|
Name |
Accession |
Description |
Interval |
E-value |
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
3-293 |
8.53e-98 |
|
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: 289.84 E-value: 8.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACG 82
Cdd:cd01174 1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 RIRHIDGVSTGVASITrV--GGDNCIVLDPGANHVLTGHDVTVVLDEVAAAgDVFVTQLECDLAATWEALAAAHARGLYT 160
Cdd:cd01174 81 YVEVVVGAPTGTAVIT-VdeSGENRIVVVPGANGELTPADVDAALELIAAA-DVLLLQLEIPLETVLAALRAARRAGVTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 161 ILNPAPAVPIPREVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSRVLCEGRTIDSRPP 240
Cdd:cd01174 159 ILNPAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2181798914 241 AVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQQAVP 293
Cdd:cd01174 239 KVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIP 291
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
8-299 |
1.26e-87 |
|
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: 263.69 E-value: 1.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 8 GSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGRIRHI 87
Cdd:TIGR02152 1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 88 DGVSTGVASITrV--GGDNCIVLDPGANHVLTGHDVTVVLDEVAAAgDVFVTQLECDLAATWEALAAAHARGLYTILNPA 165
Cdd:TIGR02152 81 KDTPTGTAFIT-VddTGENRIVVVAGANAELTPEDIDAAEALIAES-DIVLLQLEIPLETVLEAAKIAKKHGVKVILNPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 166 PAVPI-PREVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSRVLCEGRTIDSRPPAVRV 244
Cdd:TIGR02152 159 PAIKDlDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2181798914 245 IDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQQAVPAADEVA 299
Cdd:TIGR02152 239 VDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-298 |
1.27e-67 |
|
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: 213.21 E-value: 1.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACG 82
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 RIRHIDGVSTGVASITR-VGGDNCIVLDPGANHVLTGHDVTvvlDEVAAAGDVFVTQL-----ECDLAATWEALAAAHAR 156
Cdd:COG0524 81 GVRRDPGAPTGLAFILVdPDGERTIVFYRGANAELTPEDLD---EALLAGADILHLGGitlasEPPREALLAALEAARAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 157 GLYTILNPA-------PAVPIPREVWASVDAICLNETECEIVTGvfpgdELAIEHALELLADWGVGMVALTLGAQGSRVL 229
Cdd:COG0524 158 GVPVSLDPNyrpalwePARELLRELLALVDILFPNEEEAELLTG-----ETDPEEAAAALLARGVKLVVVTLGAEGALLY 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181798914 230 CEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQQAVPAADEV 298
Cdd:COG0524 233 TGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-300 |
1.06e-66 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 211.52 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 1 MGKVIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVA 80
Cdd:PTZ00292 15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 81 CGRIRHIDGVSTGVASIT--RVGGDNCIVLDPGANHVLTGHDVTVVLDEVAAAGDVFVTQLECDLAATWEALAAAHARGL 158
Cdd:PTZ00292 95 TSFVSRTENSSTGLAMIFvdTKTGNNEIVIIPGANNALTPQMVDAQTDNIQNICKYLICQNEIPLETTLDALKEAKERGC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 159 YTILNPAPA-----VPIPREVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSrVLCEGR 233
Cdd:PTZ00292 175 YTVFNPAPApklaeVEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGC-LIVEKE 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181798914 234 TIDSRPPAVRV--IDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQQAVPAADEVAA 300
Cdd:PTZ00292 254 NEPVHVPGKRVkaVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSELPA 322
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
1-300 |
2.41e-66 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 209.73 E-value: 2.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 1 MGKVIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVA 80
Cdd:PRK11142 2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 81 CGRIRHIDGVSTGVASItRVG--GDNCIVLDPGANHVLTGHDVTVVLDEVAAAgDVFVTQLECDLAATWEALAAAHARGL 158
Cdd:PRK11142 82 TAPVSVIKGESTGVALI-FVNdeGENSIGIHAGANAALTPALVEAHRELIANA-DALLMQLETPLETVLAAAKIAKQHGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 159 YTILNPAPAVPIPREVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSRVLCEGRTidSR 238
Cdd:PRK11142 160 KVILNPAPARELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEG--QR 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181798914 239 PPAVRV--IDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQQAVPAADEVAA 300
Cdd:PRK11142 238 VPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDA 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
3-289 |
1.88e-46 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 158.28 E-value: 1.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTIECPRQPrmGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACG 82
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 RIRHIDGVSTGVASI-TRVGGDNCIVLDPGANHVLTGHDVTVVLDEVAAAGDVFVT---QLECDLAATWEALAAAHARGL 158
Cdd:pfam00294 79 YVVIDEDTRTGTALIeVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISgslPLGLPEATLEELIEAAKNGGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 159 YT--ILNPAPAV-PIPREVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSRVLCEGRTI 235
Cdd:pfam00294 159 FDpnLLDPLGAArEALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2181798914 236 D-SRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQ 289
Cdd:pfam00294 239 HvPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
4-289 |
4.98e-32 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 120.11 E-value: 4.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 4 VIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGR 83
Cdd:cd01942 2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 84 IRHIDGVSTGVASITRVGGDNCIV-LDPGAN---HVLTGHDVTVVLDEVAAAGDVFVTQLECDLaatwealaaaHARGLY 159
Cdd:cd01942 82 VRVVDEDSTGVAFILTDGDDNQIAyFYPGAMdelEPNDEADPDGLADIVHLSSGPGLIELAREL----------AAGGIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 160 TILNPAPAVP-----IPREVWASVDAICLNETECEIVtgvfpgDELAIEHALELLAdwGVGMVALTLGAQGSRVLCEGRT 234
Cdd:cd01942 152 VSFDPGQELPrlsgeELEEILERADILFVNDYEAELL------KERTGLSEAELAS--GVRVVVVTLGPKGAIVFEDGEE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181798914 235 IDSRP-PAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQ 289
Cdd:cd01942 224 VEVPAvPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
3-288 |
7.67e-29 |
|
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: 111.90 E-value: 7.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTiecPRQPRMGETVtgSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACG 82
Cdd:cd01166 1 DVVTIGEVMVDLS---PPGGGRLEQA--DSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 RIRHIDGVSTGVASITRVGGDNCIVL---DPGANHVLTGHDVTvvLDEVAAAGDVFVT-----QLECDLAATWEALAAAH 154
Cdd:cd01166 76 HVRVDPGRPTGLYFLEIGAGGERRVLyyrAGSAASRLTPEDLD--EAALAGADHLHLSgitlaLSESAREALLEALEAAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 155 ARGLYTIL---------NPAPAVPIPREVWASVDAICLNETECEIVTGVFPGDElAIEHALELLAdwGVGMVALTLGAQG 225
Cdd:cd01166 154 ARGVTVSFdlnyrpklwSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTD-AAERALALAL--GVKAVVVKLGAEG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181798914 226 SRVLCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGA 288
Cdd:cd01166 231 ALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
10-302 |
2.59e-23 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 97.13 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 10 LN--MDLTIECPRqPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVfGDALVASLEGAGVACGRIRhI 87
Cdd:COG1105 6 LNpaLDRTYEVDE-LEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVP-I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 88 DGVS-TGVASITRVGGDNCIVLDPGAnhVLTGHDVTVVLD---EVAAAGDVFV----------TQLECDLAATWealaaa 153
Cdd:COG1105 83 EGETrINIKIVDPSDGTETEINEPGP--EISEEELEALLErleELLKEGDWVVlsgslppgvpPDFYAELIRLA------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 154 HARGLYTIL---NPA--PAVPiprevwASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSRV 228
Cdd:COG1105 155 RARGAKVVLdtsGEAlkAALE------AGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181798914 229 LCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQqaVPAADEVAALM 302
Cdd:COG1105 229 VTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTG--LPDREDVEELL 300
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
3-288 |
1.25e-21 |
|
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: 92.31 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTIEcprqprmgETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACG 82
Cdd:cd01167 1 KVVCFGEALIDFIPE--------GSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 RIRHIDGVSTGVASITRVG-GDNC--IVLDPGANHVLTGHDVTVVLDEVAAAgdVF--VTQLECDLAATWEAL-AAAHAR 156
Cdd:cd01167 73 GIQFDPAAPTTLAFVTLDAdGERSfeFYRGPAADLLLDTELNPDLLSEADIL--HFgsIALASEPSRSALLELlEAAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 157 GLYTIL----------NPAPAVPIPREVWASVDAICLNETECEIVTGVFPGDElaiehALELLADWGVGMVALTLGAQGS 226
Cdd:cd01167 151 GVLISFdpnlrpplwrDEEEARERIAELLELADIVKLSDEELELLFGEEDPEE-----IAALLLLFGLKLVLVTRGADGA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181798914 227 RVLCEGRTIDSRPPAVRVIDTTGAGDTYIGA----LAMGRARGLS---LDETVEWATCSSALATARLGA 288
Cdd:cd01167 226 LLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGllaqLLSRGLLALDedeLAEALRFANAVGALTCTKAGA 294
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
4-293 |
1.31e-21 |
|
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: 91.97 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 4 VIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGR 83
Cdd:cd01945 2 VLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 84 IRHIDGVSTGVASITRVGGDNCIVLdpgANHVLTG-HDVTVVLDEVAAAGDVFVTQLECDlaATWEALAAAHARGLYTIL 162
Cdd:cd01945 82 IVVAPGARSPISSITDITGDRATIS---ITAIDTQaAPDSLPDAILGGADAVLVDGRQPE--AALHLAQEARARGIPIPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 163 --NPAPAVPIPREVWASVDAIClNETECEIVTGVfpgdelAIEHALELLADWGVGMVALTLGAQGSRVL-CEGRTIDSRP 239
Cdd:cd01945 157 dlDGGGLRVLEELLPLADHAIC-SENFLRPNTGS------ADDEALELLASLGIPFVAVTLGEAGCLWLeRDGELFHVPA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2181798914 240 PAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQQAVP 293
Cdd:cd01945 230 FPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLP 283
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
37-300 |
1.34e-19 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 87.17 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 37 PGGkGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGRIRHIDGVSTGVAsiTRVGGDNCIVL--DPGANH 114
Cdd:COG2870 55 PGG-AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTK--TRVIAGGQQLLrlDFEDRF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 115 VLTGHDVTVVLDEVAAAGDvfvtqlECD-----------LAATWEALAAAHARGLYtilNPAPAVPIPREVWASVDAICL 183
Cdd:COG2870 132 PLSAELEARLLAALEAALP------EVDavilsdygkgvLTPELIQALIALARAAG---KPVLVDPKGRDFSRYRGATLL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 184 --NETECEIVTGVFPGDELAIE-HALELLADWGVGMVALTLGAQGSRVLCEGRTIDSRP-PAVRVIDTTGAGDTYIGALA 259
Cdd:COG2870 203 tpNLKEAEAAVGIPIADEEELVaAAAELLERLGLEALLVTRGEEGMTLFDADGPPHHLPaQAREVFDVTGAGDTVIATLA 282
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2181798914 260 MGRARGLSLDETVEWATCSSALATARLGAqqAVPAADEVAA 300
Cdd:COG2870 283 LALAAGASLEEAAELANLAAGIVVGKLGT--ATVSPEELLA 321
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
12-287 |
5.86e-17 |
|
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: 79.11 E-value: 5.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 12 MDLTIECPrQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDvFGDALVASLEGAGVACGRIRhidgvs 91
Cdd:cd01164 11 IDLTIELD-QLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVE------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 92 tgVASITRVggdNCIVLDPGANH---VLTGHDVTV--------VLDEVAAAGDVFV--------------TQLecdlaat 146
Cdd:cd01164 83 --VAGETRI---NVKIKEEDGTEteiNEPGPEISEeelealleKLKALLKKGDIVVlsgslppgvpadfyAEL------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 147 weaLAAAHARGLYTILNPAPAvPIPREVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGS 226
Cdd:cd01164 151 ---VRLAREKGARVILDTSGE-ALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181798914 227 RVLCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLG 287
Cdd:cd01164 227 LLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
35-288 |
2.30e-16 |
|
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: 78.04 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 35 LNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACgRIRHIDGVSTGVasitrvggdnCIVL-DPGAN 113
Cdd:cd01168 52 YIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPTGT----------CAVLvTPDAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 114 -----HVLTGHDVTVVLDEVAAAGDVFVTQLE-----CDLAATWEALAAAHARGLYTILN-PAPA-VPIPREVWAS---- 177
Cdd:cd01168 121 rtmctYLGAANELSPDDLDWSLLAKAKYLYLEgylltVPPEAILLAAEHAKENGVKIALNlSAPFiVQRFKEALLEllpy 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 178 VDAICLNETECEIVTGVFPGDELAIehALELLADwGVGMVALTLGAQGSRVLCEGRTID-SRPPAVRVIDTTGAGDTYIG 256
Cdd:cd01168 201 VDILFGNEEEAEALAEAETTDDLEA--ALKLLAL-RCRIVVITQGAKGAVVVEGGEVYPvPAIPVEKIVDTNGAGDAFAG 277
|
250 260 270
....*....|....*....|....*....|..
gi 2181798914 257 ALAMGRARGLSLDETVEWATCSSALATARLGA 288
Cdd:cd01168 278 GFLYGLVQGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
37-265 |
8.52e-16 |
|
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: 75.47 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 37 PGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGRIRHIDGvSTGVAsitrvggdncIVLDPGANHVL 116
Cdd:cd01940 21 PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEG-ENAVA----------DVELVDGDRIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 117 TGHDVTVVLDEVAAAGDV-FVTQLecDLAATWEALAAAHARGLYTILNpAPAVPIPREVWASVDAICLnETECEIVT-GV 194
Cdd:cd01940 90 GLSNKGGVAREHPFEADLeYLSQF--DLVHTGIYSHEGHLEKALQALV-GAGALISFDFSDRWDDDYL-QLVCPYVDfAF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181798914 195 FPGDELAIEHALELLAD---WGVGMVALTLGAQGSRVLCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARG 265
Cdd:cd01940 166 FSASDLSDEEVKAKLKEavsRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLAG 239
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
3-263 |
7.39e-15 |
|
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: 71.74 E-value: 7.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAvgvdvfgdalvaslegagvacg 82
Cdd:cd00287 1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVGA---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 RIRHIDGVSTGVASITRVggdncivldpgANHVLTgHDVTVVLDEVAAAGDVFVTQLEcdlaatwealaaaharglytil 162
Cdd:cd00287 59 DAVVISGLSPAPEAVLDA-----------LEEARR-RGVPVVLDPGPRAVRLDGEELE---------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 163 npapavpiprEVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSRVLCEGRTIDSRPP-A 241
Cdd:cd00287 105 ----------KLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAfP 174
|
250 260
....*....|....*....|..
gi 2181798914 242 VRVIDTTGAGDTYIGALAMGRA 263
Cdd:cd00287 175 VKVVDTTGAGDAFLAALAAGLA 196
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
3-287 |
4.30e-14 |
|
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: 71.30 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGkGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGvacg 82
Cdd:cd01944 1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 rIRHIDGVSTGVASITRV-----GGDNCIVLDPGANHVLTGHDVTVVldEVAAAGDVFVT--QL--ECDLAATWEALAAA 153
Cdd:cd01944 76 -IEILLPPRGGDDGGCLValvepDGERSFISISGAEQDWSTEWFATL--TVAPYDYVYLSgyTLasENASKVILLEWLEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 154 HARGLYTILNPAPAVP-IPREVWASVDA----ICLNETECEIVTGvfPGDELAIEHALELLADWGVGMVaLTLGAQGSRV 228
Cdd:cd01944 153 LPAGTTLVFDPGPRISdIPDTILQALMAkrpiWSCNREEAAIFAE--RGDPAAEASALRIYAKTAAPVV-VRLGSNGAWI 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 229 -LCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLG 287
Cdd:cd01944 230 rLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
37-294 |
3.71e-13 |
|
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: 68.36 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 37 PGGkGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGRIRhIDGVSTGVAsiTRVGGDN--CIVLDPGANH 114
Cdd:cd01172 39 LGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIV-DEGRPTTTK--TRVIARNqqLLRVDREDDS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 115 VLTGHDVTVV---LDEVAAAGDVFVTqleCDlaatwealaaaHARGLYT------ILNPAPAVPIP---------REVWA 176
Cdd:cd01172 115 PLSAEEEQRLierIAERLPEADVVIL---SD-----------YGKGVLTprvieaLIAAARELGIPvlvdpkgrdYSKYR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 177 SVDAICLNETECEIVTGVFPGDELAIEHALE-LLADWGVGMVALTLGAQGSRVLCEGRTIDSRPP-AVRVIDTTGAGDTY 254
Cdd:cd01172 181 GATLLTPNEKEAREALGDEINDDDELEAAGEkLLELLNLEALLVTLGEEGMTLFERDGEVQHIPAlAKEVYDVTGAGDTV 260
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2181798914 255 IGALAMGRARGLSLDETVEWATCSSALATARLGAQQAVPA 294
Cdd:cd01172 261 IATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPK 300
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
3-282 |
9.37e-13 |
|
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: 67.34 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTIECPRQPRMGETVTGSGFLlNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACg 82
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQ-SPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 RIRHIDGVSTG--VASITRVGGDNCIVLDPGANHVLTGHDVTVVLDEVAAAGDVFVtqlECDLAATWEALAAAHAR--GL 158
Cdd:cd01941 79 RGIVFEGRSTAsyTAILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVV---DANLPEEALEYLLALAAkhGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 159 YTILNP--APAVPIPREVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSrVLCEGRTID 236
Cdd:cd01941 156 PVAFEPtsAPKLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGV-LLSSREGGV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2181798914 237 SR---PPAV--RVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALA 282
Cdd:cd01941 235 ETklfPAPQpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
37-280 |
4.93e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 64.76 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 37 PGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGRIRHIDGVsTGVASITRVGGDNCI------VLdp 110
Cdd:PRK09813 22 SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGV-TAQTQVELHDNDRVFgdytegVM-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 111 gANHVLTGHDVtvvldEVAAAGDVFVTQL----ECDLaatwealAAAHARGLYTILNPA--PAVPIPREVWASVDaicln 184
Cdd:PRK09813 99 -ADFALSEEDY-----AWLAQYDIVHAAIwghaEDAF-------PQLHAAGKLTAFDFSdkWDSPLWQTLVPHLD----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 185 eteceIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSRVLCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRAR 264
Cdd:PRK09813 161 -----YAFASAPQEDEFLRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLA 235
|
250
....*....|....*.
gi 2181798914 265 GLSLDETVEWATCSSA 280
Cdd:PRK09813 236 GMTLPQAMAQGTACAA 251
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
39-302 |
2.49e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 64.08 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 39 GKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGV-ACGRIRHIDGVSTGVASITRVggdNCIVL-DPGANHVL 116
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGIsVVGLIEGTDAGDSSSASYETL---LCWVLvDPLQRHGF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 117 TGH----------DVTVVLDEVAAA----------GDVFvTQLECDLAATWEALAAAhaRGLYTILNPAP-------AVP 169
Cdd:PLN02341 197 CSRadfgpepafsWISKLSAEAKMAirqskalfcnGYVF-DELSPSAIASAVDYAID--VGTAVFFDPGPrgksllvGTP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 170 IPREVWASV----DAICLNETECEIVTGVfpgdELAIEHALELL-----ADWgvgmVALTLGAQGSrVLCEGRTIDSRP- 239
Cdd:PLN02341 274 DERRALEHLlrmsDVLLLTSEEAEALTGI----RNPILAGQELLrpgirTKW----VVVKMGSKGS-ILVTRSSVSCAPa 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181798914 240 PAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSAlATAR-LGAQQAVPAADEVAALM 302
Cdd:PLN02341 345 FKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA-ATAMgCGAGRNVATLEKVLELL 407
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-299 |
2.54e-11 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 63.03 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 1 MGKVIVFGSLNMDLTIEcprqprmgetvtGSGFLLN-PGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGV 79
Cdd:PRK09434 2 MNKVWVLGDAVVDLIPE------------GENRYLKcPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 80 ACGRIRHIDGVSTgvaSITRVGGDNC------IVLDPGANHVLTGHDVTV-------------------------VLDEV 128
Cdd:PRK09434 70 DTTYLRLDPAHRT---STVVVDLDDQgersftFMVRPSADLFLQPQDLPPfrqgewlhlcsialsaepsrsttfeAMRRI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 129 AAAGDvFVT---QLECDLAAtwealaaaharglytilNPAPAVPIPREVWASVDAICLNETECEIVTGvfpgdELAIEHA 205
Cdd:PRK09434 147 KAAGG-FVSfdpNLREDLWQ-----------------DEAELRECLRQALALADVVKLSEEELCFLSG-----TSQLEDA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 206 LELLAD-WGVGMVALTLGAQGSRVLCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARG------LSLDETVEWATCS 278
Cdd:PRK09434 204 IYALADrYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAglwtdeAELAEIIAQAQAC 283
|
330 340
....*....|....*....|.
gi 2181798914 279 SALATARLGAQQAVPAADEVA 299
Cdd:PRK09434 284 GALATTAKGAMTALPNRQELE 304
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
27-302 |
2.99e-11 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 63.10 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 27 TVTG------SGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGRIRHIDGVSTGVASIT-R 99
Cdd:PLN02323 26 TVSGvslaeaPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTlR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 100 VGGDNCIVL--DPGANHVLTGHDVTVVLDEVAAagdVF-------------VTQLEcdlaatwealAAAHARGLYTILNP 164
Cdd:PLN02323 106 SDGEREFMFyrNPSADMLLRESELDLDLIRKAK---IFhygsislitepcrSAHLA----------AMKIAKEAGALLSY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 165 APAVPIP--------RE----VWASVDAICLNETECEIVTGvfpGDELAIEHALELLADwGVGMVALTLGAQGSRVLCeg 232
Cdd:PLN02323 173 DPNLRLPlwpsaeaaREgimsIWDEADIIKVSDEEVEFLTG---GDDPDDDTVVKLWHP-NLKLLLVTEGEEGCRYYT-- 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181798914 233 RTIDSRPPAVRV--IDTTGAGDTYIGALAMGRARGLS-------LDETVEWATCSSALATARLGAQQAVPAADEVAALM 302
Cdd:PLN02323 247 KDFKGRVEGFKVkaVDTTGAGDAFVGGLLSQLAKDLSlledeerLREALRFANACGAITTTERGAIPALPTKEAVLKLL 325
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
205-282 |
6.03e-09 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 56.24 E-value: 6.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181798914 205 ALELLADWGVGMVALTLGAQGSRVLCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALA 282
Cdd:PRK09513 208 AAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALA 285
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
3-283 |
1.01e-08 |
|
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: 55.12 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 3 KVIVFGSLNMDLTIECPRQPRMGETVTGSGFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEgAGVACG 82
Cdd:cd01947 1 KIAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELE-SGGDKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 83 RIrHIDGVSTGVASITRVGGDNCIVLDPGANH-------VLTGHDvTVVLDevAAAGDVFVTQLEcdlaatwealaaahA 155
Cdd:cd01947 80 TV-AWRDKPTRKTLSFIDPNGERTITVPGERLeddlkwpILDEGD-GVFIT--AAAVDKEAIRKC--------------R 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 156 RGLYTILNPAPAVpiprevwaSVDAICLNETECEIVTGvfPGDELAIEHALELLADWGVGMVALTLGAQGSRVLCEGRTI 235
Cdd:cd01947 142 ETKLVILQVTPRV--------RVDELNQALIPLDILIG--SRLDPGELVVAEKIAGPFPRYLIVTEGELGAILYPGGRYN 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2181798914 236 DSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWAT-CSSALAT 283
Cdd:cd01947 212 HVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAqCGAICVS 260
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
4-284 |
1.68e-08 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 54.99 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 4 VIVFGSLNMDLTIECPRQPRMGETVTGSgFLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGR 83
Cdd:PRK09850 7 VVIIGSANIDVAGYSHESLNYADSNPGK-IKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 84 IRHIDGVSTG------------VASITRVGGDNCIVLDPGANHV--LTGHDVTVVldevaaagdvfvtqlECDLAATWEA 149
Cdd:PRK09850 86 CLIVPGENTSsylslldntgemLVAINDMNISNAITAEYLAQHRefIQRAKVIVA---------------DCNISEEALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 150 LAAAHARGLYTILNPAPA---VPIpREVWASVDAICLNETECEIVTGVfpgdELAIEHALELLADW----GVGMVALTLG 222
Cdd:PRK09850 151 WILDNAANVPVFVDPVSAwkcVKV-RDRLNQIHTLKPNRLEAETLSGI----ALSGREDVAKVAAWfhqhGLNRLVLSMG 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181798914 223 AQG---SRVlcEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATA 284
Cdd:PRK09850 226 GDGvyySDI--SGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
205-284 |
7.04e-08 |
|
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: 52.40 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 205 ALELLADWGVGMVALTLGAQGSRVLCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLdetvEWATCSSALATA 284
Cdd:cd01937 175 LARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDI----KEAAEFAAAAAA 250
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
37-288 |
3.59e-07 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 51.37 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 37 PGGkGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACgrirHIDGVSTgVASIT--RVGGDN--CIVLD--- 109
Cdd:PRK11316 50 PGG-AANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKC----DFVSVPT-HPTITklRVLSRNqqLIRLDfee 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 110 -----------PGANHVLTGHDVTVV-------LDEVA-------AAG-DVFV----TQLEcdlaatwealaaaHARGLy 159
Cdd:PRK11316 124 gfegvdpqpllERIEQALPSIGALVLsdyakgaLASVQamiqlarKAGvPVLIdpkgTDFE-------------RYRGA- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 160 TILNPapavpiprevwasvdaiclNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLGAQGSRVLCEGRtidsrP 239
Cdd:PRK11316 190 TLLTP-------------------NLSEFEAVVGKCKDEAELVEKGMKLIADYDLSALLVTRSEQGMTLLQPGK-----A 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2181798914 240 P------AVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGA 288
Cdd:PRK11316 246 PlhlptqAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGT 300
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
215-287 |
1.07e-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: 49.26 E-value: 1.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181798914 215 GMVALTLGAQGSRVL-CEGRTIDSRPP----AVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLG 287
Cdd:cd01943 226 GGVVLRCGKLGCYVGsADSGPELWLPAyhtkSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
5-302 |
2.46e-06 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 48.39 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 5 IVFGSLNMDL----TIECPRQPRMGETVTGSGfllnpGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGV- 79
Cdd:PRK09954 61 VVVGAINMDIrgmaDIRYPQAASHPGTIHCSA-----GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVn 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 80 --ACGRIrHIDGVSTGVASITRvggDNCIVLDPGANHV---LTGHDVTVVLDEVAAAGDVFVtqlECDLAatwealaaah 154
Cdd:PRK09954 136 vsGCIRL-HGQSTSTYLAIANR---QDETVLAINDTHIlqqLTPQLLNGSRDLIRHAGVVLA---DCNLT---------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 155 ARGLYTILNPAPAVPI------------PREVWASVDAICLNETECEIVTGVFPGDELAIEHALELLADWGVGMVALTLG 222
Cdd:PRK09954 199 AEALEWVFTLADEIPVfvdtvsefkagkIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 223 AQGsrVLC---EGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLGAQQAVPAADEVA 299
Cdd:PRK09954 279 DES--VFCsekDGEQFLLTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAISRASGSLNNPTLSADNAL 356
|
...
gi 2181798914 300 ALM 302
Cdd:PRK09954 357 SLV 359
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
26-299 |
2.81e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 48.27 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 26 ETVTGSGFLLNPGGKGANQAVAAARLGADTV--------MIGAVGVDVFGDALVASLEGAGVACGRIRHIDGVSTGVasi 97
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQSAagpalnvaMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTV--- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 98 trvggdncIVL-DPGANHVL---TGHDVTVVLDEVAA----AGDVFVTQ-----LECDLAATWEALAAAHARGLYTILNP 164
Cdd:PLN02813 191 --------IVLtTPDAQRTMlsyQGTSSTVNYDSCLAsaisKSRVLVVEgylweLPQTIEAIAQACEEAHRAGALVAVTA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 165 APAVPIPR---EVW----ASVDAICLNETECEIVTGVfpGDELAIEHALELLADWgVGMVALTLGAQGSRVLCEGRTIDS 237
Cdd:PLN02813 263 SDVSCIERhrdDFWdvmgNYADILFANSDEARALCGL--GSEESPESATRYLSHF-CPLVSVTDGARGSYIGVKGEAVYI 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181798914 238 RPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETV-EWATCSSALATARLGAQQAVPAADEVA 299
Cdd:PLN02813 340 PPSPCVPVDTCGAGDAYAAGILYGLLRGVSDLRGMgELAARVAATVVGQQGTRLRVEDAVELA 402
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
203-289 |
1.52e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 42.86 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181798914 203 EHALELLA---DWGVgmvaLTLGAQGSRVLCEGRTIdsRPPAV---RVIDTTGAGDTYIGALAMGRARGLSLDETVEWAT 276
Cdd:PLN02379 256 EAALEFLAkycNWAV----VTLGSKGCIARHGKEVV--RVPAIgetNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGA 329
|
90
....*....|...
gi 2181798914 277 CSSALATARLGAQ 289
Cdd:PLN02379 330 CSGGSVVRALGGE 342
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
217-287 |
1.97e-04 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 42.46 E-value: 1.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181798914 217 VALTLGAQGSRVLCEGRTIDSRPPAVRVIDTTGAGDTYIGALAMGRARGLSLDETVEWATCSSALATARLG 287
Cdd:PRK10294 221 VVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQG 291
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
33-95 |
2.31e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 42.59 E-value: 2.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181798914 33 FLLNPGGKGANQAVAAARLGADTVMIGAVGVDVFGDALVASLEGAGVACGRIRHIDGVSTGVA 95
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACS 229
|
|
| |
