVPEDAYVLDFVFKDG--AGNWDNNNGQNY 73
|
...
gi 1162503518 1213 HIP 1215
Cdd:pfam16760 74 HIP 76
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
1227-1669 |
1.77e-20 |
|
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: 95.30 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1227 HIVHIAVEMAPiaKVGGLGDVVTSLSRAVQDLGHNVEVIlpkygclnlsnvknlhihqSFSWGGSEIKVWRGLVEGLCVY 1306
Cdd:cd03801 1 KILLLSPELPP--PVGGAERHVRELARALAARGHDVTVL-------------------TPADPGEPPEELEDGVIVPLLP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1307 FLEpqngmfgvGYVYGRDDDRRFGFFCRSAlefllqsgsSPNIIHCHDWSSAPVAWLHKEnyakssLANARVVFTIHNLE 1386
Cdd:cd03801 60 SLA--------ALLRARRLLRELRPLLRLR---------KFDVVHAHGLLAALLAALLAL------LLGAPLVVTLHGAE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1387 FGAH------------HIGKAMRYCDKATTVSNTYSKEVSGHGAIVPHlgKFYGILNGIDPDIWDPyndnfipvhytcen 1454
Cdd:cd03801 117 PGRLllllaaerrllaRAEALLRRADAVIAVSEALRDELRALGGIPPE--KIVVIPNGVDLERFSP-------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1455 vvegkraakrALQQKFGLQQiDVPVVGIVTRLTAQKGIHLIKHAIHRTLERNGQVVLL--GSAPDSRiqadfVNLANKLH 1532
Cdd:cd03801 181 ----------PLRRKLGIPP-DRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVivGGDGPLR-----AELEELEL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1533 GVnHGQVRL--SLTYDEPLShlIYAGSDFILVPSIFEPCGLTQLVAMRYGTiPIVrktgglfdtVFDVDNDKERARDRGl 1610
Cdd:cd03801 245 GL-GDRVRFlgFVPDEELPA--LYAAADVFVLPSRYEGFGLVVLEAMAAGL-PVV---------ATDVGGLPEVVEDGE- 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162503518 1611 epNGFSFDGADSNgvdyALNRAISAWFDARSWFHSLCKR---VMEQDWSWNRPALDYIELYR 1669
Cdd:cd03801 311 --GGLVVPPDDVE----ALADALLRLLADPELRARLGRAareRVAERFSWERVAERLLDLYR 366
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
796-874 |
9.02e-20 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 85.04 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 796 LYFNRDLSavanePDVLIKGAFNGWKWR--FFTEKLhKSELAGDWWCCKLYIPKQAYRMDFVFFNGHTVYENNNNNDFVI 873
Cdd:pfam16760 2 IYYNGSLA-----KEVYIHGGFNGWKNVqdVPMEKL-PPTGGGDWFSATVPVPEDAYVLDFVFKDGAGNWDNNNGQNYHI 75
|
.
gi 1162503518 874 Q 874
Cdd:pfam16760 76 P 76
|
|
| CBM53 |
pfam16760 |
Starch/carbohydrate-binding module (family 53); |
970-1055 |
2.47e-18 |
|
Starch/carbohydrate-binding module (family 53);
Pssm-ID: 465261 [Multi-domain] Cd Length: 76 Bit Score: 80.80 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 970 RLYYNINSRPlvhstEIWMHGGYNNWIDGLS-FAERLvhHHDKDCDWWFADVVVPERTYVLDWVFADGppgsARNYDNNG 1048
Cdd:pfam16760 1 NIYYNGSLAK-----EVYIHGGFNGWKNVQDvPMEKL--PPTGGGDWFSATVPVPEDAYVLDFVFKDG----AGNWDNNN 69
|
....*..
gi 1162503518 1049 GHDFHAT 1055
Cdd:pfam16760 70 GQNYHIP 76
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
1128-1216 |
1.90e-14 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 70.08 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1128 GTTIDVLYNPSNTVlTGKPEVWFRCSF--NRWMYpggvLPPQKMVQAENGsHLKATVYVpRDAYMMDFVFSEseEGGIYD 1205
Cdd:smart01066 1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTD----VPDVRMEKTGEG-WVKATIPV-KEAYKLNFCFKD--GAGNWD 71
|
90
....*....|.
gi 1162503518 1206 NRNGLDYHIPV 1216
Cdd:smart01066 72 NNGGANYHFEI 82
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
968-1054 |
2.49e-14 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 69.69 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 968 TVRLYYNINSRPLvHSTEIWMHGGY--NNWIDGLSFAERlvhhhdKDCDWWFADVVVPERTYVLDWVFADGppgsARNYD 1045
Cdd:smart01066 3 TVTVYYNGLLATS-GAKNVYLHYGFgeNNWTDVPDVRME------KTGEGWVKATIPVKEAYKLNFCFKDG----AGNWD 71
|
....*....
gi 1162503518 1046 NNGGHDFHA 1054
Cdd:smart01066 72 NNGGANYHF 80
|
|
| CBM_25 |
smart01066 |
Carbohydrate binding domain; |
791-875 |
3.17e-12 |
|
Carbohydrate binding domain;
Pssm-ID: 198134 [Multi-domain] Cd Length: 83 Bit Score: 63.91 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 791 DSTIDLYFNRDLSAVANEPDVLIKGaFNGWKWRFFTEklHKSELAGDWWCCKLYIPKQAYRMDFVFFNGHTVYENNNNND 870
Cdd:smart01066 1 GNTVTVYYNGLLATSGAKNVYLHYG-FGENNWTDVPD--VRMEKTGEGWVKATIPVKEAYKLNFCFKDGAGNWDNNGGAN 77
|
....*
gi 1162503518 871 FVIQI 875
Cdd:smart01066 78 YHFEI 82
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
1347-1595 |
5.08e-12 |
|
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: 69.31 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1347 PNIIHCHDWSSAPVAWLhkenyaKSSLANARVVFTIHNLE-----FGAHHIgKAMRYCDKATTVSN-TYSKEVSGHGAIv 1420
Cdd:cd03819 77 IDLIHAHSRAPAWLGWL------ASRLTGVPLVTTVHGSYlatyhPKDFAL-AVRARGDRVIAVSElVRDHLIEALGVD- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1421 phLGKFYGILNGIDPDIWDPyndnfipvhytcenvvegkrAAKRALQQKFGLQQiDVPVVGIVTRLTAQKGIHLIKHAIH 1500
Cdd:cd03819 149 --PERIRVIPNGVDTDRFPP--------------------EAEAEERAQLGLPE-GKPVVGYVGRLSPEKGWLLLVDAAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1501 RtLERNGQVVLL--GSAPdsriQADFVNLANKLHGVNHgqvRLSLT-YDEPLSHLiYAGSDFILVPSIFEPCGLTQLVAM 1577
Cdd:cd03819 206 E-LKDEPDFRLLvaGDGP----ERDEIRRLVERLGLRD---RVTFTgFREDVPAA-LAASDVVVLPSLHEEFGRVALEAM 276
|
250
....*....|....*...
gi 1162503518 1578 RYGTIPIVRKTGGLFDTV 1595
Cdd:cd03819 277 ACGTPVVATDVGGAREIV 294
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
63-189 |
2.21e-10 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 65.66 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 63 TASPNVKVAAYSNYAPRLLVESSSKKSEHhdSSRHREETIDTYNGLSGSDAAElTSNRDVEIEVDLQHISEEelpgkvsi 142
Cdd:PLN02316 1 MSTSKPKGSAPRGFAPRTTVESSQKRIQQ--NNGDKEDSSTSTSSLSVSAVEK-TSNAKEEIQVDFQHNSES-------- 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1162503518 143 naSLGEMETVDEAEVEEDKFEVDTSGIVLRNVAVREVDPKDEHNAKD 189
Cdd:PLN02316 70 --AVEEVEAEDEIEVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLD 114
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
1332-1664 |
1.15e-09 |
|
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: 62.26 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1332 FCRSALEFLLQSGSSPNIIHCHDWSSAPVAWLhkenyAKSSLaNARVVFTIHNLE------------------FGAHHIg 1393
Cdd:cd03800 87 FADGLLRFIAREGGRYDLIHSHYWDSGLVGAL-----LARRL-GVPLVHTFHSLGrvkyrhlgaqdtyhpslrITAEEQ- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1394 kAMRYCDK--ATT------VSNTYSKEVSgHGAIVPhlgkfygilNGIDPDIWDPYNDnfipvhytcenvvegkRAAKRA 1465
Cdd:cd03800 160 -ILEAADRviASTpqeadeLISLYGADPS-RINVVP---------PGVDLERFFPVDR----------------AEARRA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1466 LqqkFGLQQiDVPVVGIVTRLTAQKGIH-LIK-HAIHRTLERNGQVVLLGSAPDSRIQADFVNLAN--KLHGVNhGQVRL 1541
Cdd:cd03800 213 R---LLLPP-DKPVVLALGRLDPRKGIDtLVRaFAQLPELRELANLVLVGGPSDDPLSMDREELAElaEELGLI-DRVRF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1542 SLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGTIPIVRKTGGLFDTVFDvdndkerardrglEPNGFSFDGAD 1621
Cdd:cd03800 288 PGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRD-------------GRTGLLVDPHD 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1162503518 1622 SNgvdyALNRAISAWFDARSWFHSLCKRVME---QDWSWNRPALDY 1664
Cdd:cd03800 355 PE----ALAAALRRLLDDPALWQRLSRAGLErarAHYTWESVADQL 396
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
1346-1606 |
1.42e-09 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 61.96 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1346 SPNIIHCHDWSSAPVAWLHkenYAKSslANARVVFTIHNLEFGAHHIGKAMRYCDKATTVSNTYSKEVSGHGAIVPhlgK 1425
Cdd:cd03823 96 RPDVVHTHNLSGLGASLLD---AARD--LGIPVVHTLHDYWLLCPRQFLFKKGGDAVLAPSRFTANLHEANGLFSA---R 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1426 FYGILNGIDPDIWDPyndnfipvhytcenvVEGKRAAKRalqqkfglqqidvPVVGIVTRLTAQKGIHLIKHAIHRTLER 1505
Cdd:cd03823 168 ISVIPNAVEPDLAPP---------------PRRRPGTER-------------LRFGYIGRLTEEKGIDLLVEAFKRLPRE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1506 NGQVVLLGSAPDSRIQADFVNLANKLHGvnhgqvrlSLTYDEPLSHliYAGSDFILVPSIF-EPCGLTQLVAMRYGTIPI 1584
Cdd:cd03823 220 DIELVIAGHGPLSDERQIEGGRRIAFLG--------RVPTDDIKDF--YEKIDVLVVPSIWpEPFGLVVREAIAAGLPVI 289
|
250 260 270
....*....|....*....|....*....|
gi 1162503518 1585 VRKTGGL--------FDTVFDVDNDKERAR 1606
Cdd:cd03823 290 ASDLGGIaeliqpgvNGLLFAPGDAEDLAA 319
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
1551-1673 |
4.03e-09 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 56.15 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1551 HLIYAGSDFILVPSIFEPCGLTQLVAMRYGTIPIVRKTGGLFDTVFDvdndkerardrglEPNGFSFDGADSNGVDYALN 1630
Cdd:COG0438 15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED-------------GETGLLVPPGDPEALAEAIL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1162503518 1631 RAISAwFDARSWFHSLCKRVMEQDWSWNRPALDYIELYRSASK 1673
Cdd:COG0438 82 RLLED-PELRRRLGEAARERAEERFSWEAIAERLLALYEELLA 123
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
1483-1600 |
4.49e-09 |
|
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: 58.95 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1483 VTRLTAQKGIHLIKHAIHRTLER--NGQVVLLGSAPDSriqaDFVNLANKLHGVNHGQVRLSLTYDEPLSHLIYAGSDFI 1560
Cdd:cd01635 116 VGRLVPEKGIDLLLEALALLKARlpDLVLVLVGGGGER----EEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVF 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1162503518 1561 LVPSIFEPCGLTQLVAMRYGTIPIVRKTGGLFDTVFDVDN 1600
Cdd:cd01635 192 VLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGEN 231
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
1280-1585 |
3.58e-08 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 57.37 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1280 LHIHQSFSWGGSEiKVWRGLVEGLC--------------VYFLEPQNGMFGVGYVYGRDDDRRFGFFCRSALEFL-LQSG 1344
Cdd:cd03811 3 LFVIPSLSGGGAE-RVLLNLANALDkrgydvtlvllrdeGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKrILKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1345 SSPNIIHCHDWSSAPVAwlhkenyAKSSLANARVVFTIHN-------LEFGAHHIGKAMRYCDKATTVSNTYSKEVSGHG 1417
Cdd:cd03811 82 AKPDVVISFLGFATYIV-------AKLAAARSKVIAWIHSslsklyyLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1418 AIVPHlgKFYGILNGIDPDiwdpyndnfipvhytcenvvegkrAAKRALQQKFGLQQIDVPVVGIVTRLTAQKGIHLIKH 1497
Cdd:cd03811 155 PSPPE--KIEVIYNPIDID------------------------RIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1498 AIHRTLERNGQV--VLLGSAPDsriQADFVNLANKLhGVNHgQVRL----SLTYDeplshlIYAGSDFILVPSIFEPCGL 1571
Cdd:cd03811 209 AFAKLRKKYPDVklVILGDGPL---REELEKLAKEL-GLAE-RVIFlgfqSNPYP------YLKKADLFVLSSRYEGFPN 277
|
330
....*....|....
gi 1162503518 1572 TQLVAMRYGTiPIV 1585
Cdd:cd03811 278 VLLEAMALGT-PVV 290
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
1476-1595 |
3.59e-08 |
|
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: 54.59 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1476 DVPVVGIVTRLTAQKGIHLIKHAIHRTLERNGQVVLL--GSAPDsriQADFVNLANKLHGVNHGQVRLSLTYDEPlsHLI 1553
Cdd:pfam00534 1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEE---EKRLKKLAEKLGLGDNVIFLGFVSDEDL--PEL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1162503518 1554 YAGSDFILVPSIFEPCGLTQLVAMRYGTIPIVRKTGGLFDTV 1595
Cdd:pfam00534 76 LKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV 117
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
1242-1436 |
1.25e-07 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 53.31 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1242 GGLGDVVTSLSRAVQDLGHNVEVILPKYGCLNLSNVKNLHIHqsfswggseikvwrglveglcvyflepqngmfgVGYVY 1321
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRV---------------------------------PRVPL 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1322 GRDDDRRFGFFCRSALEFLLQSGSsPNIIHCHDWSSAPVAWLhkenyAKSSLANARVVFTIHNLEFGAHHIG-------- 1393
Cdd:pfam13439 48 PLPPRLLRSLAFLRRLRRLLRRER-PDVVHAHSPFPLGLAAL-----AARLRLGIPLVVTYHGLFPDYKRLGarlsplrr 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1162503518 1394 -------KAMRYCDKATTVSNtYSKEvsghgaivpHLGKFYG--------ILNGIDPD 1436
Cdd:pfam13439 122 llrrlerRLLRRADRVIAVSE-AVAD---------ELRRLYGvppekirvIPNGVDLE 169
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
1478-1599 |
2.38e-06 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 48.66 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1478 PVVGIVTRLTA-QKGIHLIKHAIHRTLERNGQVVLL--GSAPDSRIQADFVNLANKLHgvNHGQVrlsltydEPLSHLiY 1554
Cdd:pfam13692 2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVivGDGPEEELEELAAGLEDRVI--FTGFV-------EDLAEL-L 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1162503518 1555 AGSDFILVPSIFEPCGLTQLVAMRYGTiPIV-RKTGGLFDTVFDVD 1599
Cdd:pfam13692 72 AAADVFVLPSLYEGFGLKLLEAMAAGL-PVVaTDVGGIPELVDGEN 116
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
1336-1585 |
3.11e-05 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 48.13 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1336 ALEFLLQSGSSPNIIHCHDwssapvawlhkeNYAKSSLANARVVFTIHNL------------EFGAHHIG--KAMRYCDK 1401
Cdd:cd03809 74 WLQILLPKKDKPDLLHSPH------------NTAPLLLKGCPQVVTIHDLiplrypeffpkrFRLYYRLLlpISLRRADA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1402 ATTVSNtYSK-EVSGHGAIVPHlgKFYGILNGIDPDIwdpyndnfipvhytCENVVEGKRAAKRALQQKFGLqqidvpVV 1480
Cdd:cd03809 142 IITVSE-ATRdDIIKFYGVPPE--KIVVIPLGVDPSF--------------FPPESAAVLIAKYLLPEPYFL------YV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1481 GivtRLTAQKGIH-LIK-HAIHRTLERNGQVVLLGSAPDSRiqADFVNLANKLHGvnHGQVRLsLTY--DEPLSHLiYAG 1556
Cdd:cd03809 199 G---TLEPRKNHErLLKaFALLKKQGGDLKLVIVGGKGWED--EELLDLVKKLGL--GGRVRF-LGYvsDEDLPAL-YRG 269
|
250 260
....*....|....*....|....*....
gi 1162503518 1557 SDFILVPSIFEPCGLTQLVAMRYGTiPIV 1585
Cdd:cd03809 270 ARAFVFPSLYEGFGLPVLEAMACGT-PVI 297
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
1278-1585 |
5.52e-04 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 44.23 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1278 KNLHIHQSFSWGGSEIKVWRgLVEGL--------CVYFLEPqnGMFGVG--------YVYGRDDDRRFGFFCRsaLEFLL 1341
Cdd:cd03807 1 KVAHVITGLNVGGAETMLLR-LLEHMdksrfehvVISLTGD--GVLGEEllaagvpvVCLGLSSGKDPGVLLR--LAKLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1342 QSGSsPNIIHCH----DWSSAPVAWLhkenyakssLANARVVFTIHNlefgahhigkamrycdkattvSNTYSKEVSGHG 1417
Cdd:cd03807 76 RKRN-PDVVHTWmyhaDLIGGLAAKL---------AGGVKVIWSVRS---------------------SNIPQRLTRLVR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1418 AIVPHLGKFYGILNGIDP--------DIWDPYNDNFIPVHYTCENVV--EGKRAAKRalqQKFGLQQiDVPVVGIVTRLT 1487
Cdd:cd03807 125 KLCLLLSKFSPATVANSSavaefhqeQGYAKNKIVVIYNGIDLFKLSpdDASRARAR---RRLGLAE-DRRVIGIVGRLH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1488 AQKGIHLIKHAIHRTLERNGQVVLL-----GSAPDSRIQADFVNLANKLHGVNHGQvrlsltyDEP--LSHLiyagsDFI 1560
Cdd:cd03807 201 PVKDHSDLLRAAALLVETHPDLRLLlvgrgPERPNLERLLLELGLEDRVHLLGERS-------DVPalLPAM-----DIF 268
|
330 340
....*....|....*....|....*
gi 1162503518 1561 LVPSIFEPCGLTQLVAMRYGtIPIV 1585
Cdd:cd03807 269 VLSSRTEGFPNALLEAMACG-LPVV 292
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
1429-1670 |
7.25e-04 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 43.86 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1429 ILNGIDPDIWDPYNdnfipvhytcenvvegKRAAKRalqqKFGLQQiDVPVVGIVTRLTAQ--KGIH-LIK--HAIHRtl 1503
Cdd:cd03825 166 IPNGIDTEIFAPVD----------------KAKARK----RLGIPQ-DKKVILFGAESVTKprKGFDeLIEalKLLAT-- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1504 ERNGQVVLLGSAPDSRIQADFvnlanklhgvNHgqVRLSLTYDEPLSHLIYAGSDFILVPSIFEPCGLTQLVAMRYGTIP 1583
Cdd:cd03825 223 KDDLLLVVFGKNDPQIVILPF----------DI--ISLGYIDDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162503518 1584 IVRKTGGLFDTVFDVDNDKerardrgLEPNGfsfdgaDSNGVDYALNRAISAWFDARSwFHSLCKRVMEQDWSWNRPALD 1663
Cdd:cd03825 291 VAFDTGGSPEIVQHGVTGY-------LVPPG------DVQALAEAIEWLLANPKERES-LGERARALAENHFDQRVQAQR 356
|
....*..
gi 1162503518 1664 YIELYRS 1670
Cdd:cd03825 357 YLELYKD 363
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
888-938 |
7.53e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 7.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1162503518 888 LAEEKQRELENLANEEAERRRQTDEQRRMEEER-----AADKADRVQAKVEVETKK 938
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQQEEERkrkklELEKEKRDRKRAEEQRRK 495
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
889-941 |
2.67e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.33 E-value: 2.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1162503518 889 AEEKQRELENLAnEEAERRRQTDEQRRMEEERAADKADRVQAKVEVETKKNKL 941
Cdd:COG3064 62 AEAEQRAAELAA-EAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKA 113
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
888-927 |
5.17e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 39.26 E-value: 5.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1162503518 888 LAEEKQRELENLANEEAE-RRRQTDEQRRMEEERAADKADR 927
Cdd:pfam15346 86 ILEENNRKIEEAQRKEAEeRLAMLEEQRRMKEERQRREKEE 126
|
|
| |
