|
Name |
Accession |
Description |
Interval |
E-value |
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
1-269 |
6.90e-50 |
|
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: 167.43 E-value: 6.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 1 MIAFMGEALIDLIGSSNSEGQPcFYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMVPKFQDVR 80
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPET-FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 81 ENSMIGFAKLDAKGAATYSFYIDGTtvtvltADEIVEAIEPLATL---RYLHVGSVSIALDSSGEQILSALKRLKARP-F 156
Cdd:cd01167 80 APTTLAFVTLDADGERSFEFYRGPA------ADLLLDTELNPDLLseaDILHFGSIALASEPSRSALLELLEAAKKAGvL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 157 VFFDPNVRPSVIGNFETYRKRVVEVARLASLIKLSHEDLELLFPDSSVKDGISCLLELGASHVVLTKGKDGLQWISKSGl 236
Cdd:cd01167 154 ISFDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGG- 232
|
250 260 270
....*....|....*....|....*....|...
gi 1308505515 237 DIRVPAIDNPIVDTVGAGDTVSGALLTYLEEHD 269
Cdd:cd01167 233 VGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRG 265
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
1-265 |
1.19e-41 |
|
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: 146.18 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 1 MIAFMGEALIDLIGSSNSEGQPC-------FYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMV 73
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGetvlagsFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 74 PKFQDVRENSMIGFAKLDAKGAATYSFY--IDGTtvtvLTADEIVEAIepLATLRYLHVGSVSIALDSSGEQILSALKRL 151
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYrgANAE----LTPEDLDEAL--LAGADILHLGGITLASEPPREALLAALEAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 152 KARP-FVFFDPNVRPSVignFETYRKRVVEVARLASLIKLSHEDLELLFPDSSVKDGISCLLELGASHVVLTKGKDGLQW 230
Cdd:COG0524 155 RAAGvPVSLDPNYRPAL---WEPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1308505515 231 ISKSGLdIRVPAIDNPIVDTVGAGDTVSGALLTYL 265
Cdd:COG0524 232 YTGGEV-VHVPAFPVEVVDTTGAGDAFAAGFLAGL 265
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
1-270 |
4.95e-28 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 109.74 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 1 MIAFMGEALIDLIGssNSEGQP-------CFYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKmv 73
Cdd:pfam00294 1 KVVVIGEANIDLIG--NVEGLPgelvrvsTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 74 PKFQDVRENSMIGFAKLDAKGAATYSFYIDGTTVTVLTADEIVEAIEPLATLRYLHV-GSVSIALDSSGEQILSALKRLK 152
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYIsGSLPLGLPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 153 arpfVFFDPNVRPSVIGNFETYRkrvvEVARLASLIKLSHEDLELLF--PDSSVKDGISCLLEL---GASHVVLTKGKDG 227
Cdd:pfam00294 157 ----GTFDPNLLDPLGAAREALL----ELLPLADLLKPNEEELEALTgaKLDDIEEALAALHKLlakGIKTVIVTLGADG 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1308505515 228 LQWISKSGLDIRVPAIDNPIVDTVGAGDTVSGALLT-YLEEHDI 270
Cdd:pfam00294 229 ALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAgLLAGKSL 272
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
5-270 |
9.35e-23 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 95.77 E-value: 9.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 5 MGEALIDLIgssnSEGQPCFYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMVPKFQDVRENSM 84
Cdd:PRK09434 8 LGDAVVDLI----PEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 85 IGFAKLDAKGAATYSFYIDGTTVTVLTADEIveaiEPLATLRYLHVGSVSIALDSSGEQILSALKRLK-ARPFVFFDPNV 163
Cdd:PRK09434 84 TVVVDLDDQGERSFTFMVRPSADLFLQPQDL----PPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKaAGGFVSFDPNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 164 RPSVIGNFETYRKRVVEVARLASLIKLSHEDLELLFPDSSVKDGISCLL-ELGASHVVLTKGKDG-LQWISKSGLDIRVP 241
Cdd:PRK09434 160 REDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALAdRYPIALLLVTLGAEGvLVHTRGQVQHFPAP 239
|
250 260
....*....|....*....|....*....
gi 1308505515 242 AIDnpIVDTVGAGDTVSGALLTYLEEHDI 270
Cdd:PRK09434 240 SVD--PVDTTGAGDAFVAGLLAGLSQAGL 266
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
41-267 |
7.20e-12 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 64.93 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 41 RLDSDVLYIGKLSSDMFGKQMQEYFSAN--NVKMVpkFQDVRENSMIGFAKLDAKGAAtySFYIDGTTVTVLTADEIVEA 118
Cdd:TIGR02152 43 RLGAEVSMIGKVGDDAFGDELLENLKSNgiDTEYV--GTVKDTPTGTAFITVDDTGEN--RIVVVAGANAELTPEDIDAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 119 IEPLATLRYlhvgsVSIALDSSGEQILSALKRLKARPF-VFFDPnvRPsVIGNFETyrkrvvEVARLASLIKLSHEDLEL 197
Cdd:TIGR02152 119 EALIAESDI-----VLLQLEIPLETVLEAAKIAKKHGVkVILNP--AP-AIKDLDD------ELLSLVDIITPNETEAEI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308505515 198 LFPDS-----SVKDGISCLLELGASHVVLTKGKDGLQWISKSGLDIrVPAIDNPIVDTVGAGDTVSGALLTYLEE 267
Cdd:TIGR02152 185 LTGIEvtdeeDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKL-IPAFKVKAVDTTAAGDTFNGAFAVALAE 258
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
1-269 |
6.90e-50 |
|
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: 167.43 E-value: 6.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 1 MIAFMGEALIDLIGSSNSEGQPcFYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMVPKFQDVR 80
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPET-FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 81 ENSMIGFAKLDAKGAATYSFYIDGTtvtvltADEIVEAIEPLATL---RYLHVGSVSIALDSSGEQILSALKRLKARP-F 156
Cdd:cd01167 80 APTTLAFVTLDADGERSFEFYRGPA------ADLLLDTELNPDLLseaDILHFGSIALASEPSRSALLELLEAAKKAGvL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 157 VFFDPNVRPSVIGNFETYRKRVVEVARLASLIKLSHEDLELLFPDSSVKDGISCLLELGASHVVLTKGKDGLQWISKSGl 236
Cdd:cd01167 154 ISFDPNLRPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGG- 232
|
250 260 270
....*....|....*....|....*....|...
gi 1308505515 237 DIRVPAIDNPIVDTVGAGDTVSGALLTYLEEHD 269
Cdd:cd01167 233 VGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRG 265
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
1-265 |
1.19e-41 |
|
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: 146.18 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 1 MIAFMGEALIDLIGSSNSEGQPC-------FYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMV 73
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGetvlagsFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 74 PKFQDVRENSMIGFAKLDAKGAATYSFY--IDGTtvtvLTADEIVEAIepLATLRYLHVGSVSIALDSSGEQILSALKRL 151
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYrgANAE----LTPEDLDEAL--LAGADILHLGGITLASEPPREALLAALEAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 152 KARP-FVFFDPNVRPSVignFETYRKRVVEVARLASLIKLSHEDLELLFPDSSVKDGISCLLELGASHVVLTKGKDGLQW 230
Cdd:COG0524 155 RAAGvPVSLDPNYRPAL---WEPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1308505515 231 ISKSGLdIRVPAIDNPIVDTVGAGDTVSGALLTYL 265
Cdd:COG0524 232 YTGGEV-VHVPAFPVEVVDTTGAGDAFAAGFLAGL 265
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
1-270 |
4.95e-28 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 109.74 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 1 MIAFMGEALIDLIGssNSEGQP-------CFYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKmv 73
Cdd:pfam00294 1 KVVVIGEANIDLIG--NVEGLPgelvrvsTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 74 PKFQDVRENSMIGFAKLDAKGAATYSFYIDGTTVTVLTADEIVEAIEPLATLRYLHV-GSVSIALDSSGEQILSALKRLK 152
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYIsGSLPLGLPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 153 arpfVFFDPNVRPSVIGNFETYRkrvvEVARLASLIKLSHEDLELLF--PDSSVKDGISCLLEL---GASHVVLTKGKDG 227
Cdd:pfam00294 157 ----GTFDPNLLDPLGAAREALL----ELLPLADLLKPNEEELEALTgaKLDDIEEALAALHKLlakGIKTVIVTLGADG 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1308505515 228 LQWISKSGLDIRVPAIDNPIVDTVGAGDTVSGALLT-YLEEHDI 270
Cdd:pfam00294 229 ALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAgLLAGKSL 272
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
2-270 |
5.72e-26 |
|
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: 104.19 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 2 IAFMGEALIDLIGSSNSEGQPC--FYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNV--KMVPKFQ 77
Cdd:cd01166 2 VVTIGEVMVDLSPPGGGRLEQAdsFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVdtSHVRVDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 78 DVRensmIG--FAKLDAKGAATYSFYIDGTTVTVLTADEIVEAIepLATLRYLHVGSVSIAL-DSSGEQILSALKRLKAR 154
Cdd:cd01166 82 GRP----TGlyFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAA--LAGADHLHLSGITLALsESAREALLEALEAAKAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 155 -PFVFFDPNVRPSvIGNFETYRKRVVEVARLASLIKLSHEDLELLFPDSSVKDGISCLL--ELGASHVVLTKGKDGLQWI 231
Cdd:cd01166 156 gVTVSFDLNYRPK-LWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalALGVKAVVVKLGAEGALVY 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1308505515 232 SKSGLdIRVPAIDNPIVDTVGAGDTVSGALLT-YLEEHDI 270
Cdd:cd01166 235 TGGGR-VFVPAYPVEVVDTTGAGDAFAAGFLAgLLEGWDL 273
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
5-270 |
9.35e-23 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 95.77 E-value: 9.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 5 MGEALIDLIgssnSEGQPCFYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMVPKFQDVRENSM 84
Cdd:PRK09434 8 LGDAVVDLI----PEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 85 IGFAKLDAKGAATYSFYIDGTTVTVLTADEIveaiEPLATLRYLHVGSVSIALDSSGEQILSALKRLK-ARPFVFFDPNV 163
Cdd:PRK09434 84 TVVVDLDDQGERSFTFMVRPSADLFLQPQDL----PPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKaAGGFVSFDPNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 164 RPSVIGNFETYRKRVVEVARLASLIKLSHEDLELLFPDSSVKDGISCLL-ELGASHVVLTKGKDG-LQWISKSGLDIRVP 241
Cdd:PRK09434 160 REDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALAdRYPIALLLVTLGAEGvLVHTRGQVQHFPAP 239
|
250 260
....*....|....*....|....*....
gi 1308505515 242 AIDnpIVDTVGAGDTVSGALLTYLEEHDI 270
Cdd:PRK09434 240 SVD--PVDTTGAGDAFVAGLLAGLSQAGL 266
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
122-265 |
9.10e-13 |
|
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: 65.96 E-value: 9.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 122 LATLRYLHVGSVSIALDSsGEQILSALKRlkARPFVFFDPNVRPSvignfETYRKRVVEVARLASLIKLSHEDLELLF-- 199
Cdd:cd00287 55 LVGADAVVISGLSPAPEA-VLDALEEARR--RGVPVVLDPGPRAV-----RLDGEELEKLLPGVDILTPNEEEAEALTgr 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308505515 200 PDSSVKDGISC---LLELGASHVVLTKGKDGLQWISKSGLDIRVPAIDNPIVDTVGAGDTVSGALLTYL 265
Cdd:cd00287 127 RDLEVKEAAEAaalLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
1-265 |
2.52e-12 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 66.57 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 1 MIAFMGEALIDLI----GSSNSEGqPCFYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMVPKF 76
Cdd:PLN02323 12 LVVCFGEMLIDFVptvsGVSLAEA-PAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 77 QDVRENSMIGFAKLDAKGAATYSFYIDGTTVTVLTADEIveAIEPLATLRYLHVGSVSIALDSSGEQILSALKRLK-ARP 155
Cdd:PLN02323 91 FDPGARTALAFVTLRSDGEREFMFYRNPSADMLLRESEL--DLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKeAGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 156 FVFFDPNVR----PSVignfETYRKRVVEVARLASLIKLSHEDLELLFPDSSVKDGISC-LLELGASHVVLTKGKDGLQW 230
Cdd:PLN02323 169 LLSYDPNLRlplwPSA----EAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPDDDTVVkLWHPNLKLLLVTEGEEGCRY 244
|
250 260 270
....*....|....*....|....*....|....*..
gi 1308505515 231 ISK--SGldiRVPAIDNPIVDTVGAGDTVSGALLTYL 265
Cdd:PLN02323 245 YTKdfKG---RVEGFKVKAVDTTGAGDAFVGGLLSQL 278
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
41-267 |
7.20e-12 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 64.93 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 41 RLDSDVLYIGKLSSDMFGKQMQEYFSAN--NVKMVpkFQDVRENSMIGFAKLDAKGAAtySFYIDGTTVTVLTADEIVEA 118
Cdd:TIGR02152 43 RLGAEVSMIGKVGDDAFGDELLENLKSNgiDTEYV--GTVKDTPTGTAFITVDDTGEN--RIVVVAGANAELTPEDIDAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 119 IEPLATLRYlhvgsVSIALDSSGEQILSALKRLKARPF-VFFDPnvRPsVIGNFETyrkrvvEVARLASLIKLSHEDLEL 197
Cdd:TIGR02152 119 EALIAESDI-----VLLQLEIPLETVLEAAKIAKKHGVkVILNP--AP-AIKDLDD------ELLSLVDIITPNETEAEI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308505515 198 LFPDS-----SVKDGISCLLELGASHVVLTKGKDGLQWISKSGLDIrVPAIDNPIVDTVGAGDTVSGALLTYLEE 267
Cdd:TIGR02152 185 LTGIEvtdeeDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKL-IPAFKVKAVDTTAAGDTFNGAFAVALAE 258
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
41-268 |
4.94e-11 |
|
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: 62.18 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 41 RLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMVPKFQDVRENSMIGFAKLDAKGaatysfyiDGTTVTV------LTADE 114
Cdd:cd01174 48 RLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESG--------ENRIVVVpgangeLTPAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 115 IVEAIEPLATLRYlhvgsVSIALDSSGEQILSALKRLKAR--PFVFfdpNVRPsvignfetYRKRVVEVARLASLIKLSH 192
Cdd:cd01174 120 VDAALELIAAADV-----LLLQLEIPLETVLAALRAARRAgvTVIL---NPAP--------ARPLPAELLALVDILVPNE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 193 EDLELLF--PDSSVKDGIS---CLLELGASHVVLTKGKDGLQWISKSGLdIRVPAIDNPIVDTVGAGDTVSGALLTYLEE 267
Cdd:cd01174 184 TEAALLTgiEVTDEEDAEKaarLLLAKGVKNVIVTLGAKGALLASGGEV-EHVPAFKVKAVDTTGAGDTFIGALAAALAR 262
|
.
gi 1308505515 268 H 268
Cdd:cd01174 263 G 263
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
133-267 |
2.17e-10 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 60.53 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 133 VSIALDSSGEqilsALKR-LKARPFvffdpnvrpsvignfetyrkrvvevarlasLIKLSHEDLELLF--PDSSVKDGIS 209
Cdd:COG1105 159 AKVVLDTSGE----ALKAaLEAGPD------------------------------LIKPNLEELEELLgrPLETLEDIIA 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308505515 210 C---LLELGASHVVLTKGKDGLQWISKSGLdIRVPAIDNPIVDTVGAGDTVSGALLTYLEE 267
Cdd:COG1105 205 AareLLERGAENVVVSLGADGALLVTEDGV-YRAKPPKVEVVSTVGAGDSMVAGFLAGLAR 264
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
125-268 |
2.10e-09 |
|
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: 57.54 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 125 LRYLHVGSVSIALDSSGEQILSAlkrLKARPFvffdpnvrpsvignfetyrkrvvevarlasLIKLSHEDLELLF----- 199
Cdd:cd01164 151 VRLAREKGARVILDTSGEALLAA---LAAKPF------------------------------LIKPNREELEELFgrplg 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308505515 200 PDSSVKDGISCLLELGASHVVLTKGKDGLQWISKSGLdIRVPAIDNPIVDTVGAGDTVSGALLTYLEEH 268
Cdd:cd01164 198 DEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGV-YRASPPKVKVVSTVGAGDSMVAGFVAGLAQG 265
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
128-268 |
2.49e-09 |
|
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: 57.20 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 128 LHVGSVSIALDSSGEQILSALKrlkARPFvffdpnvrpsvignfetyrkrvvevarlasLIKLSHEDLELLF--PDSSVK 205
Cdd:TIGR03168 153 ARKKGAKVILDTSGEALREALA---AKPF------------------------------LIKPNHEELEELFgrELKTLE 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308505515 206 DGISC---LLELGASHVVLTKGKDGLQWISKSGLdIRVPAIDNPIVDTVGAGDTVSGALLTYLEEH 268
Cdd:TIGR03168 200 EIIEAareLLDRGAENVLVSLGADGALLVTKEGA-LKATPPKVEVVNTVGAGDSMVAGFLAGLARG 264
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
128-262 |
4.25e-08 |
|
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: 53.75 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 128 LHVGSVSIALDSSGEQILSALKrlkARPFvffdpnvrpsvignfetyrkrvvevarlasLIKLSHEDLELLF-----PDS 202
Cdd:TIGR03828 153 AREKGAKVILDTSGEALRDGLK---AKPF------------------------------LIKPNDEELEELFgrelkTLE 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 203 SVKDGISCLLELGASHVVLTKGKDGLQWISKSGLdIRVPAIDNPIVDTVGAGDTVSGALL 262
Cdd:TIGR03828 200 EIIEAARELLDLGAENVLISLGADGALLVTKEGA-LFAQPPKGEVVSTVGAGDSMVAGFL 258
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
156-261 |
1.18e-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: 52.18 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 156 FVFFDPNVRpsvigNFETYRKrvvevarlASLIKLSHEDLEL-----LFPDSSVKDGISCLLE-LGASHVVLTKGKDGLQ 229
Cdd:cd01172 166 PVLVDPKGR-----DYSKYRG--------ATLLTPNEKEAREalgdeINDDDELEAAGEKLLElLNLEALLVTLGEEGMT 232
|
90 100 110
....*....|....*....|....*....|..
gi 1308505515 230 WISKSGLDIRVPAIDNPIVDTVGAGDTVSGAL 261
Cdd:cd01172 233 LFERDGEVQHIPALAKEVYDVTGAGDTVIATL 264
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
211-309 |
1.16e-06 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 49.10 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 211 LLELGASHVVLTKGKDGLqWISKSGLDIRVPAIDNPIVDTVGAGDTVSGALLTYLEEhDIGIGDTVTREQatealefaaA 290
Cdd:PRK11142 210 LHQKGIETVLITLGSRGV-WLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTALLE-GKPLPEAIRFAH---------A 278
|
90 100
....*....|....*....|.
gi 1308505515 291 AAAVTTSRKGANP--PRRSEI 309
Cdd:PRK11142 279 AAAIAVTRKGAQPsiPWREEI 299
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
140-261 |
1.20e-06 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 49.42 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 140 SGEQILSALKRLKAR-PFVFFDPNVRpsvigNFETYRKRVV------EVARLASLIKLSHEDLELLfpdssvkdGISCLL 212
Cdd:COG2870 166 TPELIQALIALARAAgKPVLVDPKGR-----DFSRYRGATLltpnlkEAEAAVGIPIADEEELVAA--------AAELLE 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1308505515 213 ELGASHVVLTKGKDGLQWISKSGLDIRVPAIDNPIVDTVGAGDTVSGAL 261
Cdd:COG2870 233 RLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIATL 281
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
125-262 |
2.73e-06 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 48.15 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 125 LRYLHVGSVSIALDSSGEQILSALKrlkARPFVFfDPNVRpsvigNFETYRKRvvEVARLASLIKLSHEdlellfpdssv 204
Cdd:PRK09513 154 MTRLRSQCPCIIFDSSREALVAGLK---AAPWLV-KPNRR-----ELEIWAGR--KLPELKDVIEAAHA----------- 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308505515 205 kdgiscLLELGASHVVLTKGKDGLQWISKSGLDIRVPAIDNpIVDTVGAGDTVSGALL 262
Cdd:PRK09513 212 ------LREQGIAHVVISLGAEGALWVNASGEWIAKPPACD-VVSTVGAGDSMVGGLI 262
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
41-265 |
6.35e-06 |
|
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: 47.03 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 41 RLDSDVLYIGKLSSDMFGKQMQEYFSANNVkmvPKFQDVRENSMIGFAKLDAKGAATYSFyidgttVTVLTADEIVEAiE 120
Cdd:cd01944 47 RLGIPTVNAGPLGNGNWADQIRQAMRDEGI---EILLPPRGGDDGGCLVALVEPDGERSF------ISISGAEQDWST-E 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 121 PLATL-----RYLHVGSVSIALDSSGEQIL-SALKRLKARPFVFFDPNVRPSVIgnfetYRKRVVEVARLASLIKLSHED 194
Cdd:cd01944 117 WFATLtvapyDYVYLSGYTLASENASKVILlEWLEALPAGTTLVFDPGPRISDI-----PDTILQALMAKRPIWSCNREE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308505515 195 LELLFP--DSSVKDGISCLLELGASHVVLTKGKDGLQWISKSGLDIRVPAIDNPIVDTVGAGDTVSGALLTYL 265
Cdd:cd01944 192 AAIFAErgDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGL 264
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
211-269 |
1.85e-05 |
|
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: 45.36 E-value: 1.85e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308505515 211 LLELGASHVVLTKGKDGLQWISKSGLDIRVPAIDNPIVDTVGAGDTVSGALLTYLEEHD 269
Cdd:cd01945 198 LASLGIPFVAVTLGEAGCLWLERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGM 256
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
44-270 |
1.51e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 42.71 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 44 SDVLYIGKLSSDMFGKQMQEYFSANNVKMVPKFQDV------------RENSMIgfAKLDAkgAATYSFyidgttvTVLT 111
Cdd:PTZ00247 81 GFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKaptgtcavlvcgKERSLV--ANLGA--ANHLSA-------EHMQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 112 ADEIVEAIEPlATLRYLHVgsvsIALDSSGEQILSALKrlKAR------------PFV---FFDP--NVRPSV---IGNF 171
Cdd:PTZ00247 150 SHAVQEAIKT-AQLYYLEG----FFLTVSPNNVLQVAK--HAResgklfclnlsaPFIsqfFFERllQVLPYVdilFGNE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 172 EtyrkrvvEVARLASLIKLSHEDLEllfpdsSVKDGISCLLELGASH---VVLTKGKDGLQWISKSGL-DIRVPAID-NP 246
Cdd:PTZ00247 223 E-------EAKTFAKAMKWDTEDLK------EIAARIAMLPKYSGTRprlVVFTQGPEPTLIATKDGVtSVPVPPLDqEK 289
|
250 260
....*....|....*....|....*
gi 1308505515 247 IVDTVGAGDT-VSGALLTYLEEHDI 270
Cdd:PTZ00247 290 IVDTNGAGDAfVGGFLAQYANGKDI 314
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
41-265 |
2.16e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 42.42 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 41 RLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMvpKFQDVRENSMIGFAKL--DAKGAATYSFYIDGTTvtvltaDEIVEA 118
Cdd:PTZ00292 64 KLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT--SFVSRTENSSTGLAMIfvDTKTGNNEIVIIPGAN------NALTPQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 119 IEPLATLRYLHVGSVSIA-LDSSGEQILSALKRLKARPF--VFfdpNVRPSVigNFETYRKrVVEVARLASLIKLSHEDL 195
Cdd:PTZ00292 136 MVDAQTDNIQNICKYLICqNEIPLETTLDALKEAKERGCytVF---NPAPAP--KLAEVEI-IKPFLKYVSLFCVNEVEA 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308505515 196 ELLF-----PDSSVKDGISCLLELGASHVVLTKGKDGLQWISKSGLDIRVPAIDNPIVDTVGAGDTVSGALLTYL 265
Cdd:PTZ00292 210 ALITgmevtDTESAFKASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFM 284
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
157-277 |
1.40e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 40.20 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 157 VFFDPNVRPSVIGNFETYRKRVVEVA-RLASLIKLSHEDLELLFPDSSVKDGISCLLE--LGASHVVLTKGKDGLQWISK 233
Cdd:PLN02341 257 VFFDPGPRGKSLLVGTPDERRALEHLlRMSDVLLLTSEEAEALTGIRNPILAGQELLRpgIRTKWVVVKMGSKGSILVTR 336
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1308505515 234 SGLDiRVPAIDNPIVDTVGAGDTVSGAL-LTYLeeHDIGIGDTVT 277
Cdd:PLN02341 337 SSVS-CAPAFKVNVVDTVGCGDSFAAAIaLGYI--HNLPLVNTLT 378
|
|
| PLN02967 |
PLN02967 |
kinase |
24-198 |
6.48e-03 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 38.10 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 24 FYYYSGGCALNAATAAARLDSDVLYIGKLSSDMFGKQMQEYFSANNVKMVPKFQDVRENSMIGFAKLDAKGAATYSFyID 103
Cdd:PLN02967 238 FVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTC-VK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308505515 104 GTTVTVLTADEIVEAIEPLATLRYLHVGS-VSIALDSSGEQILSALKRLKArpFVFFDPNVRPSVIGNFETYRKRVVEVA 182
Cdd:PLN02967 317 PCAEDSLSKSEINIDVLKEAKMFYFNTHSlLDPTMRSTTLRAIKISKKLGG--VIFYDLNLPLPLWSSSEETKSFIQEAW 394
|
170
....*....|....*.
gi 1308505515 183 RLASLIKLSHEDLELL 198
Cdd:PLN02967 395 NLADIIEVTKQELEFL 410
|
|
|