|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-309 |
1.40e-146 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 414.51 E-value: 1.40e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 1 MILTVTLNPSIDVSYPLDHLKIDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGGYFGKWLENQLDQDgIAHDF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHLDDQ-IKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 81 FPINAETRSSIAVLHDGgKQTEILEPGPTIAEEDAQKFLNHFDALLDKSDLITISGSMPQGLPTDYYTQMIAHAGKKNVK 160
Cdd:PRK13508 80 YKIKGETRNCIAILHEG-QQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 161 VLLDTSGATLKSALEAPVKPLLIKPNEEELAGLLQREVDKtDYAALKQDLMDPIFAGVDWIVVSLGSAGAFVKHLDKFYH 240
Cdd:PRK13508 159 VVLDCSGAALQAVLESPYKPTVIKPNIEELSQLLGKEVSE-DLDELKEVLQQPLFEGIEWIIVSLGADGAFAKHNDTFYK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943499 241 AAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAETGFVDPAKFDEYFAKVSI 309
Cdd:PRK13508 238 VDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLGMLNAQEKQTGHVNMANYDELYNQIEV 306
|
|
| lacC |
TIGR01231 |
tagatose-6-phosphate kinase; This enzyme is part of the tagatose-6-phosphate pathway of ... |
1-309 |
5.35e-136 |
|
tagatose-6-phosphate kinase; This enzyme is part of the tagatose-6-phosphate pathway of lactose degradation. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
Pssm-ID: 273515 [Multi-domain] Cd Length: 310 Bit Score: 387.71 E-value: 5.35e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 1 MILTVTLNPSIDVSYPLDHLKIDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGGYFGKWLENQLDQDGIAHDF 80
Cdd:TIGR01231 1 MILTVTLNPSVDISYPLETLKIDTVNRVKEVSKTAGGKGLNVTRVLYQSGDKVLASGFLGGKLGEFIESELDQSPIKHAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 81 FPINAETRSSIAVLHdGGKQTEILEPGPTIAEEDAQKFLNHFDALLDKSDLITISGSMPQGLPTDYYTQMIAHAGKKNVK 160
Cdd:TIGR01231 81 YKISGETRNCIAILH-EGNQTEILEQGPTISHEEAEGFLDHFENLLKKSEVVAISGSLPKGLPNDYYEQLIQLCSDEGVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 161 VLLDTSGATLKSALEAPVKPLLIKPNEEELAGLLQREVDKtDYAALKQDLMDPIFAGVDWIVVSLGSAGAFVKHLDKFYH 240
Cdd:TIGR01231 160 VVLDCSGAPLETVLKSSAKPTVIKPNNEELSQLLGKEVTK-DIEELKDALKEPLFSGIEWIIVSLGRQGAFAKHGDTFYK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491943499 241 AAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAETGFVDPAKFDEYFAKVSI 309
Cdd:TIGR01231 239 VDIPDIPVVNPVGSGDSTVAGITSALNSKKSDADLLKKANTLGMLNAQETMTGHVNLTNYDTLNSQIEV 307
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-307 |
6.41e-133 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 379.48 E-value: 6.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 2 ILTVTLNPSIDVSYPLDHLKIDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGGYFGKWLENQLDQDGIAHDFF 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 82 PINAETRSSIAVLHD-GGKQTEILEPGPTIAEEDAQKFLNHFDALLDKSDLITISGSMPQGLPTDYYTQMIAHAGKKNVK 160
Cdd:COG1105 81 PIEGETRINIKIVDPsDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 161 VLLDTSGATLKSALEApvKPLLIKPNEEELAGLLQREV-DKTDYAALKQDLmdpIFAGVDWIVVSLGSAGAFVKHLDKFY 239
Cdd:COG1105 161 VVLDTSGEALKAALEA--GPDLIKPNLEELEELLGRPLeTLEDIIAAAREL---LERGAENVVVSLGADGALLVTEDGVY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491943499 240 HAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAETGFVDPAKFDEYFAKV 307
Cdd:COG1105 236 RAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLAQV 303
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-293 |
5.28e-123 |
|
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: 353.76 E-value: 5.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 1 MILTVTLNPSIDVSYPLDHLKIDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGGYFGKWLENQLDQDGIAHDF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 81 FPINAETRSSIAVLHDGGKQTEILEPGPTIAEEDAQKFLNHFDALLDKSDLITISGSMPQGLPTDYYTQMIAHAGKKNVK 160
Cdd:cd01164 81 VEVAGETRINVKIKEEDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 161 VLLDTSGATLKSALEApvKPLLIKPNEEELAGLLQREVdkTDYAALKQDLMDPIFAGVDWIVVSLGSAGAFVKHLDKFYH 240
Cdd:cd01164 161 VILDTSGEALLAALAA--KPFLIKPNREELEELFGRPL--GDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 491943499 241 AAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAETG 293
Cdd:cd01164 237 ASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-307 |
5.54e-118 |
|
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: 341.48 E-value: 5.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 2 ILTVTLNPSIDVSYPLDHLKIDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGGYFGKWLENQLDQDGIAHDFF 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 82 PINAETRSSIAVLHDGGKQTEILEPGPTIAEEDAQKFLNHFDALLDKSDLITISGSMPQGLPTDYYTQMIAHAGKKNVKV 161
Cdd:TIGR03168 81 EVKGETRINVKIKESSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 162 LLDTSGATLKSALEApvKPLLIKPNEEELAGLLQREVdkTDYAALKQDLMDPIFAGVDWIVVSLGSAGAFVKHLDKFYHA 241
Cdd:TIGR03168 161 ILDTSGEALREALAA--KPFLIKPNHEELEELFGREL--KTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491943499 242 AIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAETGFVDPAKFDEYFAKV 307
Cdd:TIGR03168 237 TPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVEELLDQV 302
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-309 |
4.83e-94 |
|
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: 281.01 E-value: 4.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 2 ILTVTLNPSIDVSYPLDHLKIDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGGYFGKWLENQLDQDGIAHDFF 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 82 PINAETRSSIAVLHDGGKQTEILEPGPTIAEEDAQKFLNHFDALLDKSDLITISGSMPQGLPTDYYTQMIAHAGKKNVKV 161
Cdd:TIGR03828 81 RVPGETRINVKIKEPSGTETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 162 LLDTSGATLKSALEApvKPLLIKPNEEELAGLLQREV----DKTDYAalkQDLMDpifAGVDWIVVSLGSAGAFVKHLDK 237
Cdd:TIGR03828 161 ILDTSGEALRDGLKA--KPFLIKPNDEELEELFGRELktleEIIEAA---RELLD---LGAENVLISLGADGALLVTKEG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491943499 238 FYHAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAETGFVDPAKFDEYFAKVSI 309
Cdd:TIGR03828 233 ALFAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDIEELLPQVTI 304
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
7-294 |
6.80e-59 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 190.63 E-value: 6.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 7 LNPSID-VSYPLDHLK---IDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGG-YFGKWLENQLDQDGIAHDFF 81
Cdd:pfam00294 1 KVVVIGeANIDLIGNVeglPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 82 PINAETRSSIAVLH-DGGKQTEILEPGPTIAEEDAQKFLNHFDaLLDKSDLITISGSMPQGLPTDYYTQM--IAHAGKKN 158
Cdd:pfam00294 81 VIDEDTRTGTALIEvDGDGERTIVFNRGAAADLTPEELEENED-LLENADLLYISGSLPLGLPEATLEELieAAKNGGTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 159 VKVLLDTSGATLKSALEAPVKPLLIKPNEEELAGLLQREVDktDYAALKQDLMDPIFAGVDWIVVSLGSAGAFVKHLDKF 238
Cdd:pfam00294 160 DPNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLD--DIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 491943499 239 YHA-AIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAETGF 294
Cdd:pfam00294 238 VHVpAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
2-309 |
3.84e-43 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 150.23 E-value: 3.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 2 ILTVTLNPSIDVSYPLDHLKIDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGGyfgkwlENQ------LDQDG 75
Cdd:PRK09513 5 VATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGK------DNQdgfqqlFSELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 76 IAHDFFPINAETRSSIAVLHDGGKQTEILEPGPTIAEEDAQKFLNHFDALLDKSDLITISGSMPQGLPTDYYTQMIAHAG 155
Cdd:PRK09513 79 IANRFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 156 KKNVKVLLDTSGATLKSALEApvKPLLIKPNEEELAGLLQREV-DKTDYAALKQDLMDpifAGVDWIVVSLGSAGAFVKH 234
Cdd:PRK09513 159 SQCPCIIFDSSREALVAGLKA--APWLVKPNRRELEIWAGRKLpELKDVIEAAHALRE---QGIAHVVISLGAEGALWVN 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943499 235 LDKFYHAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAETGFVDPAKFDEYFAKVSI 309
Cdd:PRK09513 234 ASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVGITDRPQLAAMMARVDL 308
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-283 |
2.06e-31 |
|
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: 119.22 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 11 IDVSYPLDHL-KIDTVNRVKTVRKTAGGKGLNVSRVIHMLDHKitaTGFIG----GYFGKWLENQLDQDGIAHDFFPINA 85
Cdd:COG0524 10 VDLVARVDRLpKGGETVLAGSFRRSPGGAAANVAVALARLGAR---VALVGavgdDPFGDFLLAELRAEGVDTSGVRRDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 86 ETRSSIAV--LHDGGKQTEILEPGP--TIAEEDAQkflnhfDALLDKSDLITISGSMPQG-LPTDYYTQMIAHAGKKNVK 160
Cdd:COG0524 87 GAPTGLAFilVDPDGERTIVFYRGAnaELTPEDLD------EALLAGADILHLGGITLASePPREALLAALEAARAAGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 161 VLLDTSgatLKSALEAPVKPLL---------IKPNEEELAGLLqrevDKTDYAALKQDLMDpifAGVDWIVVSLGSAGAF 231
Cdd:COG0524 161 VSLDPN---YRPALWEPARELLrellalvdiLFPNEEEAELLT----GETDPEEAAAALLA---RGVKLVVVTLGAEGAL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 491943499 232 VKHLDKFYHAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTG 283
Cdd:COG0524 231 LYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAA 282
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-292 |
4.33e-30 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 115.65 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 2 ILTVTLNPSIDVS------YPLDHLkidtvnRVKTVRKTAGGKGLNVSRVIHMLDHKITATGFIGGYFGKWLENQLDQDG 75
Cdd:PRK10294 4 IYTLTLAPSLDSAtitpqiYPEGKL------RCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 76 IAHDFFPINAETRSSIAVLHDG-GKQTEILEPGPTIAEEDAQKFLNHFDALlDKSDLITISGSMPQGLPTDYYTQMIAHA 154
Cdd:PRK10294 78 VPVATVEAKDWTRQNLHVHVEAsGEQYRFVMPGAALNEDEFRQLEEQVLEI-ESGAILVISGSLPPGVKLEKLTQLISAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 155 GKKNVKVLLDTSGATLKSALeAPVKPLLIKPNEEELAGLLQREVDKTDyaALKQDLMDPIFAG-VDWIVVSLGSAGAFVK 233
Cdd:PRK10294 157 QKQGIRCIIDSSGDALSAAL-AIGNIELVKPNQKELSALVNRDLTQPD--DVRKAAQELVNSGkAKRVVVSLGPQGALGV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 491943499 234 HLDKFYHAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTMEAET 292
Cdd:PRK10294 234 DSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGT 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
22-280 |
3.89e-17 |
|
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: 79.90 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 22 IDTVNRVK-------TV-----RKTAGGKGLN----VSRvihmLDHKITATGFIGG-YFGKWLENQLDQDGIAHDFFPIN 84
Cdd:cd01174 10 VDLVTRVDrlpkpgeTVlgssfETGPGGKGANqavaAAR----LGARVAMIGAVGDdAFGDELLENLREEGIDVSYVEVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 85 AETRSSIAV--LHDGGKQTEILEPGP--TIAEEDAQKFLnhfdALLDKSDLITISGSMPqgLPTDYYTqmIAHAGKKNVK 160
Cdd:cd01174 86 VGAPTGTAVitVDESGENRIVVVPGAngELTPADVDAAL----ELIAAADVLLLQLEIP--LETVLAA--LRAARRAGVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 161 VLLDTSGATlksaleAPVKPLL-----IKPNEEELAGLLQREVDKTDYAALKQDLMdpIFAGVDWIVVSLGSAGAFVKHL 235
Cdd:cd01174 158 VILNPAPAR------PLPAELLalvdiLVPNETEAALLTGIEVTDEEDAEKAARLL--LAKGVKNVIVTLGAKGALLASG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 491943499 236 DKFYHAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAM 280
Cdd:cd01174 230 GEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFAN 274
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
15-288 |
8.49e-17 |
|
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: 79.16 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 15 YPLDHLKIDTVNrvkTVRKTAGGKGLNVSRVIHMLDHKitaTGFIG----GYFGKWLENQLDQDGIAHDFFPINAETRSS 90
Cdd:cd01166 13 SPPGGGRLEQAD---SFRKFFGGAEANVAVGLARLGHR---VALVTavgdDPFGRFILAELRREGVDTSHVRVDPGRPTG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 91 IAVLhdggkqtEILEPGPT-----IAEE-DAQKFLNHFD-ALLDKSDLITISGSMPQGLPTDYYTQM--IAHAGKKNVKV 161
Cdd:cd01166 87 LYFL-------EIGAGGERrvlyyRAGSaASRLTPEDLDeAALAGADHLHLSGITLALSESAREALLeaLEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 162 LLDT-------SGATLKSALE--APVKPLLIkPNEEELAGLLQREVDKTDYAALKQDLmdpifAGVDWIVVSLGSAGAFV 232
Cdd:cd01166 160 SFDLnyrpklwSAEEAREALEelLPYVDIVL-PSEEEAEALLGDEDPTDAAERALALA-----LGVKAVVVKLGAEGALV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943499 233 KHLDKFYHAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTGMLNTM 288
Cdd:cd01166 234 YTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVT 289
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
130-267 |
3.80e-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: 67.12 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 130 DLITISGSMPQGlptDYYTQMIAHAGKKNVKVLLDTSG----ATLKSALEAPVKPLLIKPNEEELAGLLQREVD--KTDY 203
Cdd:cd00287 59 DAVVISGLSPAP---EAVLDALEEARRRGVPVVLDPGPravrLDGEELEKLLPGVDILTPNEEEAEALTGRRDLevKEAA 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943499 204 AALKQDLMDpifaGVDWIVVSLGSAGAFVKHLDKFY-HAAIPKIKVVNPVGSGDSTLAGLAMGIH 267
Cdd:cd00287 136 EAAALLLSK----GPKVVIVTLGEKGAIVATRGGTEvHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
30-280 |
1.02e-10 |
|
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: 61.18 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 30 TVRKTAGGKGLNVSRVIHMLDHKITATGFIGGYF-GKWLENQLDQDGIAHDFFPINAETRSSIAVLHDGGKQTEILEPGP 108
Cdd:cd01941 29 HVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSeGESILEESEKAGLNVRGIVFEGRSTASYTAILDKDGDLVVALADM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 109 TIAEEDAQKFLNHFDALLDKSDLITISGSmpqgLPTDYYTQMIAHAGKKNVKVLLD-TSGATLKsALEAPVKPL-LIKPN 186
Cdd:cd01941 109 DIYELLTPDFLRKIREALKEAKPIVVDAN----LPEEALEYLLALAAKHGVPVAFEpTSAPKLK-KLFYLLHAIdLLTPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 187 EEELAGLLQREVDKT-DYAALKQDLMDPifaGVDWIVVSLGSAGAFVKHLD-----KFYHAAIPKiKVVNPVGSGDSTLA 260
Cdd:cd01941 184 RAELEALAGALIENNeDENKAAKILLLP---GIKNVIVTLGAKGVLLSSREggvetKLFPAPQPE-TVVNVTGAGDAFVA 259
|
250 260
....*....|....*....|
gi 491943499 261 GLAMGIHDGKSDEDIMKMAM 280
Cdd:cd01941 260 GLVAGLLEGMSLDDSLRFAQ 279
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
19-283 |
7.44e-10 |
|
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: 58.48 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 19 HLKIDTVNR------------VKTVRKTAGGKGLNVSRVIHMLDHK---ITATG--FIGGYFGKWLENQldqdGIAHDFF 81
Cdd:cd01942 7 HLNYDIILKvesfpgpfesvlVKDLRREFGGSAGNTAVALAKLGLSpglVAAVGedFHGRLYLEELREE----GVDTSHV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 82 PINAETRSSIAVLH--DGGKQTEILEPGPTIAEEDaqkflNHFDALLDKSDLITISGsmpqglptdyYTQMIAHA---GK 156
Cdd:cd01942 83 RVVDEDSTGVAFILtdGDDNQIAYFYPGAMDELEP-----NDEADPDGLADIVHLSS----------GPGLIELArelAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 157 KNVKVLLDTSGA----TLKSALEAPVKPLLIKPNEEELagllqrEVDKTDYAALKQDLMdpifAGVDWIVVSLGSAGAFV 232
Cdd:cd01942 148 GGITVSFDPGQElprlSGEELEEILERADILFVNDYEA------ELLKERTGLSEAELA----SGVRVVVVTLGPKGAIV 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 491943499 233 KHLDKFYH-AAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKMAMTTG 283
Cdd:cd01942 218 FEDGEEVEvPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAA 269
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
22-262 |
1.04e-08 |
|
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: 55.33 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 22 IDTV----NRVKTVRKTAGGKGLNVSRVIHMLDHKitaTGFIGGY----FGKWLENQLDQDGIAHDFFPINAETRSSIAV 93
Cdd:cd01167 10 IDFIpegsGAPETFTKAPGGAPANVAVALARLGGK---AAFIGKVgddeFGDFLLETLKEAGVDTRGIQFDPAAPTTLAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 94 LH---DGGKQTEILEPGPTIAEEDAQkflnHFDALLDKSDLITIsGSMPQGLPT--DYYTQMIAHAGKKNVKVLLD---- 164
Cdd:cd01167 87 VTldaDGERSFEFYRGPAADLLLDTE----LNPDLLSEADILHF-GSIALASEPsrSALLELLEAAKKAGVLISFDpnlr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 165 ---TSGATLKSALEAPVKPL--LIKPNEEELAGLLQREvdktDYAALKQDLmdpIFAGVDWIVVSLGSAGAFVKHLDKFY 239
Cdd:cd01167 162 pplWRDEEEARERIAELLELadIVKLSDEELELLFGEE----DPEEIAALL---LLFGLKLVLVTRGADGALLYTKGGVG 234
|
250 260
....*....|....*....|...
gi 491943499 240 HAAIPKIKVVNPVGSGDSTLAGL 262
Cdd:cd01167 235 EVPGIPVEVVDTTGAGDAFVAGL 257
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
193-266 |
1.97e-07 |
|
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: 51.20 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 193 LLQREVDKTDYAA---------LKQDLMDPIFA-GVDWIVVSLGSAGAFVKHLDKFYHAAIPKIKVVNPVGSGDSTLAGL 262
Cdd:cd01940 153 YLQLVCPYVDFAFfsasdlsdeEVKAKLKEAVSrGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGF 232
|
....
gi 491943499 263 AMGI 266
Cdd:cd01940 233 LLSL 236
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
31-279 |
2.32e-07 |
|
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: 51.46 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 31 VRKTAGGKGLNVSRVIHMLDhkiTATGFIGG----YFGKWLENQLDQDGIAHDFFPINAETRSSIAVLHDGGKQteilep 106
Cdd:cd01168 50 VKYIAGGSAANTIRGAAALG---GSAAFIGRvgddKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAE------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 107 gPT-IAEEDAQKFLNHFD---ALLDKSDLITISGSMpQGLPTDYYTQMIAHAGKKNVKVLLDTSGATLKSALEAPVKPLL 182
Cdd:cd01168 121 -RTmCTYLGAANELSPDDldwSLLAKAKYLYLEGYL-LTVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 183 -----IKPNEEELAGLLQREVDKTDYAALKQdlmdpIFAGVDWIVVSLGSAGAFVKHLDKFYH-AAIPKIKVVNPVGSGD 256
Cdd:cd01168 199 pyvdiLFGNEEEAEALAEAETTDDLEAALKL-----LALRCRIVVITQGAKGAVVVEGGEVYPvPAIPVEKIVDTNGAGD 273
|
250 260
....*....|....*....|...
gi 491943499 257 STLAGLAMGIHDGKSDEDIMKMA 279
Cdd:cd01168 274 AFAGGFLYGLVQGEPLEECIRLG 296
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
25-265 |
6.24e-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: 49.87 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 25 VNRVKTVRKTAGGKGlNVSRVIHMLDHKITATGFIGG-YFGKWLENQLDQDGIAHDFFPInaETRSSIA---VLHDGGKQ 100
Cdd:cd01172 29 VVKVEREEIRLGGAA-NVANNLASLGAKVTLLGVVGDdEAGDLLRKLLEKEGIDTDGIVD--EGRPTTTktrVIARNQQL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 101 TEI--LEPGPTIAEEDaQKFLNHFDALLDKSDLITISGSMPQGLPTDYYTQMIAHAGKKNVKVLLDTSGATLKSALEApv 178
Cdd:cd01172 106 LRVdrEDDSPLSAEEE-QRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIAAARELGIPVLVDPKGRDYSKYRGA-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 179 kpLLIKPNEEELAGLLQREV-DKTDYAALKQDLMDpiFAGVDWIVVSLGSAGA--FVKHLDKFYHAAIPKiKVVNPVGSG 255
Cdd:cd01172 183 --TLLTPNEKEAREALGDEInDDDELEAAGEKLLE--LLNLEALLVTLGEEGMtlFERDGEVQHIPALAK-EVYDVTGAG 257
|
250
....*....|
gi 491943499 256 DSTLAGLAMG 265
Cdd:cd01172 258 DTVIATLALA 267
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
179-268 |
1.82e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 49.06 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 179 KPLLIKPNEEELA-GLLQREVD----KTDYAALKQDLMDPIFAG---------VDWIVVSLGSAGAFVKHLDKFYHAAIP 244
Cdd:PLN02341 266 KSLLVGTPDERRAlEHLLRMSDvlllTSEEAEALTGIRNPILAGqellrpgirTKWVVVKMGSKGSILVTRSSVSCAPAF 345
|
90 100
....*....|....*....|....*
gi 491943499 245 KIKVVNPVGSGDSTLAGLAMG-IHD 268
Cdd:PLN02341 346 KVNVVDTVGCGDSFAAAIALGyIHN 370
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
199-278 |
3.16e-05 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 44.73 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 199 DKTDYaaLKQDLMDPIFAGVDWIVVSLGSAGAFVKHLDKFYHAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKSDEDIMKM 278
Cdd:PRK09813 168 QEDEF--LRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQ 245
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
186-283 |
7.27e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 44.01 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 186 NEEELAGLLQREVDKTDYAALKqdlmdpiFAG--VDWIVVSLGSAGAFVKHLDKFYH-AAIPKIKVVNPVGSGDSTLAGL 262
Cdd:PLN02379 239 NEDEARELLRGEQESDPEAALE-------FLAkyCNWAVVTLGSKGCIARHGKEVVRvPAIGETNAVDATGAGDLFASGF 311
|
90 100
....*....|....*....|.
gi 491943499 263 AMGIHDGKSDEDIMKMAMTTG 283
Cdd:PLN02379 312 LYGLIKGLSLEECCKVGACSG 332
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
36-279 |
1.47e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 42.80 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 36 GGKGLNVSRVIHMLDHKITATGFIGG-YFGK-WLENQLDQdGIAHDFFPINAETRSSIA---VLHDGGKQTEILEPGPTi 110
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTdGFGSdTIKNFKRN-GVNTSFVSRTENSSTGLAmifVDTKTGNNEIVIIPGAN- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 111 aEEDAQKFL-NHFDALLDKSDLITISGSMPqgLPTDYYTQMIAHagKKNVKVLLDTSGATlKSALEAPVKPLL-----IK 184
Cdd:PTZ00292 130 -NALTPQMVdAQTDNIQNICKYLICQNEIP--LETTLDALKEAK--ERGCYTVFNPAPAP-KLAEVEIIKPFLkyvslFC 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 185 PNEEELAGLLQREVdkTDYAALKQDLMDPIFAGVDWIVVSLGSAG-AFVKHLDKFYHAAIPKIKVVNPVGSGDSTLAGLA 263
Cdd:PTZ00292 204 VNEVEAALITGMEV--TDTESAFKASKELQQLGVENVIITLGANGcLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGSMA 281
|
250
....*....|....*.
gi 491943499 264 MGIHDGKSDEDIMKMA 279
Cdd:PTZ00292 282 YFMSRGKDLKESCKRA 297
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
185-271 |
2.44e-04 |
|
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: 42.33 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 185 PNEEELAGLL-----QREVDKTDYAALKQDLMDPIFA-GVDWIVVSLGSAGAFV---KHLDKF----YHAaiPKIKVVNP 251
Cdd:cd01943 186 PNLEEAARLLglptsEPSSDEEKEAVLQALLFSGILQdPGGGVVLRCGKLGCYVgsaDSGPELwlpaYHT--KSTKVVDP 263
|
90 100
....*....|....*....|
gi 491943499 252 VGSGDSTLAGLAMGIHDGKS 271
Cdd:cd01943 264 TGGGNSFLGGFAAGLALTKS 283
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
217-271 |
3.35e-04 |
|
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: 41.62 E-value: 3.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 491943499 217 GVDWIVVSLGSAGAFVKHLDKFYHAAIPKIKVVNPVGSGDSTLAGLAMGIHDGKS 271
Cdd:cd01937 183 GVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKD 237
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
183-266 |
1.51e-03 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 39.53 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943499 183 IKPNEEELAGLlqreVDKTDYAALKQDLMDPIfaGVDWIVVSLGSAGAFVKHLDKFYHAAIPKIKVVNPVGSGDSTLAGL 262
Cdd:PRK09434 184 VKLSEEELCFL----SGTSQLEDAIYALADRY--PIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGL 257
|
....
gi 491943499 263 AMGI 266
Cdd:PRK09434 258 LAGL 261
|
|
| |
