|
Name |
Accession |
Description |
Interval |
E-value |
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
101-389 |
3.66e-55 |
|
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: 185.47 E-value: 3.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 101 DVLLSGTVFFDIVFTGmDRLPRPGEELWSKGMGSSPGG-IANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGID 179
Cdd:COG0524 1 DVLVIGEALVDLVARV-DRLPKGGETVLAGSFRRSPGGaAANVAVALARLGARVALVGAVGDDPFGDFLLAELR-AEGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 180 LSASRRFTDFHSALT-VSIAAEGDRAMATHG--------HDLPEP---------LSTLIAGAPDARAAVVDLAgetswwA 241
Cdd:COG0524 79 TSGVRRDPGAPTGLAfILVDPDGERTIVFYRganaeltpEDLDEAllagadilhLGGITLASEPPREALLAAL------E 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 242 QLAQRGSLIFADIGFDAtERWNIA--DLAPLV-HCHAFTPNALEAMAYTRTDTPDRAVRALAEM-VPLAVVTDGADGSYA 317
Cdd:COG0524 153 AARAAGVPVSLDPNYRP-ALWEPAreLLRELLaLVDILFPNEEEAELLTGETDPEEAAAALLARgVKLVVVTLGAEGALL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256558122 318 IDGstGEEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFGGSLAAPGWGDI 389
Cdd:COG0524 232 YTG--GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
101-380 |
9.38e-49 |
|
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: 167.87 E-value: 9.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 101 DVLLSGTVFFDIVFTGMdRLPRPGEE-LWSKGMGSSPGGIANLATAAARLGLRTGLVAGFGDDAYADWMWHtMAHEEGID 179
Cdd:cd01942 1 DVAVVGHLNYDIILKVE-SFPGPFESvLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLE-ELREEGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 180 LSASRRFTDFHSALTVSIAaEGDRAMATHGHdlPEPLSTL---IAGAPDARAAVVDLAGETS--WWAQLAQRGsliFADI 254
Cdd:cd01942 79 TSHVRVVDEDSTGVAFILT-DGDDNQIAYFY--PGAMDELepnDEADPDGLADIVHLSSGPGliELARELAAG---GITV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 255 GFD---ATERWNIADLAP-LVHCHAFTPNALEAMA-YTRTDTPDRAvraLAEMVPLAVVTDGADGSYAIDGstGEEAFCP 329
Cdd:cd01942 153 SFDpgqELPRLSGEELEEiLERADILFVNDYEAELlKERTGLSEAE---LASGVRVVVVTLGPKGAIVFED--GEEVEVP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 256558122 330 AVPVT-AIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFGGS 380
Cdd:cd01942 228 AVPAVkVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
111-384 |
3.38e-29 |
|
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: 115.72 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 111 DIVFTgMDRLPRPGEELWSKGMGSSPGGI-ANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGIDLSASRRFTDF 189
Cdd:cd01174 11 DLVTR-VDRLPKPGETVLGSSFETGPGGKgANQAVAAARLGARVAMIGAVGDDAFGDELLENLR-EEGIDVSYVEVVVGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 190 HSAL-TVSIAAEGDR-------AMATHGHDLPEPLSTLIAGApdaraAVVDLAGETSWWA-----QLAQRGSLIF----A 252
Cdd:cd01174 89 PTGTaVITVDESGENrivvvpgANGELTPADVDAALELIAAA-----DVLLLQLEIPLETvlaalRAARRAGVTVilnpA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 253 DIGFDATERWNIADLaplvhchaFTPNALEA-----MAYTRTDTPDRAVRALAEM-VPLAVVTDGADGSYAIDGstGEEA 326
Cdd:cd01174 164 PARPLPAELLALVDI--------LVPNETEAalltgIEVTDEEDAEKAARLLLAKgVKNVIVTLGAKGALLASG--GEVE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 256558122 327 FCPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFGGSLAAP 384
Cdd:cd01174 234 HVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIP 291
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
111-378 |
4.06e-26 |
|
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: 107.30 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 111 DIVFTgMDRLPRPGEELWSKGMGSSPGGI-ANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGIDLSASRRFTDF 189
Cdd:TIGR02152 6 DLVLR-TDRLPKPGETVHGHSFQIGPGGKgANQAVAAARLGAEVSMIGKVGDDAFGDELLENLK-SNGIDTEYVGTVKDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 190 HSAL-TVSIAAEGDRAMAthghdlpeplstLIAGAPDA-RAAVVDLAgetswWAQLAQrGSLIFA--DIGFDATERwnIA 265
Cdd:TIGR02152 84 PTGTaFITVDDTGENRIV------------VVAGANAElTPEDIDAA-----EALIAE-SDIVLLqlEIPLETVLE--AA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 266 DL------------AP---------LVHCHAFTPNALEAMAYTRT-----DTPDRAVRALAEMVPLAV-VTDGADGSYAI 318
Cdd:TIGR02152 144 KIakkhgvkvilnpAPaikdlddelLSLVDIITPNETEAEILTGIevtdeEDAEKAAEKLLEKGVKNViITLGSKGALLV 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 319 DGstGEEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:TIGR02152 224 SK--DESKLIPAFKVKAVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKG 281
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
101-385 |
5.33e-25 |
|
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: 103.91 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 101 DVLLSGTVFFDIVFTgMDRLPRPGEELWSKGMGSSPGGIA-NLATAAARLGLRTGLVAGFGDDAYADWMWHtMAHEEGID 179
Cdd:cd01945 1 RVLGVGLAVLDLIYL-VASFPGGDGKIVATDYAVIGGGNAaNAAVAVARLGGQARLIGVVGDDAIGRLILA-ELAAEGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 180 LSASRRFTDFHSALTVSIAAEGDRAMA--THGHDLPEPLSTLIAGAPDARAAVVD---LAGETSWWAQLAQRGSLIFADI 254
Cdd:cd01945 79 TSFIVVAPGARSPISSITDITGDRATIsiTAIDTQAAPDSLPDAILGGADAVLVDgrqPEAALHLAQEARARGIPIPLDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 255 GFDATERwnIADLAPLVHCHAFTPNALEAMAYTRTDTpdrAVRALAEM-VPLAVVTDGADGSYAIDgSTGEEAFCPAVPV 333
Cdd:cd01945 159 DGGGLRV--LEELLPLADHAICSENFLRPNTGSADDE---ALELLASLgIPFVAVTLGEAGCLWLE-RDGELFHVPAFPV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 256558122 334 TAIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFGGSLAAPG 385
Cdd:cd01945 233 EVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
135-381 |
2.28e-24 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 102.42 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 135 SPGGI-ANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGIDLSASRRFTDFHSAL-TVSIAAEGDRAMATHG--- 209
Cdd:pfam00294 32 GPGGKgANVAVALARLGGDVAFIGAVGDDNFGEFLLQELK-KEGVDTDYVVIDEDTRTGTaLIEVDGDGERTIVFNRgaa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 210 -----HDLPEPLSTLIAGAPDARAAVVDLAGETSWWAQLAQRGSLI-FADIGFDATeRWNIAD--LAPLVHCHAFTPNA- 280
Cdd:pfam00294 111 adltpEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGgTFDPNLLDP-LGAAREalLELLPLADLLKPNEe 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 281 -LEAMAYTRTDTPDRAVRALAEM----VPLAVVTDGADGSYAIDGstGEEAFCPAVP-VTAIDTTGAGDVFAAAMVLGTL 354
Cdd:pfam00294 190 eLEALTGAKLDDIEEALAALHKLlakgIKTVIVTLGADGALVVEG--DGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLL 267
|
250 260
....*....|....*....|....*..
gi 256558122 355 ASWPLEERLRFGSLCSALAVQQFGGSL 381
Cdd:pfam00294 268 AGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
102-378 |
2.00e-23 |
|
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: 99.63 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 102 VLLSGTVFFDIVFTGmdrlpRPGEELWSKGMGSSPggiANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGIDLS 181
Cdd:cd01167 2 VVCFGEALIDFIPEG-----SGAPETFTKAPGGAP---ANVAVALARLGGKAAFIGKVGDDEFGDFLLETLK-EAGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 182 ASRRFTDFHSAL-TVSIAAEGDRAMATHG------HDLPEPLSTLIAGA------------PDARAAVVDLAgetswwAQ 242
Cdd:cd01167 73 GIQFDPAAPTTLaFVTLDADGERSFEFYRgpaadlLLDTELNPDLLSEAdilhfgsialasEPSRSALLELL------EA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 243 LAQRGSLIFADI-------GFDATERWNIADLAPLVHchaFTPNALEAMAY-TRTDTPDRAVRALAEM-VPLAVVTDGAD 313
Cdd:cd01167 147 AKKAGVLISFDPnlrpplwRDEEEARERIAELLELAD---IVKLSDEELELlFGEEDPEEIAALLLLFgLKLVLVTRGAD 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256558122 314 GSYAIDGstGEEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLASW-------PLEERLRFGSLCSALAVQQFG 378
Cdd:cd01167 224 GALLYTK--GGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSRGllaldedELAEALRFANAVGALTCTKAG 293
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
137-378 |
6.67e-23 |
|
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: 98.03 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 137 GGIANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGIDLSASRRFTDFHSALT-VSIAAEGDR----------AM 205
Cdd:cd01166 32 GAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELR-REGVDTSHVRVDPGRPTGLYfLEIGAGGERrvlyyragsaAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 206 ATHGHDLPEplsTLIAGA-------------PDARAAVVDLAgetswwAQLAQRGSLIFADIGFDAtERWNIADLAP--- 269
Cdd:cd01166 111 RLTPEDLDE---AALAGAdhlhlsgitlalsESAREALLEAL------EAAKARGVTVSFDLNYRP-KLWSAEEAREale 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 270 --LVHCHAFTPNALEAMA---YTRTDTPDRAVRALAEMVPLAVVTDGADGSYAIDGstGEEAFCPAVPVTAIDTTGAGDV 344
Cdd:cd01166 181 elLPYVDIVLPSEEEAEAllgDEDPTDAAERALALALGVKAVVVKLGAEGALVYTG--GGRVFVPAYPVEVVDTTGAGDA 258
|
250 260 270
....*....|....*....|....*....|....
gi 256558122 345 FAAAMVLGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:cd01166 259 FAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
135-375 |
1.51e-20 |
|
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: 91.22 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 135 SPGGIA-NLATAAARLGLRTGLVAGFGDDAYADwMWHTMAHEEGIDlsasRRFTDFHSALTVS----IAAEGDRAMATHG 209
Cdd:cd01941 33 SPGGVGrNIAENLARLGVSVALLSAVGDDSEGE-SILEESEKAGLN----VRGIVFEGRSTASytaiLDKDGDLVVALAD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 210 HDL-----PEPLSTLIAGAPDARAAVVD--LAGET-SWWAQLAQrgsLIFADIGFDATERWNIADLAPLVH-CHAFTPNA 280
Cdd:cd01941 108 MDIyelltPDFLRKIREALKEAKPIVVDanLPEEAlEYLLALAA---KHGVPVAFEPTSAPKLKKLFYLLHaIDLLTPNR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 281 LEAMAYTR------TDTPDRAVRALAEMVPLAVVTDGADGSYAIDGSTGEEA--FCPAVPVTAIDTTGAGDVFAAAMVLG 352
Cdd:cd01941 185 AELEALAGaliennEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVETklFPAPQPETVVNVTGAGDAFVAGLVAG 264
|
250 260
....*....|....*....|...
gi 256558122 353 TLASWPLEERLRFGSLCSALAVQ 375
Cdd:cd01941 265 LLEGMSLDDSLRFAQAAAALTLE 287
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
135-381 |
1.82e-20 |
|
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: 91.52 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 135 SPGG-IANLATAAARLGLRTGLVAGFGDDAYADwMWHTMAHEEGIDLSASRRFTDFHSALTVSIAAEGDRAMATHGhDLP 213
Cdd:cd01168 53 IAGGsAANTIRGAAALGGSAAFIGRVGDDKLGD-FLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYL-GAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 214 EPLS-TLIAGAPDARAAVVDLAGETswW----------AQLAQRGSLIFAD-------IGFDATERWNIADLAPLVHCha 275
Cdd:cd01168 131 NELSpDDLDWSLLAKAKYLYLEGYL--LtvppeaillaAEHAKENGVKIALnlsapfiVQRFKEALLELLPYVDILFG-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 276 ftpNALEAMAYTR---TDTPDRAVRALAEMVPLAVVTDGADGSYAIDGstGEEAFCPAVP-VTAIDTTGAGDVFAAAMVL 351
Cdd:cd01168 207 ---NEEEAEALAEaetTDDLEAALKLLALRCRIVVITQGAKGAVVVEG--GEVYPVPAIPvEKIVDTNGAGDAFAGGFLY 281
|
250 260 270
....*....|....*....|....*....|
gi 256558122 352 GTLASWPLEERLRFGSLCSALAVQQFGGSL 381
Cdd:cd01168 282 GLVQGEPLEECIRLGSYAAAEVIQQLGPRL 311
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
102-378 |
2.01e-18 |
|
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: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 102 VLLSGTVFFDIVFTGmDRLPRPGEELWSKGMGSSPGGI-ANLATAAARLGLRTGLVAGFGDDAYADWMWHTMahEEGIDL 180
Cdd:cd01947 2 IAVVGHVEWDIFLSL-DAPPQPGGISHSSDSRESPGGGgANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEEL--ESGGDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 181 SASRRFTDFHSALTVSIAAEGDRAMATHGHDLPEPLSTLIAGAPDArAAVVDLAGETSWWAQLAQRGSLIFA---DIGFD 257
Cdd:cd01947 79 HTVAWRDKPTRKTLSFIDPNGERTITVPGERLEDDLKWPILDEGDG-VFITAAAVDKEAIRKCRETKLVILQvtpRVRVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 258 ATERWNIadlaplvHCHAFTPNALEAmaytrtDTPDRAVRALAEMVPLAVVTDGADGSYAIDGstGEEAFCPAVPVTAID 337
Cdd:cd01947 158 ELNQALI-------PLDILIGSRLDP------GELVVAEKIAGPFPRYLIVTEGELGAILYPG--GRYNHVPAKKAKVPD 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 256558122 338 TTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:cd01947 223 STGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
136-378 |
3.35e-16 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 78.24 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 136 PGGIA-NLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGIDLSaSRRFTDFHSALTVSIAAEGDRamaTHGHDLPE 214
Cdd:PRK09813 22 SGGNAvNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLA-RMGVDIS-HVHTKHGVTAQTQVELHDNDR---VFGDYTEG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 215 PLSTLIAGAPDAR-AAVVDLAGETSW------WAQLAQRGSLIfadiGFDATERWNiadlAPLVHchAFTPNALEAMAYT 287
Cdd:PRK09813 97 VMADFALSEEDYAwLAQYDIVHAAIWghaedaFPQLHAAGKLT----AFDFSDKWD----SPLWQ--TLVPHLDYAFASA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 288 RTDTP---DRAVRALAEMVPLAVVTDGADGSYAIDGSTGEEAfcPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLEERLR 364
Cdd:PRK09813 167 PQEDEflrLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQ--APEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMA 244
|
250
....*....|....
gi 256558122 365 FGSLCSALAVQQFG 378
Cdd:PRK09813 245 QGTACAAKTIQYHG 258
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
101-384 |
5.12e-15 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 75.54 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 101 DVLLSGTVFFDIvFTGMDRLPRPGEELWSKGMGSSPGGI-ANLATAAARLGLRTGLVAGFGDDAYADwmwHTMAH--EEG 177
Cdd:PTZ00292 17 DVVVVGSSNTDL-IGYVDRMPQVGETLHGTSFHKGFGGKgANQAVMASKLGAKVAMVGMVGTDGFGS---DTIKNfkRNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 178 IDLSASRRFTDFHSALtvsiaaegdrAMATHGHDLPEPLSTLIAGAPDA-RAAVVDLAgetswWAQLAQRGSLIFA--DI 254
Cdd:PTZ00292 93 VNTSFVSRTENSSTGL----------AMIFVDTKTGNNEIVIIPGANNAlTPQMVDAQ-----TDNIQNICKYLICqnEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 255 GFDAT--------ER-----WNIA------------DLAPLVHchAFTPNALEA-----MAYTRTDTPDRAVRALAEM-V 303
Cdd:PTZ00292 158 PLETTldalkeakERgcytvFNPApapklaeveiikPFLKYVS--LFCVNEVEAalitgMEVTDTESAFKASKELQQLgV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 304 PLAVVTDGADGsYAIDGSTGEEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFGGSLAA 383
Cdd:PTZ00292 236 ENVIITLGANG-CLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSY 314
|
.
gi 256558122 384 P 384
Cdd:PTZ00292 315 P 315
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
278-384 |
7.96e-15 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 74.79 E-value: 7.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 278 PNALEAMAYTRTDTPDR-----AVRALAEM-VPLAVVTDGADGSYAIdgsTGEEAF-CPAVPVTAIDTTGAGDVFAAAMV 350
Cdd:COG1105 183 PNLEELEELLGRPLETLediiaAARELLERgAENVVVSLGADGALLV---TEDGVYrAKPPKVEVVSTVGAGDSMVAGFL 259
|
90 100 110
....*....|....*....|....*....|....
gi 256558122 351 LGTLASWPLEERLRFGSLCSALAVQQFGGSLAAP 384
Cdd:COG1105 260 AGLARGLDLEEALRLAVAAGAAAALSPGTGLPDR 293
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
102-354 |
6.25e-14 |
|
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: 70.20 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 102 VLLSGTVFFDIVFTGMDRLPRPGEELWSKGMGSSPGGIANLATAAARLGLRTGLVAgfgddayADWMwhtmaheegidls 181
Cdd:cd00287 2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG-------ADAV------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 182 asrrftdfhsaltvsiaaegdramathghdlpeplstLIAGAPDARAAVVDLAgetswwAQLAQRGSLIFADIGFDATER 261
Cdd:cd00287 62 -------------------------------------VISGLSPAPEAVLDAL------EEARRRGVPVVLDPGPRAVRL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 262 WNIADLAPLVHCHAFTPNALEAMAYTRTDTPD------RAVRALAEMVPLAVVTDGADGSYAIDgSTGEEAFCPAVPVTA 335
Cdd:cd00287 99 DGEELEKLLPGVDILTPNEEEAEALTGRRDLEvkeaaeAAALLLSKGPKVVIVTLGEKGAIVAT-RGGTEVHVPAFPVKV 177
|
250
....*....|....*....
gi 256558122 336 IDTTGAGDVFAAAMVLGTL 354
Cdd:cd00287 178 VDTTGAGDAFLAALAAGLA 196
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
279-381 |
2.66e-12 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 68.30 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 279 NALEAMA---YTRTDTPDRAVRALAEMVPLAVVTDGADGSYAidGSTGEEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLA 355
Cdd:PLN02813 289 NSDEARAlcgLGSEESPESATRYLSHFCPLVSVTDGARGSYI--GVKGEAVYIPPSPCVPVDTCGAGDAYAAGILYGLLR 366
|
90 100
....*....|....*....|....*..
gi 256558122 356 SWP-LEERLRFGSLCSALAVQQFGGSL 381
Cdd:PLN02813 367 GVSdLRGMGELAARVAATVVGQQGTRL 393
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
278-378 |
2.68e-12 |
|
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: 67.17 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 278 PNA--LEAMAYTRTDTPD---RAVRALAEM-VPLAVVTDGADGSYAIdgsTGEEA-FCPAVPVTAIDTTGAGDVFAAAMV 350
Cdd:cd01164 183 PNReeLEELFGRPLGDEEdviAAARKLIERgAENVLVSLGADGALLV---TKDGVyRASPPKVKVVSTVGAGDSMVAGFV 259
|
90 100
....*....|....*....|....*...
gi 256558122 351 LGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:cd01164 260 AGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
102-378 |
2.79e-12 |
|
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: 67.06 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 102 VLLSGTVFFDIVFTgMDRLPRPGEELWSKGMGSSPGGIANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGIDLS 181
Cdd:cd01944 2 VLVIGAAVVDIVLD-VDKLPASGGDIEAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMR-DEGIEIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 182 ASRRFTDFHSALTVSIAAEGDRAMAT----HGHDLPEPLSTLIAGAPDaraaVVDLAGET------------SWWAQLAQ 245
Cdd:cd01944 80 LPPRGGDDGGCLVALVEPDGERSFISisgaEQDWSTEWFATLTVAPYD----YVYLSGYTlasenaskvillEWLEALPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 246 RGSLIFaDIG-----FDATERWNIADLAPLVHChaftpNALEAMAYTRTDTPDRAVRALAEMVPLA---VVTDGADGSYa 317
Cdd:cd01944 156 GTTLVF-DPGprisdIPDTILQALMAKRPIWSC-----NREEAAIFAERGDPAAEASALRIYAKTAapvVVRLGSNGAW- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256558122 318 IDGSTGEEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:cd01944 229 IRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
136-379 |
6.37e-12 |
|
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: 65.45 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 136 PGGIA-NLATAAARLGLRTGLVAGFGDDAYADWMWHTMaHEEGIDLSASRrFTDFHSALTVSIAAEGDR--------AMA 206
Cdd:cd01940 21 PGGNAlNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTL-KRLGVDISHCR-VKEGENAVADVELVDGDRifglsnkgGVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 207 THgHDLPEPLSTLiagapdaRAAVVDLAGETSWWAQLAQRGSLIFAD---IGFDATERWNIADLAPLVhchaftpNALEA 283
Cdd:cd01940 99 RE-HPFEADLEYL-------SQFDLVHTGIYSHEGHLEKALQALVGAgalISFDFSDRWDDDYLQLVC-------PYVDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 284 MAYTRTDTPDRAVRAL-----AEMVPLAVVTDGADGSYAIDGSTGEEAfcPAVPVTAIDTTGAGDVFAAAMVLGTLAS-W 357
Cdd:cd01940 164 AFFSASDLSDEEVKAKlkeavSRGAKLVIVTRGEDGAIAYDGAVFYSV--APRPVEVVDTLGAGDSFIAGFLLSLLAGgT 241
|
250 260
....*....|....*....|..
gi 256558122 358 PLEERLRFGSLCSALAVQQFGG 379
Cdd:cd01940 242 AIAEAMRQGAQFAAKTCGHEGA 263
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
54-363 |
2.08e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 65.62 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 54 ATPGDAAPAVPRGEQPAGASTPAPpEAAECQDWdplaAQRAAADPPLDVLLSGTVFFDIVFTgMDRLPRPGEELWSKGMG 133
Cdd:PLN02341 32 RRVCSRCRASARASSRARAGARSR-ARRRLGDT----EVGSAAGKEIDVATLGNLCVDIVLP-VPELPPPSREERKAYME 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 134 S---SP--------GGIANLATAAARLGLRTGLVAGFGDDAYADWMWHTMaHEEGIDLSASRRFTDfhsaltvsIAAEGD 202
Cdd:PLN02341 106 ElaaSPpdkksweaGGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVL-AEEGISVVGLIEGTD--------AGDSSS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 203 RAMAT------------HG----HDL-PEPL----STLIAGA---------------------PDARAAVVDLAGETsww 240
Cdd:PLN02341 177 ASYETllcwvlvdplqrHGfcsrADFgPEPAfswiSKLSAEAkmairqskalfcngyvfdelsPSAIASAVDYAIDV--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 241 aqlaqrGSLIFADIG------FDATErwniADLAPLVHCHAFTPNAL----EAMAYTRTDTPDRAVRAL------AEMVp 304
Cdd:PLN02341 254 ------GTAVFFDPGprgkslLVGTP----DERRALEHLLRMSDVLLltseEAEALTGIRNPILAGQELlrpgirTKWV- 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 256558122 305 laVVTDGADGSYAIDGSTGEEAFCPAVPVtaIDTTGAGDVFAAAMVLGTLASWPLEERL 363
Cdd:PLN02341 323 --VVKMGSKGSILVTRSSVSCAPAFKVNV--VDTVGCGDSFAAAIALGYIHNLPLVNTL 377
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
120-378 |
3.92e-11 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 63.74 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 120 LPRPGEELWSKGMGSSPGGI-ANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAhEEGIDLSASRR-----------FT 187
Cdd:PRK11142 22 FPRPGETLTGRHYQVAFGGKgANQAVAAARLGADIAFIACVGDDSIGESMRQQLA-KDGIDTAPVSVikgestgvaliFV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 188 DFHSALTVSIAAEGDRAM---ATHGH------------DLPEPLSTLIAGAPDARAA----VVDLAGETSWWAQLaqrgs 248
Cdd:PRK11142 101 NDEGENSIGIHAGANAALtpaLVEAHrelianadallmQLETPLETVLAAAKIAKQHgtkvILNPAPARELPDEL----- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 249 LIFADIgfdaterwniadlaplvhchaFTPNALEAMAYT-----RTDTPDRAVRALAEMVPLAVV-TDGADGSYAidGST 322
Cdd:PRK11142 176 LALVDI---------------------ITPNETEAEKLTgirveDDDDAAKAAQVLHQKGIETVLiTLGSRGVWL--SEN 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 256558122 323 GEEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:PRK11142 233 GEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKG 288
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
272-378 |
7.65e-10 |
|
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: 59.88 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 272 HCHAFTPNALEAMAYTRTDTPDR-----AVRALAEMVPLA--VVTDGADGSYAIDGSTGEEAFcPAVPVTAIDTTGAGDV 344
Cdd:cd01172 181 GATLLTPNEKEAREALGDEINDDdeleaAGEKLLELLNLEalLVTLGEEGMTLFERDGEVQHI-PALAKEVYDVTGAGDT 259
|
90 100 110
....*....|....*....|....*....|....
gi 256558122 345 FAAAMVLGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:cd01172 260 VIATLALALAAGADLEEAAFLANAAAGVVVGKVG 293
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
137-386 |
1.56e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 59.42 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 137 GGIAN-LATAAARLGLRTGLVAGFGDDAYADWMWHTMAHEeGIDLSASRRFTDfHSALTVSIA-AEGDRAMAthghdlPE 214
Cdd:PLN02379 87 GSVANtIRGLSAGFGVSTGIIGACGDDEQGKLFVSNMGFS-GVDLSRLRAKKG-PTAQCVCLVdALGNRTMR------PC 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 215 PLSTLIAGAPDARAAvvDLAGetSWWAQL--AQRG-SLIFADIGFDATERWNIA-DLA----------PLVH-------- 272
Cdd:PLN02379 159 LSSAVKLQADELTKE--DFKG--SKWLVLryGFYNlEVIEAAIRLAKQEGLSVSlDLAsfemvrnfrsPLLQllesgkid 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 273 -CHAFTPNALEAMAYTRTDTPDRAVRALAEMVPLAVVTDGADGSYAIDGStgEEAFCPAV-PVTAIDTTGAGDVFAAAMV 350
Cdd:PLN02379 235 lCFANEDEARELLRGEQESDPEAALEFLAKYCNWAVVTLGSKGCIARHGK--EVVRVPAIgETNAVDATGAGDLFASGFL 312
|
250 260 270
....*....|....*....|....*....|....*.
gi 256558122 351 LGTLASWPLEERLRFGSLCSALAVQQFGGSLAAPGW 386
Cdd:PLN02379 313 YGLIKGLSLEECCKVGACSGGSVVRALGGEVTPENW 348
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
287-384 |
4.78e-08 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 54.17 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 287 TRTDTPDRAVRALAEM--VPLAVVTDGADGSYAIDGstGEEAFCPAVPVTAIDTTGAGDVFAAAMvLGTLAS---WP--- 358
Cdd:PRK09434 195 SGTSQLEDAIYALADRypIALLLVTLGAEGVLVHTR--GQVQHFPAPSVDPVDTTGAGDAFVAGL-LAGLSQaglWTdea 271
|
90 100
....*....|....*....|....*..
gi 256558122 359 -LEERLRFGSLCSALAVQQFGGSLAAP 384
Cdd:PRK09434 272 eLAEIIAQAQACGALATTAKGAMTALP 298
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
135-374 |
9.86e-07 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 50.37 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 135 SPGGIA-NLATAAARLGLRTGLVAGFGDDAYADWMWhTMAHEEGIDL-----------SASRRFTDFHSALTVSIaaegd 202
Cdd:PRK09850 38 TPGGVGrNIAQNLALLGNKAWLLSAVGSDFYGQSLL-TQTNQSGVYVdkclivpgentSSYLSLLDNTGEMLVAI----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 203 RAMATHGHDLPEPLSTLIAGAPDARAAVVD--LAGETSWWAqLAQRGSlifADIGFDATERWNIADLAP-LVHCHAFTPN 279
Cdd:PRK09850 112 NDMNISNAITAEYLAQHREFIQRAKVIVADcnISEEALAWI-LDNAAN---VPVFVDPVSAWKCVKVRDrLNQIHTLKPN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 280 ALEAMAYT------RTDTPDRAVRALAEMVPLAVVTDGADGSYAIDGStGEEAFCPAVPVTAIDTTGAGDVfaaaMVLGT 353
Cdd:PRK09850 188 RLEAETLSgialsgREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDIS-GESGWSAPIKTNVINVTGAGDA----MMAGL 262
|
250 260
....*....|....*....|....*
gi 256558122 354 LASW----PLEERLRFGSLCSALAV 374
Cdd:PRK09850 263 ASCWvdgmPFAESVRFAQGCSSMAL 287
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
106-374 |
1.47e-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: 49.32 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 106 GTVFFDIVFTGMDRLPRPGeelwskgmgsspGGIANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAHEEGIDLSASRR 185
Cdd:cd01937 6 GHVTIDEIVTNGSGVVKPG------------GPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDLFDNGIEVISLLSTET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 186 fTDFHSALTvsiAAEGDRAMathgHDLPEPLSTLIAGAPDARAAVV---DLAGETSwwAQLAQRGSLIFADI-GF-DATE 260
Cdd:cd01937 74 -TTFELNYT---NEGRTRTL----LAKCAAIPDTESPLSTITAEIVilgPVPEEIS--PSLFRKFAFISLDAqGFlRRAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 261 RWNIADLAPLVHCHAFTPNALEAmayTRTDTPDRAVRALAEM-VPLAVVTDGADGSYAIDGStGEEAFcPAVPVTAIDTT 339
Cdd:cd01937 144 QEKLIKCVILKLHDVLKLSRVEA---EVISTPTELARLIKETgVKEIIVTDGEEGGYIFDGN-GKYTI-PASKKDVVDPT 218
|
250 260 270
....*....|....*....|....*....|....*
gi 256558122 340 GAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAV 374
Cdd:cd01937 219 GAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
270-364 |
4.30e-06 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 47.96 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 270 LVHCHAF--TPNALEA-----MAYTRTDTPDRAVRALAEM-VPLAVVT---DGADGSYAIDGSTGEEAFCPAVPVTAIDT 338
Cdd:cd01173 132 LLVPLADiiTPNQFELelltgKKINDLEDAKAAARALHAKgPKTVVVTsveLADDDRIEMLGSTATEAWLVQRPKIPFPA 211
|
90 100
....*....|....*....|....*...
gi 256558122 339 --TGAGDVFAAAMVLGTLASWPLEERLR 364
Cdd:cd01173 212 yfNGTGDLFAALLLARLLKGKSLAEALE 239
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
272-378 |
5.24e-06 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 48.11 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 272 HCHAFTPNALEAMAYTRTDTPDRAVRALAEMV--------------PLAVVTDGADGSYAIDGSTGEEAFCPAV---PVT 334
Cdd:cd01943 180 RVDVFSPNLEEAARLLGLPTSEPSSDEEKEAVlqallfsgilqdpgGGVVLRCGKLGCYVGSADSGPELWLPAYhtkSTK 259
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 256558122 335 AIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:cd01943 260 VVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
237-376 |
7.26e-06 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 47.77 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 237 TSWWAQLAQRGSLIFadigFDATERWNIADL--AP-LVhchafTPN--ALEAMAYTRTDTPDRAVRALAEM----VPLAV 307
Cdd:PRK09513 151 TDWMTRLRSQCPCII----FDSSREALVAGLkaAPwLV-----KPNrrELEIWAGRKLPELKDVIEAAHALreqgIAHVV 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256558122 308 VTDGADGSYAIDGSTGEEAFCPAVPVtaIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQ 376
Cdd:PRK09513 222 ISLGAEGALWVNASGEWIAKPPACDV--VSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQ 288
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
136-384 |
1.05e-05 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 47.31 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 136 PGGI-ANLATAAARLGLRTGLVAGFGDDAYAdWMWHTMAHEEGIDLSASRRFTDFHSALT-VSIAAEGDRAMATHGH--- 210
Cdd:PLN02323 42 PGGApANVAVGISRLGGSSAFIGKVGDDEFG-HMLADILKKNGVNNEGVRFDPGARTALAfVTLRSDGEREFMFYRNpsa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 211 DL---PEPLST-LIAGAPDARAAVVDLAGETSWWAQLA------QRGSLIFADIGF---------DATER----WNIADL 267
Cdd:PLN02323 121 DMllrESELDLdLIRKAKIFHYGSISLITEPCRSAHLAamkiakEAGALLSYDPNLrlplwpsaeAAREGimsiWDEADI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 268 APLvhchaftpNALEAMAYTRTDTP--DRAVRALAEMVPLAVVTDGADGS-YAIDGSTGEeafCPAVPVTAIDTTGAGDV 344
Cdd:PLN02323 201 IKV--------SDEEVEFLTGGDDPddDTVVKLWHPNLKLLLVTEGEEGCrYYTKDFKGR---VEGFKVKAVDTTGAGDA 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 256558122 345 FAAAMvLGTLASWP--------LEERLRFGSLCSALAVQQFGGSLAAP 384
Cdd:PLN02323 270 FVGGL-LSQLAKDLslledeerLREALRFANACGAITTTERGAIPALP 316
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
307-378 |
1.46e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 46.72 E-value: 1.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256558122 307 VVTDGADGS--YAIDGstgeEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLEERLRFGSLCSALAVQQFG 378
Cdd:PLN02630 207 IVTNGKKGCriYWKDG----EMRVPPFPAIQVDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
27-443 |
3.74e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.40 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 27 ARRPDDPTVQPDAATQSADASAPARDAATPGDAAPAVPRGEQPAGASTPAPPEAAECQDWDPLAAQRAAADPPLDVLLSG 106
Cdd:COG3321 858 RRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAA 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 107 TVFFDIVFTGMDRLPRPGEELWSKGMGSSPGGIANLATAAARLGLRTGLVAGFGDDAYADWMWHTMAHEEGIDLSASRRF 186
Cdd:COG3321 938 AAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAA 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 187 TDFHSALTVSIAAEGDRAMATHGHDLPEPLSTLIAGAPDARAAVVDLAGETSWWAQLAQRGSLIFADIGFDATERWNIAD 266
Cdd:COG3321 1018 AAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 267 LAPLVHCHAFTPNALEAMA-YTRTDTPDRAVRALAEMVPLAVVTDGADGSYAIDGSTGEEAFCPAVPVTAIDTTGAGDVF 345
Cdd:COG3321 1098 ALAALAAALLLLALLAALAlAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 346 AAAMVLGTLASWPLEERLRFGSLCSALAVQQFGGSLAAPGWGDITDWWRSLSAAADGGDLRAAYTRSGYRFLDAVVPDHP 425
Cdd:COG3321 1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
|
410
....*....|....*...
gi 256558122 426 VQGRRRAQGTFALRSDAG 443
Cdd:COG3321 1258 ALAALALLAAAAGLAALA 1275
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
278-366 |
2.43e-04 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 42.85 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 278 PNALEAMAYTRTD--TPDRAVRALAEMVPLA-----VVTDGADGSYAIDGSTGEEAFCPavPVTAIDTTGAGDVFAAAMV 350
Cdd:PRK10294 186 PNQKELSALVNRDltQPDDVRKAAQELVNSGkakrvVVSLGPQGALGVDSENCIQVVPP--PVKSQSTVGAGDSMVGAMT 263
|
90
....*....|....*.
gi 256558122 351 LGTLASWPLEERLRFG 366
Cdd:PRK10294 264 LKLAENASLEEMVRFG 279
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
135-384 |
2.79e-04 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 43.00 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 135 SPGGIA-NLATAAARLGLRTGLVAGFGDDAYADWMWHTmAHEEGIDLSASRRFTDFHSALTVSIAAEGDRA-MATHGHDL 212
Cdd:PRK09954 91 SAGGVGrNIAHNLALLGRDVHLLSAIGDDFYGETLLEE-TRRAGVNVSGCIRLHGQSTSTYLAIANRQDETvLAINDTHI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 213 PEPLS-TLIAGAPD--ARAAVV----DLAGETSWWAQLAQRGSLIFADI--GFDATerwNIADLAPLVHCHAFTPNALEA 283
Cdd:PRK09954 170 LQQLTpQLLNGSRDliRHAGVVladcNLTAEALEWVFTLADEIPVFVDTvsEFKAG---KIKHWLAHIHTLKPTQPELEI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 284 M-AYTRTDTPDR--AVRALAEMVPLAVVTDGADGSYAIDGSTGEEAFCPAVPVTAIDTTGAGDVFAAAMVLGTLASWPLE 360
Cdd:PRK09954 247 LwGQAITSDADRnaAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLLTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFR 326
|
250 260
....*....|....*....|....
gi 256558122 361 ERLRFGSLCSALAvqQFGGSLAAP 384
Cdd:PRK09954 327 DSARFAMACAAIS--RASGSLNNP 348
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
102-378 |
4.12e-04 |
|
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: 42.01 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 102 VLLSGTVFFDIVfTGMDRLPRPGEEL------WSKGmgsspGGIANLATAAARLGLRtglVAGFG------------DDA 163
Cdd:cd01939 2 VLCVGLTVLDFI-TTVDKYPFEDSDQrttngrWQRG-----GNASNSCTVLRLLGLS---CEFLGvlsrgpvfesllDDF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 164 YADwmwhtmaheeGIDLSASRRfTDFHSALTVSIAAE--GDRAMATHGHDLPEPLSTLIAGAPDARAAVVDLAG----ET 237
Cdd:cd01939 73 QSR----------GIDISHCYR-KDIDEPASSYIIRSraGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGrnpdET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 238 S--WWAQLAQRGSLIFADIGFDA---TERWNIADLAPLVHCHAFTPNALEAMAYTrtdTPDRAVRALAEMV---PLAVVT 309
Cdd:cd01939 142 LrmMQHIEEHNNRRPEIRITISVeveKPREELLELAAYCDVVFVSKDWAQSRGYK---SPEECLRGEGPRAkkaALLVCT 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256558122 310 DGADGSYAIDgSTGEEAFCPA-VPVTAIDTTGAGDVFAAAMVLGTL-ASWPLEERLRFGSLCSALAVQQFG 378
Cdd:cd01939 219 WGDQGAGALG-PDGEYVHSPAhKPIRVVDTLGAGDTFNAAVIYALNkGPDDLSEALDFGNRVASQKCTGVG 288
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
294-378 |
5.14e-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: 41.68 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 294 RAVRALAEMVPLAVVTDgaDGSYAIDGSTGEEAF-CPAVPV-TAIDTTGAGDVFAAAMvLGTLASWP--LEERLR----F 365
Cdd:cd01946 185 KAARLILAMGPKALIIK--RGEYGALLFTDDGYFaAPAYPLeSVFDPTGAGDTFAGGF-IGYLASQKdtSEANMRraiiY 261
|
90
....*....|...
gi 256558122 366 GSLCSALAVQQFG 378
Cdd:cd01946 262 GSAMASFCVEDFG 274
|
|
| PRK14965 |
PRK14965 |
DNA polymerase III subunits gamma and tau; Provisional |
27-95 |
7.28e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237871 [Multi-domain] Cd Length: 576 Bit Score: 42.04 E-value: 7.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 27 ARRPDDPTVQPDAATQSADASAPAR-DAATPGDAAPAVPRGEQPAGASTPAPPEAAECQDWDPLAAQRAA 95
Cdd:PRK14965 378 ERGAPAPPSAAWGAPTPAAPAAPPPaAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSADPAAAASAG 447
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
277-361 |
5.77e-03 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 38.59 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256558122 277 TPNALEA-----MAYTRTDTPDRAVRALAEM---------VPLAVVTDGADGSYAIDGSTGEEAFCPAVPVtaiDTTGAG 342
Cdd:COG2240 143 TPNLTELalltgRPYETLEEALAAARALLALgpkivvvtsVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTG 219
|
90
....*....|....*....
gi 256558122 343 DVFAAAMVLGTLASWPLEE 361
Cdd:COG2240 220 DLFAALLLAHLLRGKSLEE 238
|
|
| |
