|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-309 |
2.12e-142 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 403.72 E-value: 2.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 1 MILTVTLNPSIDVSYPLEHLAIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGGYFGQWLQHQLDIEgIKHDF 80
Cdd:PRK13508 1 MILTVTLNPSIDISYPLDELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATGLIGGELGQFIAEHLDDQ-IKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 81 MTIDAETRSSIAILHDsGNQTEILEAGPMLSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTYYTSMIAHAEKQGVQ 160
Cdd:PRK13508 80 YKIKGETRNCIAILHE-GQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIELANQAGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 161 VLLDTSGATLKNALGAPLKPLLIKPNDEELSDLLKRQINKkDYAALKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYH 240
Cdd:PRK13508 159 VVLDCSGAALQAVLESPYKPTVIKPNIEELSQLLGKEVSE-DLDELKEVLQQPLFEGIEWIIVSLGADGAFAKHNDTFYK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239528014 241 AGIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTGFVDPSQFQKYFDLVTI 309
Cdd:PRK13508 238 VDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLGMLNAQEKQTGHVNMANYDELYNQIEV 306
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-308 |
1.47e-129 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 371.00 E-value: 1.47e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 2 ILTVTLNPSIDVSYPLEHLAIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGGYFGQWLQHQLDIEGIKHDFM 81
Cdd:COG1105 1 ILTVTLNPALDRTYEVDELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFTGEFIEELLDEEGIPTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 82 TIDAETRSSIAILHD-SGNQTEILEAGPMLSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTYYTSMIAHAEKQGVQ 160
Cdd:COG1105 81 PIEGETRINIKIVDPsDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLARARGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 161 VLLDTSGATLKNALGAplKPLLIKPNDEELSDLLKRQInkKDYAALKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYH 240
Cdd:COG1105 161 VVLDTSGEALKAALEA--GPDLIKPNLEELEELLGRPL--ETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVYR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239528014 241 AGIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTGFVDPSQFQKYFDLVT 308
Cdd:COG1105 237 AKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVEELLAQVE 304
|
|
| lacC |
TIGR01231 |
tagatose-6-phosphate kinase; This enzyme is part of the tagatose-6-phosphate pathway of ... |
1-309 |
1.60e-125 |
|
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: 361.13 E-value: 1.60e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 1 MILTVTLNPSIDVSYPLEHLAIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGGYFGQWLQHQLDIEGIKHDF 80
Cdd:TIGR01231 1 MILTVTLNPSVDISYPLETLKIDTVNRVKEVSKTAGGKGLNVTRVLYQSGDKVLASGFLGGKLGEFIESELDQSPIKHAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 81 MTIDAETRSSIAILHDsGNQTEILEAGPMLSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTYYTSMIAHAEKQGVQ 160
Cdd:TIGR01231 81 YKISGETRNCIAILHE-GNQTEILEQGPTISHEEAEGFLDHFENLLKKSEVVAISGSLPKGLPNDYYEQLIQLCSDEGVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 161 VLLDTSGATLKNALGAPLKPLLIKPNDEELSDLLKRQINkKDYAALKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYH 240
Cdd:TIGR01231 160 VVLDCSGAPLETVLKSSAKPTVIKPNNEELSQLLGKEVT-KDIEELKDALKEPLFSGIEWIIVSLGRQGAFAKHGDTFYK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239528014 241 AGIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTGFVDPSQFQKYFDLVTI 309
Cdd:TIGR01231 239 VDIPDIPVVNPVGSGDSTVAGITSALNSKKSDADLLKKANTLGMLNAQETMTGHVNLTNYDTLNSQIEV 307
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-293 |
1.15e-118 |
|
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: 342.98 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 1 MILTVTLNPSIDVSYPLEHLAIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGGYFGQWLQHQLDIEGIKHDF 80
Cdd:cd01164 1 MIYTVTLNPAIDLTIELDQLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGFTGDFFEALLKEEGIPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 81 MTIDAETRSSIAILHDSGNQTEILEAGPMLSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTYYTSMIAHAEKQGVQ 160
Cdd:cd01164 81 VEVAGETRINVKIKEEDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAREKGAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 161 VLLDTSGATLKNALGAplKPLLIKPNDEELSDLLKRQINkkDYAALKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYH 240
Cdd:cd01164 161 VILDTSGEALLAALAA--KPFLIKPNREELEELFGRPLG--DEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVYR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 239528014 241 AGIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTG 293
Cdd:cd01164 237 ASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-308 |
7.71e-116 |
|
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: 336.08 E-value: 7.71e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 2 ILTVTLNPSIDVSYPLEHLAIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGGYFGQWLQHQLDIEGIKHDFM 81
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVDGLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLGGFTGEFIEALLAEEGIKNDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 82 TIDAETRSSIAILHDSGNQTEILEAGPMLSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTYYTSMIAHAEKQGVQV 161
Cdd:TIGR03168 81 EVKGETRINVKIKESSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 162 LLDTSGATLKNALGAplKPLLIKPNDEELSDLLKRqiNKKDYAALKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYHA 241
Cdd:TIGR03168 161 ILDTSGEALREALAA--KPFLIKPNHEELEELFGR--ELKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239528014 242 GIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTGFVDPSQFQKYFDLVT 308
Cdd:TIGR03168 237 TPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVEELLDQVT 303
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-309 |
1.91e-90 |
|
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: 271.77 E-value: 1.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 2 ILTVTLNPSIDVSYPLEHLAIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGGYFGQWLQHQLDIEGIKHDFM 81
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELDGLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFLGGFTGDFIEALLREEGIKTDFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 82 TIDAETRSSIAILHDSGNQTEILEAGPMLSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTYYTSMIAHAEKQGVQV 161
Cdd:TIGR03828 81 RVPGETRINVKIKEPSGTETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAREKGAKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 162 LLDTSGATLKNALGAplKPLLIKPNDEELSDLLKRqiNKKDYAALKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYHA 241
Cdd:TIGR03828 161 ILDTSGEALRDGLKA--KPFLIKPNDEELEELFGR--ELKTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239528014 242 GIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTGFVDPSQFQKYFDLVTI 309
Cdd:TIGR03828 237 QPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDIEELLPQVTI 304
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
11-294 |
8.09e-53 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 174.84 E-value: 8.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 11 IDVsYPLEHLAIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGG-YFGQWLQHQLDIEGIKHDFMTIDAETRS 89
Cdd:pfam00294 10 IDL-IGNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDdNFGEFLLQELKKEGVDTDYVVIDEDTRT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 90 SIAILH-DSGNQTEILEAGPmlsqDDADRFLTHFDT---LLASADLVTISGSMPQGLPPTYYTSMIAHAEKQG--VQVLL 163
Cdd:pfam00294 89 GTALIEvDGDGERTIVFNRG----AAADLTPEELEEnedLLENADLLYISGSLPLGLPEATLEELIEAAKNGGtfDPNLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 164 DTSGATLKNALGAPLKPLLIKPNDEELSDLLKRQINkkDYAALKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYHA-G 242
Cdd:pfam00294 165 DPLGAAREALLELLPLADLLKPNEEELEALTGAKLD--DIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVpA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 239528014 243 IPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTGF 294
Cdd:pfam00294 243 VPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
2-311 |
9.40e-42 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 146.76 E-value: 9.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 2 ILTVTLNPSIDVSYPLEHLAIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGGYFGQWLQHQLDIEGIKHDFM 81
Cdd:PRK09513 5 VATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 82 TIDAETRSSIAILHDSGNQTEILEAGPMLSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTYYTSMIAHAEKQGVQV 161
Cdd:PRK09513 85 VVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQCPCI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 162 LLDTSGATLKNALGAplKPLLIKPNDEELSDLLKRQINK-KDYAALKQNLQEpifNGVSWIVVSLGADGAFVKHNSKFYH 240
Cdd:PRK09513 165 IFDSSREALVAGLKA--APWLVKPNRRELEIWAGRKLPElKDVIEAAHALRE---QGIAHVVISLGAEGALWVNASGEWI 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239528014 241 AGIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTGFVDPSQFQKYFDLVTIDP 311
Cdd:PRK09513 240 AKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVGITDRPQLAAMMARVDLTP 310
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-283 |
3.83e-32 |
|
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: 121.14 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 11 IDVSYPLEHL-AIDTINRTTDVRKTAGGKGLNVSRVIHQLNHDitaTGFIG----GYFGQWLQHQLDIEGIKHDFMTIDA 85
Cdd:COG0524 10 VDLVARVDRLpKGGETVLAGSFRRSPGGAAANVAVALARLGAR---VALVGavgdDPFGDFLLAELRAEGVDTSGVRRDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 86 ETRSSIAI--LHDSGNQTeileagpMLSQDDADRFLTHFD---TLLASADLVTISGSMPQG-LPPTYYTSMIAHAEKQGV 159
Cdd:COG0524 87 GAPTGLAFilVDPDGERT-------IVFYRGANAELTPEDldeALLAGADILHLGGITLASePPREALLAALEAARAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 160 QVLLDTS-GATLKNALGAPLKPLL-----IKPNDEELSDLLkrqiNKKDYAALKQNLQEpifNGVSWIVVSLGADGAFVK 233
Cdd:COG0524 160 PVSLDPNyRPALWEPARELLRELLalvdiLFPNEEEAELLT----GETDPEEAAAALLA---RGVKLVVVTLGAEGALLY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 239528014 234 HNSKFYHAGIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTG 283
Cdd:COG0524 233 TGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAA 282
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-308 |
1.49e-30 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 117.19 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 2 ILTVTLNPSIDVS------YPLEHLaidtinRTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGGYFGQWLQHQLDIEG 75
Cdd:PRK10294 4 IYTLTLAPSLDSAtitpqiYPEGKL------RCSAPVFEPGGGGINVARAIAHLGGSATAIFPAGGATGEHLVSLLADEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 76 IKHDfmTIDAE--TRSSIAI-LHDSGNQTEILEAGPMLSQDDADRFLTHFDTLLASADLVtISGSMPQGLPPTYYTSMIA 152
Cdd:PRK10294 78 VPVA--TVEAKdwTRQNLHVhVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILV-ISGSLPPGVKLEKLTQLIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 153 HAEKQGVQVLLDTSGATLKNALgAPLKPLLIKPNDEELSDLLKRQINKKDyaALKQNLQEPIFNGVS-WIVVSLGADGAF 231
Cdd:PRK10294 155 AAQKQGIRCIIDSSGDALSAAL-AIGNIELVKPNQKELSALVNRDLTQPD--DVRKAAQELVNSGKAkRVVVSLGPQGAL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239528014 232 VKHNSKFYHAGIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTMQAQTGFVDPSQFQKYFDLVT 308
Cdd:PRK10294 232 GVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRLCSHDDTQKIYAYLS 308
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
15-288 |
1.14e-16 |
|
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: 78.77 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 15 YPLEHLAIDTINRttdVRKTAGGKGLNVSRVIHQLNHDitaTGFIG----GYFGQWLQHQLDIEGIKHDFMTIDAETRSS 90
Cdd:cd01166 13 SPPGGGRLEQADS---FRKFFGGAEANVAVGLARLGHR---VALVTavgdDPFGRFILAELRREGVDTSHVRVDPGRPTG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 91 IAIL-HDSGNQTEIL-----EAGPMLSQDDADRFLthfdtlLASADLVTISGSMPQGLPPTYYTSM--IAHAEKQGVQVL 162
Cdd:cd01166 87 LYFLeIGAGGERRVLyyragSAASRLTPEDLDEAA------LAGADHLHLSGITLALSESAREALLeaLEAAKARGVTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 163 LDT-------SGATLKNALG--APLKPLLIkPNDEELSDLLKRQINKKDYAALKQNLqepifNGVSWIVVSLGADGAFVK 233
Cdd:cd01166 161 FDLnyrpklwSAEEAREALEelLPYVDIVL-PSEEEAEALLGDEDPTDAAERALALA-----LGVKAVVVKLGAEGALVY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 239528014 234 HNSKFYHAGIPKVNVVNPVGSGDATLAGLAMGIHDQNSDEIILKTAMTTGMLNTM 288
Cdd:cd01166 235 TGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVT 289
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
32-290 |
8.87e-16 |
|
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: 76.14 E-value: 8.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 32 RKTAGGKGLNVSRVIHQLNHDitaTGFIGGY----FGQWLQHQLDIEGIKHDFMTIDAETRSSIAI--LHDSGNQTEILE 105
Cdd:cd01167 24 TKAPGGAPANVAVALARLGGK---AAFIGKVgddeFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFvtLDADGERSFEFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 106 AGPmlsqdDADRFLT--HFDTLLASADLVTIsGSMPQGLPPTY--YTSMIAHAEKQGVQVLLD-------TSGATLKNAL 174
Cdd:cd01167 101 RGP-----AADLLLDteLNPDLLSEADILHF-GSIALASEPSRsaLLELLEAAKKAGVLISFDpnlrpplWRDEEEARER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 175 GAPLKPL--LIKPNDEELSDLLKRQINKKDYAALKqnlqepiFNGVSWIVVSLGADGAFVKHNSKFYHAGIPKVNVVNPV 252
Cdd:cd01167 175 IAELLELadIVKLSDEELELLFGEEDPEEIAALLL-------LFGLKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTT 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 239528014 253 GSGDATLAGLAMGIHDQNSDEI-------ILKTAMTTGMLNTMQA 290
Cdd:cd01167 248 GAGDAFVAGLLAQLLSRGLLALdedelaeALRFANAVGALTCTKA 292
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
20-263 |
3.51e-15 |
|
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: 74.51 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 20 LAIDTINRT------------TDVRKTAGGKGLNVSRVIHQLNHDITATGFIGG-YFGQWLQHQLDIEGIKHDFMTIDAE 86
Cdd:cd01174 8 INVDLVTRVdrlpkpgetvlgSSFETGPGGKGANQAVAAARLGARVAMIGAVGDdAFGDELLENLREEGIDVSYVEVVVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 87 TRSSIAI--LHDSGNQTEILEAGP--MLSQDDADRFLThfdtLLASADLVTISGSMPqgLPPTYYTsmIAHAEKQGVQVL 162
Cdd:cd01174 88 APTGTAVitVDESGENRIVVVPGAngELTPADVDAALE----LIAAADVLLLQLEIP--LETVLAA--LRAARRAGVTVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 163 LDTSGAtlkNALGAPLKPL--LIKPNDEELSDLLKRQI-NKKDYAALKQNLQEPifnGVSWIVVSLGADGAFVKHNSKFY 239
Cdd:cd01174 160 LNPAPA---RPLPAELLALvdILVPNETEAALLTGIEVtDEEDAEKAARLLLAK---GVKNVIVTLGAKGALLASGGEVE 233
|
250 260
....*....|....*....|....
gi 239528014 240 HAGIPKVNVVNPVGSGDATLAGLA 263
Cdd:cd01174 234 HVPAFKVKAVDTTGAGDTFIGALA 257
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
123-267 |
1.33e-12 |
|
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: 65.58 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 123 DTLLASADLVTISGSMPQglpPTYYTSMIAHAEKQGVQVLLDTS--GATLKNALGAPLKPL--LIKPNDEELSDLLKRQI 198
Cdd:cd00287 52 SVTLVGADAVVISGLSPA---PEAVLDALEEARRRGVPVVLDPGprAVRLDGEELEKLLPGvdILTPNEEEAEALTGRRD 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239528014 199 N--KKDYAALKQNLQEpifnGVSWIVVSLGADGAFVKHNSKFY-HAGIPKVNVVNPVGSGDATLAGLAMGIH 267
Cdd:cd00287 129 LevKEAAEAAALLLSK----GPKVVIVTLGEKGAIVATRGGTEvHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
32-265 |
2.22e-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: 60.27 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 32 RKTAGGKGlNVSRVIHQLNHDITATGFIGG-YFGQWLQHQLDIEGIKHDFMTIdaETRSSIA---ILhdSGNQtEIL--- 104
Cdd:cd01172 36 EIRLGGAA-NVANNLASLGAKVTLLGVVGDdEAGDLLRKLLEKEGIDTDGIVD--EGRPTTTktrVI--ARNQ-QLLrvd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 105 -EAGPMLSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTYYTSMIAHAEKQGVQVLLDTSGATLKNALGAplkpLLI 183
Cdd:cd01172 110 rEDDSPLSAEEEQRLIERIAERLPEADVVILSDYGKGVLTPRVIEALIAAARELGIPVLVDPKGRDYSKYRGA----TLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 184 KPNDEELSDLLKRQINKKD-YAALKQNLQEpiFNGVSWIVVSLGADG-AFVKHNSKFYHagIPKVN--VVNPVGSGDATL 259
Cdd:cd01172 186 TPNEKEAREALGDEINDDDeLEAAGEKLLE--LLNLEALLVTLGEEGmTLFERDGEVQH--IPALAkeVYDVTGAGDTVI 261
|
....*.
gi 239528014 260 AGLAMG 265
Cdd:cd01172 262 ATLALA 267
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
19-266 |
4.62e-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: 59.25 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 19 HLAIDTINR------------TTDVRKTAGGKGLNVSRVIHQLNHD---ITATG--FIGGYFGQWLQHqldiEGIKHDFM 81
Cdd:cd01942 7 HLNYDIILKvesfpgpfesvlVKDLRREFGGSAGNTAVALAKLGLSpglVAAVGedFHGRLYLEELRE----EGVDTSHV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 82 TIDAETRSSIAILH--DSGNQTEILEAGPMLSQDDADRflthfDTLLASADLVTISGsmpqglpptyYTSMIAHAEKQGV 159
Cdd:cd01942 83 RVVDEDSTGVAFILtdGDDNQIAYFYPGAMDELEPNDE-----ADPDGLADIVHLSS----------GPGLIELARELAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 160 ----------QVLLDTSGATLKNALGaplKPLLIKPNDEELsDLLKRQINKKDYAALKqnlqepifnGVSWIVVSLGADG 229
Cdd:cd01942 148 ggitvsfdpgQELPRLSGEELEEILE---RADILFVNDYEA-ELLKERTGLSEAELAS---------GVRVVVVTLGPKG 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 239528014 230 AFVKHNSKFYH-AGIPKVNVVNPVGSGDATLAGLAMGI 266
Cdd:cd01942 215 AIVFEDGEEVEvPAVPAVKVVDTTGAGDAFRAGFLYGL 252
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
31-280 |
4.97e-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: 59.25 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 31 VRKTAGGKGLNVSRVIHQLNHDITATGFIGGYF-GQWLQHQLDIEGIKHDFMTIDAETRSSIAILHDSGNQTEILEAGPM 109
Cdd:cd01941 30 VKQSPGGVGRNIAENLARLGVSVALLSAVGDDSeGESILEESEKAGLNVRGIVFEGRSTASYTAILDKDGDLVVALADMD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 110 LSQDDADRFLTHFDTLLASADLVTISGSMPQGLPPTyytsMIAHAEKQGVQVLLD-TSGATLKNaLGAPLKPL-LIKPND 187
Cdd:cd01941 110 IYELLTPDFLRKIREALKEAKPIVVDANLPEEALEY----LLALAAKHGVPVAFEpTSAPKLKK-LFYLLHAIdLLTPNR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 188 EELSDLLKRQINKKDyaALKQNLQEPIFNGVSWIVVSLGADGAFV-----KHNSKFYHAGIPKvNVVNPVGSGDATLAGL 262
Cdd:cd01941 185 AELEALAGALIENNE--DENKAAKILLLPGIKNVIVTLGAKGVLLssregGVETKLFPAPQPE-TVVNVTGAGDAFVAGL 261
|
250
....*....|....*...
gi 239528014 263 AMGIHDQNSDEIILKTAM 280
Cdd:cd01941 262 VAGLLEGMSLDDSLRFAQ 279
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
33-266 |
2.83e-09 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 57.25 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 33 KTAGGKGLNVSRVIHQLNHDitaTGFIGGY----FGQWLQHQLDIEGIKHDFMTIDAETRSSIAI--LHDSGNQTEILEA 106
Cdd:PRK09434 25 KCPGGAPANVAVGIARLGGE---SGFIGRVgddpFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVvdLDDQGERSFTFMV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 107 GPmlsqdDADRFLThfdtllasadlvtisgsmPQGLPPT-----YYTSMIAHAEKQGVQVLLdTSGATLKNALG------ 175
Cdd:PRK09434 102 RP-----SADLFLQ------------------PQDLPPFrqgewLHLCSIALSAEPSRSTTF-EAMRRIKAAGGfvsfdp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 176 ----------APLKPLL---------IKPNDEELSDLLKRQINKKDYAALKQNLQEPIfngvswIVVSLGADGAFVKHNS 236
Cdd:PRK09434 158 nlredlwqdeAELRECLrqalaladvVKLSEEELCFLSGTSQLEDAIYALADRYPIAL------LLVTLGAEGVLVHTRG 231
|
250 260 270
....*....|....*....|....*....|
gi 239528014 237 KFYHAGIPKVNVVNPVGSGDATLAGLAMGI 266
Cdd:PRK09434 232 QVQHFPAPSVDPVDTTGAGDAFVAGLLAGL 261
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
36-266 |
4.09e-09 |
|
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: 56.21 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 36 GGKGLNVSRVIHQLNHDitaTGFIGGY----FGQWLQHQLDIEGIKHDFMTIdAETRSSIAILHDSGNQTEILEA--GPM 109
Cdd:cd01940 22 GGNALNVAVYAKRLGHE---SAYIGAVgnddAGAHVRSTLKRLGVDISHCRV-KEGENAVADVELVDGDRIFGLSnkGGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 110 LSQ--DDADRflthfdTLLASADLVTISgsmpqglpptyYTSMIAHAEKqgvqvlldtsgatLKNALGAPLKPLLIKPND 187
Cdd:cd01940 98 AREhpFEADL------EYLSQFDLVHTG-----------IYSHEGHLEK-------------ALQALVGAGALISFDFSD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 188 EELSDLLKRQINKKDYAA----------LKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYHAGIPKVNVVNPVGSGDA 257
Cdd:cd01940 148 RWDDDYLQLVCPYVDFAFfsasdlsdeeVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDS 227
|
....*....
gi 239528014 258 TLAGLAMGI 266
Cdd:cd01940 228 FIAGFLLSL 236
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
142-269 |
8.07e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 56.38 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 142 LPPTYYTSMIAHAEKQGVQVLLDTsgatlknalGAPLKPLLIKPNDE--------ELSDLLkrqINKKDYAALKQNLQEP 213
Cdd:PLN02341 238 LSPSAIASAVDYAIDVGTAVFFDP---------GPRGKSLLVGTPDErralehllRMSDVL---LLTSEEAEALTGIRNP 305
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239528014 214 I-------FNGV--SWIVVSLGADGAFVKHNSKFYHAGIPKVNVVNPVGSGDATLAGLAMG-IHDQ 269
Cdd:PLN02341 306 IlagqellRPGIrtKWVVVKMGSKGSILVTRSSVSCAPAFKVNVVDTVGCGDSFAAAIALGyIHNL 371
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
32-283 |
1.43e-05 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 45.50 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 32 RKTAGGKGLNVSRVIHQLNHDITATGFIGG-YFGQWLQHQLDIEG--IKHdFMTIDAETRSSIAILHDS----GNQTEIL 104
Cdd:PRK09813 19 KAFSGGNAVNVAVYCTRYGIQPGCITWVGDdDYGTKLKQDLARMGvdISH-VHTKHGVTAQTQVELHDNdrvfGDYTEGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 105 EAGPMLSQDDAdRFLTHFDtLLASAdlvtISGSMPQGLPPTyytsmiaHAekQGVQVLLDTSgatlkNALGAPLKPLLIK 184
Cdd:PRK09813 98 MADFALSEEDY-AWLAQYD-IVHAA----IWGHAEDAFPQL-------HA--AGKLTAFDFS-----DKWDSPLWQTLVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 185 PNDEELSdllkrqINKKDYAALKQNLQEPIFNGVSWIVVSLGADGAFVKHNSKFYHAGIPKVNVVNPVGSGDATLAGLAM 264
Cdd:PRK09813 158 HLDYAFA------SAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLC 231
|
250
....*....|....*....
gi 239528014 265 GIhdQNSDEIilKTAMTTG 283
Cdd:PRK09813 232 GW--LAGMTL--PQAMAQG 246
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
27-263 |
7.65e-04 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 40.49 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 27 RTTDVRKTAGGKGLNVSRVIHQLNHDITATGFIGG-YFGQWLQHQLDIEGIKHDFMTIDAETRSSIA-ILHDSGN-QTEI 103
Cdd:PTZ00292 43 HGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTdGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAmIFVDTKTgNNEI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 104 L---EAGPMLSQDDADRfltHFDTLLASADLVTISGSMPqgLPPTYYTSMIAHaeKQGVQVLLDTSGATlKNALGAPLKP 180
Cdd:PTZ00292 123 ViipGANNALTPQMVDA---QTDNIQNICKYLICQNEIP--LETTLDALKEAK--ERGCYTVFNPAPAP-KLAEVEIIKP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 181 LL-----IKPNDEELSDLLKRQINkkDYAALKQNLQEPIFNGVSWIVVSLGADGAFV--KHNSKFYHAGIpKVNVVNPVG 253
Cdd:PTZ00292 195 FLkyvslFCVNEVEAALITGMEVT--DTESAFKASKELQQLGVENVIITLGANGCLIveKENEPVHVPGK-RVKAVDTTG 271
|
250
....*....|
gi 239528014 254 SGDATLAGLA 263
Cdd:PTZ00292 272 AGDCFVGSMA 281
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
217-262 |
1.14e-03 |
|
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: 39.69 E-value: 1.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 239528014 217 GVSWIVVSLGADGAFVKHNSKFYHAGIPKVNVVNPVGSGDATLAGL 262
Cdd:cd01937 183 GVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAF 228
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
31-263 |
1.15e-03 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 39.97 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 31 VRKTAGGKGLNVSRVIHQLNHD---ITATGfiGGYFGQWLQHQLDIEGIKHD-FMTIDAETRSSIAILHDsgNQTEILEA 106
Cdd:PRK09850 35 IKFTPGGVGRNIAQNLALLGNKawlLSAVG--SDFYGQSLLTQTNQSGVYVDkCLIVPGENTSSYLSLLD--NTGEMLVA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 107 GPMLSQDDA--DRFLTHFDTLLASADLVTISGSMPQglpptyyTSMIAHAEKQG-VQVLLDTSGA----TLKNALGaplK 179
Cdd:PRK09850 111 INDMNISNAitAEYLAQHREFIQRAKVIVADCNISE-------EALAWILDNAAnVPVFVDPVSAwkcvKVRDRLN---Q 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 180 PLLIKPNDEELSDLLKRQIN-KKDYAALKQNLQEpifNGVSWIVVSLGADGAFVKHNSKFYHAGIP-KVNVVNPVGSGDA 257
Cdd:PRK09850 181 IHTLKPNRLEAETLSGIALSgREDVAKVAAWFHQ---HGLNRLVLSMGGDGVYYSDISGESGWSAPiKTNVINVTGAGDA 257
|
....*.
gi 239528014 258 TLAGLA 263
Cdd:PRK09850 258 MMAGLA 263
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
185-267 |
3.94e-03 |
|
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: 38.48 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 185 PNDEELSDLL-----KRQINKKDYAALKQNLQEPIF-NGVSWIVVSLGADGAFVKHNSKF-------YHAGIPKVnvVNP 251
Cdd:cd01943 186 PNLEEAARLLglptsEPSSDEEKEAVLQALLFSGILqDPGGGVVLRCGKLGCYVGSADSGpelwlpaYHTKSTKV--VDP 263
|
90
....*....|....*.
gi 239528014 252 VGSGDATLAGLAMGIH 267
Cdd:cd01943 264 TGGGNSFLGGFAAGLA 279
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
113-245 |
4.34e-03 |
|
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.
Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 37.46 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239528014 113 DDADRFLTHFDTLLASADLVTISGsmpqGLPPTY--YTsmiahaeKQGVQvlldtsgatlkNALGAPLKPllikpnDEEL 190
Cdd:cd00885 43 DDEDRIAEALRRASERADLVITTG----GLGPTHddLT-------REAVA-----------KAFGRPLVL------DEEA 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239528014 191 SDLLKRQINKKDYAALKQNLQ--------EPIFNGVSWivvslgADGAFVKHNSKFYH--AGIPK 245
Cdd:cd00885 95 LERIEARFARRGREMTEANLKqamlpegaTLLPNPVGT------APGFSVEHNGKNVFllPGVPS 153
|
|
| |
