|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
2-261 |
7.93e-175 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 481.93 E-value: 7.93e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 2 KTLATIGDNCVDIYPQLNKAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQ 81
Cdd:PRK09813 1 KKLATIGDNCVDIYPQLGKAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 82 VELHDNDRVFGDYTEGVMADFALSEEDYAWLAQYDIVHAAIWGHAEDAFPQLHAAGKLTAFDFSDKWDSPLWQTLVPHLD 161
Cdd:PRK09813 81 VELHDNDRVFGDYTEGVMADFALSEEDYAWLAQYDIVHAAIWGHAEDAFPQLHAAGKLTAFDFSDKWDSPLWQTLVPHLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 162 FAFASAPQEDETLRLKMKAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLP 241
Cdd:PRK09813 161 YAFASAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLP 240
|
250 260
....*....|....*....|
gi 1929626394 242 QAIAQGTACAAKTIQYHGAW 261
Cdd:PRK09813 241 QAMAQGTACAAKTIQYHGAW 260
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
3-261 |
1.46e-135 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 382.47 E-value: 1.46e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 3 TLATIGDNCVDIYPQLNKAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQV 82
Cdd:cd01940 1 RLAAIGDNVVDKYLHLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAVADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 83 ELHDNDRVFGDYTEGVMADFALSEEDYAWLAQYDIVHAAI---WGHAEDAFPQLHAAGKLTAFDFSDKWDSPLWQTLVPH 159
Cdd:cd01940 81 ELVDGDRIFGLSNKGGVAREHPFEADLEYLSQFDLVHTGIyshEGHLEKALQALVGAGALISFDFSDRWDDDYLQLVCPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 160 LDFAFASAPQEDETLRL-KMKAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSAGM 238
Cdd:cd01940 161 VDFAFFSASDLSDEEVKaKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAGG 240
|
250 260
....*....|....*....|....
gi 1929626394 239 T-LPQAIAQGTACAAKTIQYHGAW 261
Cdd:cd01940 241 TaIAEAMRQGAQFAAKTCGHEGAF 264
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
4-261 |
2.68e-53 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 174.69 E-value: 2.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 4 LATIGDNCVDIYPQLN--------------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISH 69
Cdd:COG0524 2 VLVIGEALVDLVARVDrlpkggetvlagsfRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 70 VHTKHGV-TAQTQVEL-HDNDRVFgDYTEGVMADFALSEEDYAWLAQYDIVHAAIWGHAED--------AFPQLHAAGKL 139
Cdd:COG0524 82 VRRDPGApTGLAFILVdPDGERTI-VFYRGANAELTPEDLDEALLAGADILHLGGITLASEppreallaALEAARAAGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 140 TAFDFSdkWDSPLWQT-------LVPHLDFAFASapqEDETLRLK--------MKAIVARGAGTVIVTLGENGSIAWDGA 204
Cdd:COG0524 161 VSLDPN--YRPALWEParellreLLALVDILFPN---EEEAELLTgetdpeeaAAALLARGVKLVVVTLGAEGALLYTGG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626394 205 QFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLPQAIAQGTACAAKTIQYHGAW 261
Cdd:COG0524 236 EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ 292
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-260 |
1.41e-40 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 141.56 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 4 LATIGDNCVDIYP----------QLNKAFSGGnAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 73
Cdd:cd01166 2 VVTIGEVMVDLSPpgggrleqadSFRKFFGGA-EANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 74 HGV-TAQTQVELHDNDRVFGDYTEGVMADFALSEEDYAW--LAQYDIVH-----AAIWG----HAEDAFPQLHAAGKLTA 141
Cdd:cd01166 81 PGRpTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEaaLAGADHLHlsgitLALSEsareALLEALEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 142 FDFSdkWDSPLW---------QTLVPHLDFAFASapQEDETLRLKMKAI---------VARGAGTVIVTLGENGSIAWDG 203
Cdd:cd01166 161 FDLN--YRPKLWsaeearealEELLPYVDIVLPS--EEEAEALLGDEDPtdaaeralaLALGVKAVVVKLGAEGALVYTG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1929626394 204 AQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLPQAIAQGTACAAKTIQYHGA 260
Cdd:cd01166 237 GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
24-260 |
5.84e-37 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 132.08 E-value: 5.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGV-TAQTQVEL---HDNDRVFGDYTEGVM 99
Cdd:pfam00294 34 GGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDTrTGTALIEVdgdGERTIVFNRGAAADL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 100 aDFALSEEDYAWLAQYDIVHAA---IWGHAEDAFPQL-HAAGKLTAFDFSdkWDSPLWQT------LVPHLDFAFAS--- 166
Cdd:pfam00294 114 -TPEELEENEDLLENADLLYISgslPLGLPEATLEELiEAAKNGGTFDPN--LLDPLGAArealleLLPLADLLKPNeee 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 167 ------APQEDETLRLKM-KAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEP-VTVIDTMGAGDSFIAGFLCGWSAGM 238
Cdd:pfam00294 191 lealtgAKLDDIEEALAAlHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGK 270
|
250 260
....*....|....*....|..
gi 1929626394 239 TLPQAIAQGTACAAKTIQYHGA 260
Cdd:pfam00294 271 SLEEALRFANAAAALVVQKSGA 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
24-260 |
6.94e-33 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 120.88 E-value: 6.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK---HGVTAQTQVELHDNdRVFGDYtEGVMa 100
Cdd:cd01942 36 GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVdedSTGVAFILTDGDDN-QIAYFY-PGAM- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 101 DFALSEEDYAWLAQYDIVH-AAIWGHAEDAFpQLHAAGKLTAFDFSD---KWDSPLWQTLVPHLDFAFasaPQEDETLRL 176
Cdd:cd01942 113 DELEPNDEADPDGLADIVHlSSGPGLIELAR-ELAAGGITVSFDPGQelpRLSGEELEEILERADILF---VNDYEAELL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 177 KMK-----AIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVT-VIDTMGAGDSFIAGFLCGWSAGMTLPQAIAQGTAC 250
Cdd:cd01942 189 KERtglseAELASGVRVVVVTLGPKGAIVFEDGEEVEVPAVPAVkVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLA 268
|
250
....*....|
gi 1929626394 251 AAKTIQYHGA 260
Cdd:cd01942 269 ASLKVERRGA 278
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
24-260 |
1.09e-31 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 117.78 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG----VTAQTQVELhDNDRVFGDYTEGVM 99
Cdd:cd01945 36 GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGarspISSITDITG-DRATISITAIDTQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 100 ADFALSEEDyawLAQYDIVHAAiwGHAEDA----FPQLHAAGKLTAFDFsDKWDSPLWQTLVPHLDFAFASAP------- 168
Cdd:cd01945 115 APDSLPDAI---LGGADAVLVD--GRQPEAalhlAQEARARGIPIPLDL-DGGGLRVLEELLPLADHAICSENflrpntg 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 169 -QEDETLRLkmkaIVARGAGTVIVTLGENGSIAWDGA-QFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLPQAIAQ 246
Cdd:cd01945 189 sADDEALEL----LASLGIPFVAVTLGEAGCLWLERDgELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRF 264
|
250
....*....|....
gi 1929626394 247 GTACAAKTIQYHGA 260
Cdd:cd01945 265 ASAAAALKCRGLGG 278
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
7-261 |
6.35e-30 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 113.50 E-value: 6.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 7 IGDNCVDIYPQLN---KAFS---GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV-HTKHGVTAQ 79
Cdd:cd01167 5 FGEALIDFIPEGSgapETFTkapGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIqFDPAAPTTL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 80 TQVELHDN-DRVFgDYTEGVMADFALSEE-DYAWLAQYDIVH------------AAIwghaEDAFPQLHAAGKLTAFDF- 144
Cdd:cd01167 85 AFVTLDADgERSF-EFYRGPAADLLLDTElNPDLLSEADILHfgsialasepsrSAL----LELLEAAKKAGVLISFDPn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 145 --SDKWDSP-----LWQTLVPHLDFAFAS-------APQEDETLRLKmkAIVARGAGTVIVTLGENGSIAWDGAQFWRQA 210
Cdd:cd01167 160 lrPPLWRDEeeareRIAELLELADIVKLSdeelellFGEEDPEEIAA--LLLLFGLKLVLVTRGADGALLYTKGGVGEVP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1929626394 211 PEPVTVIDTMGAGDSFIAGFLCGWSAG-------MTLPQAIAQGTACAAKTIQYHGAW 261
Cdd:cd01167 238 GIPVEVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAGAI 295
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
24-260 |
4.39e-27 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 106.10 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVH-TKHGVTAQTQVELHDNdrvfGD----YTEGv 98
Cdd:cd01174 36 GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEvVVGAPTGTAVITVDES----GEnrivVVPG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 99 mADFALSEEDY----AWLAQYDIV-------HAAIwghaEDAFPQLHAAGKLTAFDFS--DKWDSPLWqtlvPHLDF--- 162
Cdd:cd01174 111 -ANGELTPADVdaalELIAAADVLllqleipLETV----LAALRAARRAGVTVILNPApaRPLPAELL----ALVDIlvp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 163 ----AFASAPQEDETLRLKMKA---IVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWS 235
Cdd:cd01174 182 neteAALLTGIEVTDEEDAEKAarlLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALA 261
|
250 260
....*....|....*....|....*
gi 1929626394 236 AGMTLPQAIAQGTACAAKTIQYHGA 260
Cdd:cd01174 262 RGLSLEEAIRFANAAAALSVTRPGA 286
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
23-260 |
1.43e-25 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 102.31 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 23 SGGNAVNVAVYCTRYGIQPGCitwVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVelhdndRVFGDY------TE 96
Cdd:cd01168 57 SAANTIRGAAALGGSAAFIGR---VGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAV------LVTPDAertmctYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 97 GVMADFALSEEDYAWLAQYDI--VHAAIWGHAEDAF----PQLHAAGKLTAFDFSDkWD------SPLWQtLVPHLDFAF 164
Cdd:cd01168 128 GAANELSPDDLDWSLLAKAKYlyLEGYLLTVPPEAIllaaEHAKENGVKIALNLSA-PFivqrfkEALLE-LLPYVDILF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 165 ASapqEDETLRLKM----------KAIVARGAGTVIVTLGENGSIAWDGAQ-FWRQAPEPVTVIDTMGAGDSFIAGFLCG 233
Cdd:cd01168 206 GN---EEEAEALAEaettddleaaLKLLALRCRIVVITQGAKGAVVVEGGEvYPVPAIPVEKIVDTNGAGDAFAGGFLYG 282
|
250 260
....*....|....*....|....*..
gi 1929626394 234 WSAGMTLPQAIAQGTACAAKTIQYHGA 260
Cdd:cd01168 283 LVQGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
24-260 |
1.63e-24 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 99.44 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDyGTKLKQDLARMGVDISHVHTKhGVTaQTQVELHDNDRvfGDYTEGVMADFA 103
Cdd:COG1105 35 GGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIE-GET-RINIKIVDPSD--GTETEINEPGPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 104 LSEEDYAWLAQY--DIVHAAIW---------GHAEDAFPQL----HAAGKLTAFDFSDkwdsplwqtlvPHLDFAFASAP 168
Cdd:COG1105 110 ISEEELEALLERleELLKEGDWvvlsgslppGVPPDFYAELirlaRARGAKVVLDTSG-----------EALKAALEAGP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 169 ------------------QEDETLRLKMKAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIAGF 230
Cdd:COG1105 179 dlikpnleeleellgrplETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGF 258
|
250 260 270
....*....|....*....|....*....|
gi 1929626394 231 LCGWSAGMTLPQAIAQGTACAAKTIQYHGA 260
Cdd:COG1105 259 LAGLARGLDLEEALRLAVAAGAAAALSPGT 288
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
24-260 |
1.18e-22 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 94.18 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDyGTKLKQDLARMGVDISHVHTKhGVTAQTqVELHDNDrvfGDYTEGVMADFA 103
Cdd:TIGR03168 35 GGKGINVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVK-GETRIN-VKIKESS---GEETELNEPGPE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 104 LSEEDY--------AWLAQYDIVhaAIWGHA-----EDAFPQL----HAAGKLTAFDFSDKwdsPLWQTLVPH------- 159
Cdd:TIGR03168 109 ISEEELeqlleklrELLASGDIV--VISGSLppgvpPDFYAQLiaiaRKKGAKVILDTSGE---ALREALAAKpflikpn 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 160 ---LDFAFASAPQEDETLRLKMKAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSA 236
Cdd:TIGR03168 184 heeLEELFGRELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLAR 263
|
250 260
....*....|....*....|....
gi 1929626394 237 GMTLPQAIAQGTACAAKTIQYHGA 260
Cdd:TIGR03168 264 GLSLEEALRFAVAAGSAAAFSPGT 287
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
24-259 |
1.83e-21 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 90.67 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDyGTKLKQDLARMGVDISHVHTKhGVTaQTQVELHDNDrvfGDYTEGVMADFA 103
Cdd:cd01164 36 GGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDDFVEVA-GET-RINVKIKEED---GTETEINEPGPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 104 LSEEDY--------AWLAQYDIVhaAIWGH-----AEDAFPQL----HAAGKLTAFDFSDKwdsPLWQTLVPHLDF---- 162
Cdd:cd01164 110 ISEEELealleklkALLKKGDIV--VLSGSlppgvPADFYAELvrlaREKGARVILDTSGE---ALLAALAAKPFLikpn 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 163 -----AFASAPQEDETLRLKM-KAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSA 236
Cdd:cd01164 185 reeleELFGRPLGDEEDVIAAaRKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQ 264
|
250 260
....*....|....*....|...
gi 1929626394 237 GMTLPQAIAQGTACAAKTIQYHG 259
Cdd:cd01164 265 GLSLEEALRLAVAAGSATAFSPG 287
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
24-260 |
1.73e-19 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 84.78 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGvDISHVHTKHGVTAQTQVEL-HDNDRVFGDYTEGVMADF 102
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGG-DKHTVAWRDKPTRKTLSFIdPNGERTITVPGERLEDDL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 103 ALSEedyawLAQYD-------IVHAAIWGH-AEDAFPQLHAAGKLTAFDFSDKWDsplwqtlvpHLDFAFASApqEDETL 174
Cdd:cd01947 115 KWPI-----LDEGDgvfitaaAVDKEAIRKcRETKLVILQVTPRVRVDELNQALI---------PLDILIGSR--LDPGE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 175 RLKMKAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLPQAIAQGTACAAKT 254
Cdd:cd01947 179 LVVAEKIAGPFPRYLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAIC 258
|
....*.
gi 1929626394 255 IQYHGA 260
Cdd:cd01947 259 VSHFGP 264
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
131-260 |
2.13e-19 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 85.33 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 131 PQLHAAGKLTAFDFSDKwdsPLWQTLVPH----------LDFAFASAPQEDETLRLKMKAIVARGAGTVIVTLGENGSIA 200
Cdd:TIGR03828 151 ALAREKGAKVILDTSGE---ALRDGLKAKpflikpndeeLEELFGRELKTLEEIIEAARELLDLGAENVLISLGADGALL 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 201 WDGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLPQAIAQGTACAAKTIQYHGA 260
Cdd:TIGR03828 228 VTKEGALFAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGT 287
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
7-252 |
1.45e-18 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 83.06 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 7 IGDNCVDIYPQLNKAF---SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVH--TKHgVTAQTQ 81
Cdd:PRK09434 8 LGDAVVDLIPEGENRYlkcPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRldPAH-RTSTVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 82 VELHDN-DRVFgdyTEGVM--ADFALSEEDYAWLAQYDIVH-AAIWGHAE-------DAFPQLHAAGKLTAFD---FSDK 147
Cdd:PRK09434 87 VDLDDQgERSF---TFMVRpsADLFLQPQDLPPFRQGEWLHlCSIALSAEpsrsttfEAMRRIKAAGGFVSFDpnlREDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 148 WDSPlwQTLVPHLDFAFASAP----QEDETLRLK--------MKAIVAR-GAGTVIVTLGENGSIAWDGAQFWRQAPEPV 214
Cdd:PRK09434 164 WQDE--AELRECLRQALALADvvklSEEELCFLSgtsqledaIYALADRyPIALLLVTLGAEGVLVHTRGQVQHFPAPSV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1929626394 215 TVIDTMGAGDSFIAGFLCG------WSAGMTLPQAIAQGTACAA 252
Cdd:PRK09434 242 DPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGA 285
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
12-260 |
3.11e-17 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 79.78 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 12 VDIYPQ-----LNKAFS---GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV-HTKHGVTAQTQV 82
Cdd:PTZ00292 32 VDRMPQvgetlHGTSFHkgfGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVsRTENSSTGLAMI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 83 ----ELHDNDRVF-GDYTEGVMADFA-LSEEDYAWLAQYDIVHAAIWGHAE-DAFPQLHAAGKLTAFDFSDKWDSPLWQT 155
Cdd:PTZ00292 112 fvdtKTGNNEIVIiPGANNALTPQMVdAQTDNIQNICKYLICQNEIPLETTlDALKEAKERGCYTVFNPAPAPKLAEVEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 156 LVPHLDFAFASAPQEDETLRLK-------------MKAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEP-VTVIDTMG 221
Cdd:PTZ00292 192 IKPFLKYVSLFCVNEVEAALITgmevtdtesafkaSKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKrVKAVDTTG 271
|
250 260 270
....*....|....*....|....*....|....*....
gi 1929626394 222 AGDSFIAGFLCGWSAGMTLPQAIAQGTACAAKTIQYHGA 260
Cdd:PTZ00292 272 AGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGT 310
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
24-256 |
2.43e-14 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 71.19 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDIsHVHTKHGVTAQTQVELHDNDRV------------- 90
Cdd:cd01941 35 GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV-RGIVFEGRSTASYTAILDKDGDlvvaladmdiyel 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 91 -FGDYTEG----------VMADFALSEEDYAWLAQY-DIVHAAIWGHAEDAFPQLHAAGKLTAFDfsdkwdsplwqTLVP 158
Cdd:cd01941 114 lTPDFLRKirealkeakpIVVDANLPEEALEYLLALaAKHGVPVAFEPTSAPKLKKLFYLLHAID-----------LLTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 159 HLD--FAFASAPQEDETLRLKMKAI-VARGAGTVIVTLGENGSIAWDGAQ---FWR-QAPEPVTVIDTMGAGDSFIAGFL 231
Cdd:cd01941 183 NRAelEALAGALIENNEDENKAAKIlLLPGIKNVIVTLGAKGVLLSSREGgveTKLfPAPQPETVVNVTGAGDAFVAGLV 262
|
250 260
....*....|....*....|....*
gi 1929626394 232 CGWSAGMTLPQAIAQGTACAAKTIQ 256
Cdd:cd01941 263 AGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
24-252 |
5.95e-13 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 67.53 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGnAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVH--------TKHGVTAQTQVELhdndRV-FGDy 94
Cdd:COG2870 56 GG-AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVvdprrpttTKTRVIAGGQQLL----RLdFED- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 95 tegvmaDFALSEED--------YAWLAQYDIV-------HAAIWGHAEDAFPQLHAAGKLTAFDfsDKWDSplWQ----- 154
Cdd:COG2870 130 ------RFPLSAELearllaalEAALPEVDAVilsdygkGVLTPELIQALIALARAAGKPVLVD--PKGRD--FSryrga 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 155 TLV----PHLDFAFASAPQEDETLRLKMKAIVAR-GAGTVIVTLGENG-SIAWDGAQFWRQAPEPVTVIDTMGAGDSFIA 228
Cdd:COG2870 200 TLLtpnlKEAEAAVGIPIADEEELVAAAAELLERlGLEALLVTRGEEGmTLFDADGPPHHLPAQAREVFDVTGAGDTVIA 279
|
250 260
....*....|....*....|....
gi 1929626394 229 GFLCGWSAGMTLPQAIAQGTACAA 252
Cdd:COG2870 280 TLALALAAGASLEEAAELANLAAG 303
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
37-256 |
1.31e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 63.66 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 37 YGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTqVELHDndrVFGDYTE--------GVMADfALSEED 108
Cdd:PLN02379 100 FGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQC-VCLVD---ALGNRTMrpclssavKLQAD-ELTKED 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 109 YA---WL----AQY--DIVHAAI-WGHAEDAFPQLhaagKLTAFDFSDKWDSPLWQTLVP-HLDFAFASAPQEDETLRLK 177
Cdd:PLN02379 175 FKgskWLvlryGFYnlEVIEAAIrLAKQEGLSVSL----DLASFEMVRNFRSPLLQLLESgKIDLCFANEDEARELLRGE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 178 MKA-------IVARGAGTVIVTLGENGSIAWDGAQFWR-QAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLPQAIAQGTA 249
Cdd:PLN02379 251 QESdpeaaleFLAKYCNWAVVTLGSKGCIARHGKEVVRvPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGAC 330
|
....*..
gi 1929626394 250 CAAKTIQ 256
Cdd:PLN02379 331 SGGSVVR 337
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
20-259 |
3.40e-11 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 62.05 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 20 KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDIS--HVHTKHGVTAQTQVElHDNDRVF------ 91
Cdd:cd01944 31 KSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILlpPRGGDDGGCLVALVE-PDGERSFisisga 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 92 -GDYTEGVMADFALSEEDYAWLAQYDIVHAAIWGHAEDAFPQLHAAGKLTAFDFSDKWDS---PLWQTLVP-------HL 160
Cdd:cd01944 110 eQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGTTLVFDPGPRISDipdTILQALMAkrpiwscNR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 161 DFAFASAPQEDETLRLKMKAIVARGAGTVIVTLGENGSIAWDGAQFWRQAP-EPVTVIDTMGAGDSFIAGFLCGWSAGMT 239
Cdd:cd01944 190 EEAAIFAERGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPgFKVKAVDTIGAGDTHAGGMLAGLAKGMS 269
|
250 260
....*....|....*....|
gi 1929626394 240 LPQAIAQGTACAAKTIQYHG 259
Cdd:cd01944 270 LADAVLLANAAAAIVVTRSG 289
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
59-259 |
9.21e-10 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 57.80 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 59 DLARMGVDISHVH-TKHGVTAQTQVELHDNDR----VF-GDYTEGVMADFA-LSEEDYAWL---AQYDIVHAAIWGHAEd 128
Cdd:cd01939 71 DFQSRGIDISHCYrKDIDEPASSYIIRSRAGGrttiVNdNNLPEVTYDDFSkIDLTQYGWIhfeGRNPDETLRMMQHIE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 129 AFPQLHAAGKLT-AFDFsDKWDSPLWQtLVPHLDFAFAS----------APQEdetlRLKMKAIVARGAGTVIVTLGENG 197
Cdd:cd01939 150 EHNNRRPEIRITiSVEV-EKPREELLE-LAAYCDVVFVSkdwaqsrgykSPEE----CLRGEGPRAKKAALLVCTWGDQG 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929626394 198 SIAW--DGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCGWS-AGMTLPQAIAQGTACAAKTIQYHG 259
Cdd:cd01939 224 AGALgpDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNkGPDDLSEALDFGNRVASQKCTGVG 288
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
115-234 |
3.30e-09 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 55.18 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 115 YDIVHAAIWGHA----EDAFPQLHAAGKLTAFDFSDKWDSPLWQTLVPHLDFAFASAPQEDETLRL-------------K 177
Cdd:cd00287 58 ADAVVISGLSPApeavLDALEEARRRGVPVVLDPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALtgrrdlevkeaaeA 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1929626394 178 MKAIVARGAGTVIVTLGENGSIAWDGaQFWRQA--PEPVTVIDTMGAGDSFIAGFLCGW 234
Cdd:cd00287 138 AALLLSKGPKVVIVTLGEKGAIVATR-GGTEVHvpAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
4-251 |
2.24e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 54.45 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 4 LATIGDNCVDIY---PQL-------NKAF---------------SGGNAvNVAVYCTRYGIQPGCITWVGDDDYGTKLKQ 58
Cdd:PLN02341 75 VATLGNLCVDIVlpvPELpppsreeRKAYmeelaasppdkksweAGGNC-NFAIAAARLGLRCSTIGHVGDEIYGKFLLD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 59 DLARMGvdISHV----HTKHGVTAQTQVE------LHDNdrvFGDYTEGVMADFA----------LSEEDYAWLAQYDIV 118
Cdd:PLN02341 154 VLAEEG--ISVVglieGTDAGDSSSASYEtllcwvLVDP---LQRHGFCSRADFGpepafswiskLSAEAKMAIRQSKAL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 119 HAAiwGHAEDAF-PQLHAAGKLTAFD-----FSDKwdSPLWQTLVPH-----------LDFAFASAPQEDE-----TLRL 176
Cdd:PLN02341 229 FCN--GYVFDELsPSAIASAVDYAIDvgtavFFDP--GPRGKSLLVGtpderralehlLRMSDVLLLTSEEaealtGIRN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 177 KMKA---IVARGAGT--VIVTLGENGSI--AWDGAQFwrqAPEP-VTVIDTMGAGDSFIA----GFLCGWSAGMTLPQAI 244
Cdd:PLN02341 305 PILAgqeLLRPGIRTkwVVVKMGSKGSIlvTRSSVSC---APAFkVNVVDTVGCGDSFAAaialGYIHNLPLVNTLTLAN 381
|
....*..
gi 1929626394 245 AQGTACA 251
Cdd:PLN02341 382 AVGAATA 388
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
95-245 |
7.83e-08 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 52.39 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 95 TEGVMAD-----FALSEEDY--------AWLAQYDIVhaAIWGH-----AEDAFP----QLHAAGKLTAFDFSDKW---- 148
Cdd:PRK09513 99 KDGEVTDfnfsgFEVTPADWerfvtdslSWLGQFDMV--AVSGSlprgvSPEAFTdwmtRLRSQCPCIIFDSSREAlvag 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 149 --DSPlWqtLV-PHLD----FAFASAPQEDETLRlKMKAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMG 221
Cdd:PRK09513 177 lkAAP-W--LVkPNRReleiWAGRKLPELKDVIE-AAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVG 252
|
170 180
....*....|....*....|....*...
gi 1929626394 222 AGDSFIA----GFLCGWSAGMTLPQAIA 245
Cdd:PRK09513 253 AGDSMVGgliyGLLMRESSEHTLRLATA 280
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
189-247 |
1.65e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 51.35 E-value: 1.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 189 VIVTLGENGS-IAWDGAQFwRQAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLPQAIAQG 247
Cdd:PLN02630 206 VIVTNGKKGCrIYWKDGEM-RVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLG 264
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
42-260 |
3.78e-07 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 50.41 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 42 GCitwVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELHDNDRVfgdytegVMADFA----LSEEDYAWLAQYDI 117
Cdd:PTZ00247 87 GC---VGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERS-------LVANLGaanhLSAEHMQSHAVQEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 118 VHAAIWGHAEDAF----PQL--------HAAGKLTAFDFS-----DKWDSPLWQtLVPHLDFAFASApQEDETLRLKMK- 179
Cdd:PTZ00247 157 IKTAQLYYLEGFFltvsPNNvlqvakhaRESGKLFCLNLSapfisQFFFERLLQ-VLPYVDILFGNE-EEAKTFAKAMKw 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 180 ------AIVARGAG----------TVIVTLGENGSIAWDGAQFWRQAPEPVT---VIDTMGAGDSFIAGFLCGWSAGMTL 240
Cdd:PTZ00247 235 dtedlkEIAARIAMlpkysgtrprLVVFTQGPEPTLIATKDGVTSVPVPPLDqekIVDTNGAGDAFVGGFLAQYANGKDI 314
|
250 260
....*....|....*....|
gi 1929626394 241 PQAIAQGTACAAKTIQYHGA 260
Cdd:PTZ00247 315 DRCVEAGHYSAQVIIQHNGC 334
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
24-260 |
5.08e-07 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 49.87 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 24 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVT---AQTQVelhdndrvfGDYTEGVM- 99
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGEStgvALIFV---------NDEGENSIg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 100 ----ADFALSEE----DYAWLAQYD------------IVHAAIWGHAEDAFPQLHAAGKltafdfsdkwdSPLWQTLVPH 159
Cdd:PRK11142 110 ihagANAALTPAlveaHRELIANADallmqletpletVLAAAKIAKQHGTKVILNPAPA-----------RELPDELLAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 160 LDFAfasAPQEDETLRL-----------KMKAIV--ARGAGTVIVTLGENGsiAWDGAQ-FWRQAPEP-VTVIDTMGAGD 224
Cdd:PRK11142 179 VDII---TPNETEAEKLtgirveddddaAKAAQVlhQKGIETVLITLGSRG--VWLSENgEGQRVPGFrVQAVDTIAAGD 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 1929626394 225 SFIAGFLCGWSAGMTLPQAIAQGTACAAKTIQYHGA 260
Cdd:PRK11142 254 TFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGA 289
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
20-252 |
9.73e-07 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 48.71 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 20 KAFSGGnAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVH-------------------------TKH 74
Cdd:cd01172 36 EIRLGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVdegrptttktrviarnqqllrvdreDDS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 75 GVTAQTQVELHDNDR---------VFGDYTEGVMADFALSEedyawlaqydiVHAAIWGHAEDAF--PQLHAAGKLTAFD 143
Cdd:cd01172 115 PLSAEEEQRLIERIAerlpeadvvILSDYGKGVLTPRVIEA-----------LIAAARELGIPVLvdPKGRDYSKYRGAT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 144 FsdkwdsplwqtLVPHLD---FAFASAPQEDETLRLKMKAIVAR-GAGTVIVTLGENGSIAWDG-AQFWRQAPEPVTVID 218
Cdd:cd01172 184 L-----------LTPNEKearEALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERdGEVQHIPALAKEVYD 252
|
250 260 270
....*....|....*....|....*....|....
gi 1929626394 219 TMGAGDSFIAGFLCGWSAGMTLPQAIAQGTACAA 252
Cdd:cd01172 253 VTGAGDTVIATLALALAAGADLEEAAFLANAAAG 286
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
185-233 |
2.82e-06 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 47.40 E-value: 2.82e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1929626394 185 GAGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIAGFLCG 233
Cdd:cd01937 183 GVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYS 231
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
16-260 |
8.94e-06 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 46.15 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 16 PQLNKAfSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGV-TAQTQVEL-HDNDRVFGD 93
Cdd:PLN02323 36 PAFKKA-PGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGArTALAFVTLrSDGEREFMF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 94 YtEGVMADFAL--SEEDYAWLAQYDIVHaaiWG------------HAEdAFPQLHAAGKLTAFDFSDK---WDSP----- 151
Cdd:PLN02323 115 Y-RNPSADMLLreSELDLDLIRKAKIFH---YGsislitepcrsaHLA-AMKIAKEAGALLSYDPNLRlplWPSAeaare 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 152 ----LWQTL----VPHLDFAF---ASAPQEDETLRL---KMKAIvargagtvIVTLGENGSIAWDGAQFWRQAPEPVTVI 217
Cdd:PLN02323 190 gimsIWDEAdiikVSDEEVEFltgGDDPDDDTVVKLwhpNLKLL--------LVTEGEEGCRYYTKDFKGRVEGFKVKAV 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1929626394 218 DTMGAGDSFIAGFLCGWSAGMTLPQ-------AIAQGTACAAKTIQYHGA 260
Cdd:PLN02323 262 DTTGAGDAFVGGLLSQLAKDLSLLEdeerlreALRFANACGAITTTERGA 311
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
23-252 |
3.60e-05 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 44.54 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 23 SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQV-------------------- 82
Cdd:PRK09954 92 AGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLaianrqdetvlaindthilq 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 83 ----ELHDNDRVFGDYTEGVMADFALSEEDYAWLAQY--------DIVHAAIWGHAEDAFPQLHAAgKLTAFDFSDKWDS 150
Cdd:PRK09954 172 qltpQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLadeipvfvDTVSEFKAGKIKHWLAHIHTL-KPTQPELEILWGQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 151 PLwqtlvphldfafasapqEDETLRLK-MKAIVARGAGTVIVTLGENGSI--AWDGAQFWRQAPEPvTVIDTMGAGDSFI 227
Cdd:PRK09954 251 AI-----------------TSDADRNAaVNALHQQGVQQIFVYLPDESVFcsEKDGEQFLLTAPAH-TTVDSFGADDGFM 312
|
250 260
....*....|....*....|....*
gi 1929626394 228 AGFLCGWSAGMTLPQAIAQGTACAA 252
Cdd:PRK09954 313 AGLVYSFLEGYSFRDSARFAMACAA 337
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
4-257 |
1.87e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 41.90 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 4 LATIGDNCVDI----YPQLNKAFS---------GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV 70
Cdd:PRK09850 7 VVIIGSANIDVagysHESLNYADSnpgkikftpGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 71 HTKHGVTAQTQVELHDNDR----VFGDY--TEGVMADFALSEEDYAWLAQYDIVHAAIwghAEDAFPQ-LHAAGKLTAF- 142
Cdd:PRK09850 87 LIVPGENTSSYLSLLDNTGemlvAINDMniSNAITAEYLAQHREFIQRAKVIVADCNI---SEEALAWiLDNAANVPVFv 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 143 DFSDKWDSplwQTLVPHLDFAFASAPQ--EDETL-------RLKMKAIVA----RGAGTVIVTLGENGSIAWD--GAQFW 207
Cdd:PRK09850 164 DPVSAWKC---VKVRDRLNQIHTLKPNrlEAETLsgialsgREDVAKVAAwfhqHGLNRLVLSMGGDGVYYSDisGESGW 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1929626394 208 rQAPEPVTVIDTMGAGDSFIAGFLCGWSAGMTLPQAI--AQGTACAAKTIQY 257
Cdd:PRK09850 241 -SAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVrfAQGCSSMALSCEY 291
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
179-256 |
4.39e-04 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 40.91 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 179 KAIVARGAGTVIVTLGENGSIAWDGAQFWRQAPEPV-TVIDTMGAGDSFIAGFL-----CGWSAGMTLPQAIAQGTACAA 252
Cdd:cd01946 188 RLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLeSVFDPTGAGDTFAGGFIgylasQKDTSEANMRRAIIYGSAMAS 267
|
....
gi 1929626394 253 KTIQ 256
Cdd:cd01946 268 FCVE 271
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
169-255 |
5.27e-04 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 40.54 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 169 QEDEtLRLKMKAIVARG-AGTVIVTLGENGSIAWDGAQFWRQAPEPVTVIDTMGAGDSFIagflcgwsAGMTLpqAIAQG 247
Cdd:PRK10294 201 QPDD-VRKAAQELVNSGkAKRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMV--------GAMTL--KLAEN 269
|
....*...
gi 1929626394 248 TACAAKTI 255
Cdd:PRK10294 270 ASLEEMVR 277
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
172-259 |
2.00e-03 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 38.93 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929626394 172 ETLRLKMKAI-VARGAG--TVIVTLGENGSI-AWDGA--QFwrqapePVTVI------DTMGAGDSFIAGFLCGWSAGMT 239
Cdd:PLN02548 229 EEIALKISALpKASGTHkrTVVITQGADPTVvAEDGKvkEF------PVIPLpkeklvDTNGAGDAFVGGFLSQLVQGKD 302
|
90 100
....*....|....*....|
gi 1929626394 240 LPQAIAQGTACAAKTIQYHG 259
Cdd:PLN02548 303 IEECVRAGNYAANVIIQRSG 322
|
|
| |
