|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
7-646 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1024.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 7 PSDRRFDLACLGRLAVDLYAQQFGSPLEDTRSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCD 86
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 87 VSQVQIDPQRLTAQVLLALKDRDTFPLLFMRENCADMAIDAALIDESFIAQCRALAITGTHLSTPGTRRASLAALAAARR 166
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 167 HGVVRVLDIDYRPVLWGLTPRGAGENRYVPDAEVTLQLQQVLSQFDMLVGTEEEFFIAGGAPNDLMAsLRAVREISSAVL 246
Cdd:COG3892 161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAA-LRAVRRVSTATL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 247 VVKRGALGCSVIEGSIPAAIDDAPTFKGERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAA 326
Cdd:COG3892 240 VCKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 327 MPTPAELDH-WFSGTRNPKPDADQQLAHLHRVSPNRAQWNELCVMAFDHRSQFYDIAREAGVSDRRVPALKQLLVKAAEQ 405
Cdd:COG3892 320 MPTWEELDYfLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 406 VEASRNLQGHMGVLIDGSdYGRDALASATGRDWWVGRPVELPSSRPLRFDGTRSIGSALIHWPTEQVVKCLVHYHPDDAV 485
Cdd:COG3892 400 VAAGAGLRGGIGVLIDDR-YGQDALNAATGRGWWIGRPVELPGSRPLRFEHGRDIGSQLVEWPQEHVVKCLVFYHPDDPA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 486 DLRLEQEARVLELWEATRESGNELLLEIIPPKaltPAGTEDEAVLRAVKRFYNLGVKPEWWKLAPMSADGWSALEALVAQ 565
Cdd:COG3892 479 ELRLEQEAQLRRLYDACRRSGHELLLEVIPPK---DGPVDDDTVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 566 RDPFCRGAVILGLNQPLDYLAASFAQA-TNPIVKGFMVGRTLWVSASLRWFKGEIDDAAFIDEVARNFTVLVDAWKNRRN 644
Cdd:COG3892 556 RDPYCRGVVLLGLDAPEEELAAGFAAAaGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQ 635
|
..
gi 501316684 645 VA 646
Cdd:COG3892 636 AA 637
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
332-643 |
6.21e-173 |
|
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various prokaryotic carbohydrate kinases, has no known function.
Pssm-ID: 430888 Cd Length: 310 Bit Score: 494.49 E-value: 6.21e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 332 ELDHWFS-GTRNPKPDADQQLAHLHRVSPNRAQWNELCVMAFDHRSQFYDIAREAGVSDRRVPALKQLLVKAAEQVEASR 410
Cdd:pfam09863 1 ELDYFLSrGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 411 NLQGHMGVLIDGSdYGRDALASATGRDWWVGRPVELPSSRPLRFDGTRSIGSALIHWPTEQVVKCLVHYHPDDAVDLRLE 490
Cdd:pfam09863 81 GLQGGAGVLIDGR-YGQDALNAATGRGWWIGRPIELPGSRPLRFEHGRSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 491 QEARVLELWEATRESGNELLLEIIPPKALtPAGteDEAVLRAVKRFYNLGVKPEWWKLAPMSADGWSALEALVAQRDPFC 570
Cdd:pfam09863 160 QEAQLRELYDACRKSGHELLLEVIPPKDG-PVD--DETYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYC 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501316684 571 RGAVILGLNQPLDYLAASFAQATN-PIVKGFMVGRTLWVSASLRWFKGEIDDAAFIDEVARNFTVLVDAWKNRR 643
Cdd:pfam09863 237 RGVVILGLDAPEEELAAGFAAAAGfPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
11-337 |
3.87e-136 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 400.44 E-value: 3.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 11 RFDLACLGRLAVDLYAQQFGSPLEDTRSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQV 90
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 91 QIDPQRLTAQVLLALKDRDTFPLLFMRENCADMAIDAALIDESFIAQCRALAITGTHLSTPGTRRASLAALAAARRHGVV 170
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 171 RVLDIDYRPVLWGltprgagenryvPDAEVTLQLQQVLSQFDMLVGTEEEFFIAGGApNDLMASLRAVREISSAVLVVKR 250
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGE-GDDEAAARALLDAGVEILVVKR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 251 GALGCSVIEGSipaaiDDAPTFKGERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAAMPTP 330
Cdd:TIGR04382 228 GPEGSLVYTGD-----GEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTL 302
|
....*..
gi 501316684 331 AELDHWF 337
Cdd:TIGR04382 303 EELEAFL 309
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
13-324 |
5.93e-66 |
|
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: 218.21 E-value: 5.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 13 DLACLGRLAVDLYAQQFGsPLEDTRSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQI 92
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 93 DPQRLTAQVLLALKDRDTFPLLFMRENCADMAIDAALIDESFIAQCRALAITGTHLS-TPGTRRASLAALAAARRHGVVR 171
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 172 VLDIDYRPVLWGltPRGAGEnryvpdaevtlQLQQVLSQFDMLVGTEEEFFIAGG--APNDLMASLRAvREISSAVLVVK 249
Cdd:cd01166 160 SFDLNYRPKLWS--AEEARE-----------ALEELLPYVDIVLPSEEEAEALLGdeDPTDAAERALA-LALGVKAVVVK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501316684 250 RGALGCSVIEGsipaaiDDAPTFKGERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACS 324
Cdd:cd01166 226 LGAEGALVYTG------GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
13-333 |
1.84e-61 |
|
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: 206.66 E-value: 1.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 13 DLACLGRLAVDLYAQQFGSP----LEDTRSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVS 88
Cdd:COG0524 1 DVLVIGEALVDLVARVDRLPkggeTVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 89 QVQIDPQRLTAQVLLALKDRDTFPLLFMRenCADMAIDAALIDESFIAQCRALAITGTHLSTPGTRRASLAALAAARRHG 168
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 169 VVRVLDIDYRPVLWgltprgagenryvpdAEVTLQLQQVLSQFDMLVGTEEEFFIAGGAPnDLMASLRAVREISSAVLVV 248
Cdd:COG0524 159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGET-DPEEAAAALLARGVKLVVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 249 KRGALGCSVIEGsipaaiDDAPTFKGERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAAMP 328
Cdd:COG0524 223 TLGAEGALLYTG------GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALP 296
|
....*
gi 501316684 329 TPAEL 333
Cdd:COG0524 297 TREEV 301
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
13-325 |
4.40e-39 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 145.56 E-value: 4.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 13 DLACLGRLAVDLYAQQFGSPLEDTR--SFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQV 90
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVRvsTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 91 QIDPQRLTAQVLLAL-KDRDTFpLLFMRENCADMAIDAALIDESFIAQCRALAITGTHLstPGTRRASLAALAAARRHGV 169
Cdd:pfam00294 81 VIDEDTRTGTALIEVdGDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISGSLP--LGLPEATLEELIEAAKNGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 170 VRVLDidYRPVLWgltprgagenryvpdaEVTLQLQQVLSQFDMLVGTEEEF----FIAGGAPNDLMASLRAVREISSAV 245
Cdd:pfam00294 158 TFDPN--LLDPLG----------------AAREALLELLPLADLLKPNEEELealtGAKLDDIEEALAALHKLLAKGIKT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 246 LVVKRGALGCSVIEGSIPAAIDDAPTfkgerIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSA 325
Cdd:pfam00294 220 VIVTLGADGALVVEGDGEVHVPAVPK-----VKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
16-320 |
3.09e-36 |
|
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: 137.77 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 16 CLGRLAVDLYAQQFGSPledtRSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQIDPQ 95
Cdd:cd01167 4 CFGEALIDFIPEGSGAP----ETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 96 RLTAQVLLALK---DRdTFplLFMRENCADMAIDAALIDESFiAQCRALaITGTH-LSTPGTRRASLAALAAARRHGVVR 171
Cdd:cd01167 80 APTTLAFVTLDadgER-SF--EFYRGPAADLLLDTELNPDLL-SEADIL-HFGSIaLASEPSRSALLELLEAAKKAGVLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 172 VLDIDYRPVLWgltprgagenryvPDAEVTLQL-QQVLSQFDMLVGTEEEF-FIAGGAPNDLMASLRAVREIssAVLVVK 249
Cdd:cd01167 155 SFDPNLRPPLW-------------RDEEEARERiAELLELADIVKLSDEELeLLFGEEDPEEIAALLLLFGL--KLVLVT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501316684 250 RGALGCSVIEGSIPAAIddaptfKGERIEVLNVLGAGDAFMSGLMASLLRGKD-------WAESTKVANACGAIVVSR 320
Cdd:cd01167 220 RGADGALLYTKGGVGEV------PGIPVEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTK 291
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
13-324 |
9.79e-24 |
|
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: 101.62 E-value: 9.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 13 DLACLGRLAVDLYAQQFGSPLEDTRSFSMTL----GGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVS 88
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDLrrefGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 89 QVQIDPQRLTAQVLLaLKDRDTFPLLFMRENCADMAIDAALIDESFIAQCralaitgTHLSTPgtrraslaalaaarrHG 168
Cdd:cd01942 81 HVRVVDEDSTGVAFI-LTDGDDNQIAYFYPGAMDELEPNDEADPDGLADI-------VHLSSG---------------PG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 169 VV---RVLDIDYRPVLWGLTPRGAGenRYVPDAEvtlqlqQVLSQFDMLVGTEEEFfiagGAPNDLMASLRAVREISSAV 245
Cdd:cd01942 138 LIelaRELAAGGITVSFDPGQELPR--LSGEELE------EILERADILFVNDYEA----ELLKERTGLSEAELASGVRV 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501316684 246 LVVKRGALGCSVIEGSIPAAIDDAPtfkgeRIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACS 324
Cdd:cd01942 206 VVVTLGPKGAIVFEDGEEVEVPAVP-----AVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
44-334 |
1.40e-23 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 101.55 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 44 GGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQIDPQRLTAQVLLALKDRDTFPLLFMRENCADM 123
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 124 AIDA-----------------ALIDE----SFIAQCRALAITGTHLStpgtrraslaalaaarrhgvvrvLDIDYRPVLW 182
Cdd:PRK09434 108 FLQPqdlppfrqgewlhlcsiALSAEpsrsTTFEAMRRIKAAGGFVS-----------------------FDPNLREDLW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 183 GLTprgagenryvpdAEVTLQLQQVLSQFDMLVGTEEEF-FIAGGApnDLMASLRAVR-EISSAVLVVKRGALGCSVI-E 259
Cdd:PRK09434 165 QDE------------AELRECLRQALALADVVKLSEEELcFLSGTS--QLEDAIYALAdRYPIALLLVTLGAEGVLVHtR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 260 GSIpaaiddaPTFKGERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKV------ANACGAIVVSRHACSAAMPTPAEL 333
Cdd:PRK09434 231 GQV-------QHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAGLWTDEAELaeiiaqAQACGALATTAKGAMTALPNRQEL 303
|
.
gi 501316684 334 D 334
Cdd:PRK09434 304 E 304
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
16-332 |
6.36e-20 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 91.22 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 16 CLGRLAVDLYAQQFGSPLEDTRSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQIDPQ 95
Cdd:PLN02323 15 CFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 96 RLTAQVLLALKDRDTFPLLFMRENCADMAIDAALIDESFIAQCRALAITGTHLSTPGTRRASLAALAAARRHGVVRVLDI 175
Cdd:PLN02323 95 ARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSYDP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 176 DYRPVLWgltprgagenryvPDAEVTlqLQQVLS---QFDMLVGTEEEF-FIAGGAPNDLMASLRAVREiSSAVLVVKRG 251
Cdd:PLN02323 175 NLRLPLW-------------PSAEAA--REGIMSiwdEADIIKVSDEEVeFLTGGDDPDDDTVVKLWHP-NLKLLLVTEG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 252 ALGCSVIegsipaaiddAPTFKGE----RIEVLNVLGAGDAFMSGLMASLlrGKDWA---------ESTKVANACGAIVV 318
Cdd:PLN02323 239 EEGCRYY----------TKDFKGRvegfKVKAVDTTGAGDAFVGGLLSQL--AKDLSlledeerlrEALRFANACGAITT 306
|
330
....*....|....
gi 501316684 319 SRHACSAAMPTPAE 332
Cdd:PLN02323 307 TERGAIPALPTKEA 320
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
38-329 |
1.31e-18 |
|
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: 86.84 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 38 SFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQIDPQRLTAQVLLALKDRdtfpllfmR 117
Cdd:cd01174 30 SFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDES--------G 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 118 ENC------ADMAIDAALID--ESFIAQCRALaitGTHLSTPgtRRASLAALAAARRHGVVRVLDidyrPvlwgltprga 189
Cdd:cd01174 102 ENRivvvpgANGELTPADVDaaLELIAAADVL---LLQLEIP--LETVLAALRAARRAGVTVILN----P---------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 190 genryvpdAEVTLQLQQVLSQFDMLVGTEEEF-FIAGGAPNDLMASLRAVREISS---AVLVVKRGALGCSVIEGSIPAA 265
Cdd:cd01174 163 --------APARPLPAELLALVDILVPNETEAaLLTGIEVTDEEDAEKAARLLLAkgvKNVIVTLGAKGALLASGGEVEH 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501316684 266 IddaPTFKgerIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAAMPT 329
Cdd:cd01174 235 V---PAFK---VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
11-325 |
7.78e-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: 78.81 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 11 RFDLACLGRLAVDLYAQQFGSPLE--DTRSFSMTL-------------------GGSSGNMAFGVARLGLKSAMISRVGN 69
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFLEklGLKKGDMILadmeeqeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 70 EQMGRFLtETLAREGCDVSQVQIDPQRLTAQ--VLL-ALKDRDTFPLLFMRENCADMAIDAALIDESFIaqcraLAITGT 146
Cdd:cd01168 81 DKLGDFL-LKDLRAAGVDTRYQVQPDGPTGTcaVLVtPDAERTMCTYLGAANELSPDDLDWSLLAKAKY-----LYLEGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 147 HLSTPgtRRASLAALAAARRHGVVRVLDIdyrpvlwgltprgagENRYVPDAeVTLQLQQVLSQFDMLVGTEEEF--FIA 224
Cdd:cd01168 155 LLTVP--PEAILLAAEHAKENGVKIALNL---------------SAPFIVQR-FKEALLELLPYVDILFGNEEEAeaLAE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 225 GGAPNDLMASLRAVREISSAVlVVKRGALGCSVIEGsipAAIDDAPTFKGEriEVLNVLGAGDAFMSGLMASLLRGKDWA 304
Cdd:cd01168 217 AETTDDLEAALKLLALRCRIV-VITQGAKGAVVVEG---GEVYPVPAIPVE--KIVDTNGAGDAFAGGFLYGLVQGEPLE 290
|
330 340
....*....|....*....|.
gi 501316684 305 ESTKVANACGAIVVSRHACSA 325
Cdd:cd01168 291 ECIRLGSYAAAEVIQQLGPRL 311
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
41-333 |
1.37e-12 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 69.07 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 41 MTLGGSsGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQIDPQRLT---------AQVLLALkDR-DT 110
Cdd:COG2870 53 ERPGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTttktrviagGQQLLRL-DFeDR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 111 FPLlfmrencaDMAIDAALID--ESFIAQCRAL--------AITGTHLStpgtrraslaalaaarrhGVVRVLDIDYRPV 180
Cdd:COG2870 131 FPL--------SAELEARLLAalEAALPEVDAVilsdygkgVLTPELIQ------------------ALIALARAAGKPV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 181 LWglTPRGAGENRYVPDAEVTLQLQQVLSQFDMLVGTEEEFFIAGGApndLMASLRAvreissAVLVVKRGALGCSVIEG 260
Cdd:COG2870 185 LV--DPKGRDFSRYRGATLLTPNLKEAEAAVGIPIADEEELVAAAAE---LLERLGL------EALLVTRGEEGMTLFDA 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501316684 261 SIPAAIDDAPtfkgeRIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAAmpTPAEL 333
Cdd:COG2870 254 DGPPHHLPAQ-----AREVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLGTATV--SPEEL 319
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
37-333 |
1.57e-12 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 69.00 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 37 RSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQIDPQRLTAQVLLALKDRDTFPLLFM 116
Cdd:PTZ00292 45 TSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNEIVI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 117 RENcADMAIDAALIDE--SFIAQCRALAITGTHLSTPGTRRASLAALAaarrHGVVRVldidyrpvlWGLTPrgagenry 194
Cdd:PTZ00292 125 IPG-ANNALTPQMVDAqtDNIQNICKYLICQNEIPLETTLDALKEAKE----RGCYTV---------FNPAP-------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 195 VPDAEVTLQLQQVLSQFDML-VGTEEEFFIAGGAPNDLMASLRAVRE---ISSAVLVVKRGALGCSVIE-GSIPAAIdda 269
Cdd:PTZ00292 183 APKLAEVEIIKPFLKYVSLFcVNEVEAALITGMEVTDTESAFKASKElqqLGVENVIITLGANGCLIVEkENEPVHV--- 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501316684 270 ptfKGERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAAMPTPAEL 333
Cdd:PTZ00292 260 ---PGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
40-333 |
5.47e-12 |
|
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: 67.20 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 40 SMTLGGSsGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVqIDPQRLT---------AQVLLALKDRDT 110
Cdd:cd01172 36 EIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGI-VDEGRPTttktrviarNQQLLRVDREDD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 111 FPLlfmrencaDMAIDAALID--ESFIAQCRALAitgthLSTPGtrraslaalaaarrHGVV--RVLD--IDYRPVLwGL 184
Cdd:cd01172 114 SPL--------SAEEEQRLIEriAERLPEADVVI-----LSDYG--------------KGVLtpRVIEalIAAAREL-GI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 185 T----PRGAGENRYvpdaevtlqlqqvlSQFDMLVGTEEEFFIAGGAPNDLMASLRAV-----REISSAVLVVKRGALGC 255
Cdd:cd01172 166 PvlvdPKGRDYSKY--------------RGATLLTPNEKEAREALGDEINDDDELEAAgekllELLNLEALLVTLGEEGM 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501316684 256 SVIEGSipAAIDDAPTFKgerIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAAmpTPAEL 333
Cdd:cd01172 232 TLFERD--GEVQHIPALA---KEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPV--TPKEL 302
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
14-321 |
1.18e-11 |
|
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: 65.52 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 14 LACLGRLAVDLYAQQFGSPLEDTRSFSMT----LGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREG-CDVS 88
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDsresPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGdKHTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 89 QVQIDPQRLTAQVLLALKDRDTF----PLLFMRENCADMAIDAALIDESF-----IAQCRALAItgthlstpgtrrasla 159
Cdd:cd01947 82 AWRDKPTRKTLSFIDPNGERTITvpgeRLEDDLKWPILDEGDGVFITAAAvdkeaIRKCRETKL---------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 160 alaaarrhgvvrvldidyrpVLWGLTPRgagenryvpdaEVTLQLQQVLSQFDMLVGTEEEFFIAGGAPNDLMASLRavr 239
Cdd:cd01947 146 --------------------VILQVTPR-----------VRVDELNQALIPLDILIGSRLDPGELVVAEKIAGPFPR--- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 240 eissaVLVVKRGALGCSVIEGSIPAAIddaPTFKgerIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVS 319
Cdd:cd01947 192 -----YLIVTEGELGAILYPGGRYNHV---PAKK---AKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVS 260
|
..
gi 501316684 320 RH 321
Cdd:cd01947 261 HF 262
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
15-329 |
7.73e-11 |
|
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: 63.47 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 15 ACLGRLAVDLYAQQFGSPLED----TRSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQV 90
Cdd:cd01945 3 LGVGLAVLDLIYLVASFPGGDgkivATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 91 QIDPQRLTAQ--VLLALKDRDTfpllfMRENCADMAIDAALIDESFIAQCRALAITGtHLSTPGTRRASLAALAaarrhG 168
Cdd:cd01945 83 VVAPGARSPIssITDITGDRAT-----ISITAIDTQAAPDSLPDAILGGADAVLVDG-RQPEAALHLAQEARAR-----G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 169 VVRVLDIdyrpvlwgltprgagenryvpDAEVTLQLQQVLSQFDMLVGTEEEFFIAGGAPNDLMasLRAVREISSAVLVV 248
Cdd:cd01945 152 IPIPLDL---------------------DGGGLRVLEELLPLADHAICSENFLRPNTGSADDEA--LELLASLGIPFVAV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 249 KRGALGCSVIE-----GSIPAaiddaptfkgERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHAC 323
Cdd:cd01945 209 TLGEAGCLWLErdgelFHVPA----------FPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGG 278
|
....*.
gi 501316684 324 SAAMPT 329
Cdd:cd01945 279 RAGLPT 284
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
14-321 |
2.39e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 58.60 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 14 LACLGRLAVDLYAQQfgspledTRSFSmtlGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQID 93
Cdd:PRK09813 3 LATIGDNCVDIYPQL-------GKAFS---GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 94 PQRlTAQVLLALKDRDTFPLLFMRENCADMAIDAAliDESFIAQcralaitgthlstpgtrraslaalaaarrHGVVRVl 173
Cdd:PRK09813 73 HGV-TAQTQVELHDNDRVFGDYTEGVMADFALSEE--DYAWLAQ-----------------------------YDIVHA- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 174 didyrpVLWGltprgagenryvpDAEVTL-QLQQ--VLSQFDMLVGTEEE------------FFIAGGAPNDLMASLRAV 238
Cdd:PRK09813 120 ------AIWG-------------HAEDAFpQLHAagKLTAFDFSDKWDSPlwqtlvphldyaFASAPQEDEFLRLKMKAI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 239 REISSAVLVVKRGAlgcsviEGSIpaAIDDAPTFKG--ERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAI 316
Cdd:PRK09813 181 VARGAGVVIVTLGE------NGSI--AWDGAQFWRQapEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAK 252
|
....*
gi 501316684 317 VVSRH 321
Cdd:PRK09813 253 TIQYH 257
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
14-319 |
5.80e-09 |
|
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: 57.71 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 14 LACLGRLAVDLYAQQFGSPLEDT----RSFSMtLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQ 89
Cdd:cd01941 2 IVVIGAANIDLRGKVSGSLVPGTsnpgHVKQS-PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 90 VQIdPQRLTAQVLLAL-KDRDtfpllfMRENCADMAIdAALIDESFIAQ-----CRALAItgthlstpgtrraslaalaa 163
Cdd:cd01941 81 IVF-EGRSTASYTAILdKDGD------LVVALADMDI-YELLTPDFLRKirealKEAKPI-------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 164 arrhgvvrVLDIDY-RPVLWGLTPRGAGENRYVP----DAEVTLQLQQVLSQFDMLVGTEEEFFIAGGAP--NDLMASLR 236
Cdd:cd01941 133 --------VVDANLpEEALEYLLALAAKHGVPVAfeptSAPKLKKLFYLLHAIDLLTPNRAELEALAGALieNNEDENKA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 237 AVREISSAV--LVVKRGA---LGCSVIEGSI----PAAIDDaptfkgeriEVLNVLGAGDAFMSGLMASLLRGKDWAEST 307
Cdd:cd01941 205 AKILLLPGIknVIVTLGAkgvLLSSREGGVEtklfPAPQPE---------TVVNVTGAGDAFVAGLVAGLLEGMSLDDSL 275
|
330
....*....|..
gi 501316684 308 KVANACGAIVVS 319
Cdd:cd01941 276 RFAQAAAALTLE 287
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
14-315 |
1.06e-08 |
|
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: 56.59 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 14 LACLGRLAVDLYAQQFGspledtrsfsMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQID 93
Cdd:cd01940 2 LAAIGDNVVDKYLHLGK----------MYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 94 PqRLTAQVLLALKDRDTfplLFMREN---CADMAIDAAliDESFIAQcralaITGTHLSTPGTRRASLAALAAARRHGVV 170
Cdd:cd01940 72 E-GENAVADVELVDGDR---IFGLSNkggVAREHPFEA--DLEYLSQ-----FDLVHTGIYSHEGHLEKALQALVGAGAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 171 RVLDIDYRpvlwgltprgagenryVPDAEVTLQLQqvlsqfdmlvGTEEEFFIAGGAPNDLM-ASLRAVREISSAVLVVK 249
Cdd:cd01940 141 ISFDFSDR----------------WDDDYLQLVCP----------YVDFAFFSASDLSDEEVkAKLKEAVSRGAKLVIVT 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501316684 250 RGALGCSVIEGS--IPAAIddaptfkgERIEVLNVLGAGDAFMSGLMASLLRGKDW-AESTKVANACGA 315
Cdd:cd01940 195 RGEDGAIAYDGAvfYSVAP--------RPVEVVDTLGAGDSFIAGFLLSLLAGGTAiAEAMRQGAQFAA 255
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
228-337 |
3.67e-08 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 55.53 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 228 PNDLMASLRAVREISSAVLVVKRGAlgcsviEGSIpaAIDDAPTFKGE--RIEVLNVLGAGDAFMSGLMASLLRGKDWAE 305
Cdd:COG1105 199 LEDIIAAARELLERGAENVVVSLGA------DGAL--LVTEDGVYRAKppKVEVVSTVGAGDSMVAGFLAGLARGLDLEE 270
|
90 100 110
....*....|....*....|....*....|..
gi 501316684 306 STKVANACGAIVVSRHAcsAAMPTPAELDHWF 337
Cdd:COG1105 271 ALRLAVAAGAAAALSPG--TGLPDREDVEELL 300
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
10-315 |
7.73e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 55.22 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 10 RRFDLACLGRLAVDLY---AQQFGSPLEDTRSFSMTLG-----------GSSGNMAFGVARLGLKSAMISRVGNEQMGRF 75
Cdd:PLN02341 71 KEIDVATLGNLCVDIVlpvPELPPPSREERKAYMEELAasppdkksweaGGNCNFAIAAARLGLRCSTIGHVGDEIYGKF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 76 LTETLAREGCDV-----SQVQIDPQRLTAQVLL--ALKD---RDTF---------PLL-FMRE--NCADMAIDAALI--- 130
Cdd:PLN02341 151 LLDVLAEEGISVvglieGTDAGDSSSASYETLLcwVLVDplqRHGFcsradfgpePAFsWISKlsAEAKMAIRQSKAlfc 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 131 -----DE---SFIAQCRALAI-TGTHL-STPGtrraslaalaaarrhgvvrvldidyrpvlwgltPRGAGENRYVPDAEV 200
Cdd:PLN02341 231 ngyvfDElspSAIASAVDYAIdVGTAVfFDPG---------------------------------PRGKSLLVGTPDERR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 201 TlqLQQVLSQFDMLVGTEEEFFIAGGAPNDLMASLRAVRE-ISSAVLVVKRGAlgcsviEGSIPAAIDD---APTFKger 276
Cdd:PLN02341 278 A--LEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPgIRTKWVVVKMGS------KGSILVTRSSvscAPAFK--- 346
|
330 340 350
....*....|....*....|....*....|....*....
gi 501316684 277 IEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGA 315
Cdd:PLN02341 347 VNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
25-329 |
2.68e-07 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 53.01 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 25 YAQQFGSPledtRSFSMTLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQ-VQIDPQRLTAQVLL 103
Cdd:PRK09954 78 YPQAASHP----GTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGcIRLHGQSTSTYLAI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 104 ALKDRDTfpllfmrencadmaidaalidesfiaqcrALAITGTHLSTPGTRRASLAALAAARRHGVVrVLDIDYRP--VL 181
Cdd:PRK09954 154 ANRQDET-----------------------------VLAINDTHILQQLTPQLLNGSRDLIRHAGVV-LADCNLTAeaLE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 182 WGLTPrgAGENRYVPDAEVTLQLQQV---LSQFDMLVGTEEEFFIAGGAP----NDLMASLRAVRE--ISSAVLVVKRGA 252
Cdd:PRK09954 204 WVFTL--ADEIPVFVDTVSEFKAGKIkhwLAHIHTLKPTQPELEILWGQAitsdADRNAAVNALHQqgVQQIFVYLPDES 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501316684 253 LGCSVIEGSipAAIDDAPTFKgerieVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIvvSRHACSAAMPT 329
Cdd:PRK09954 282 VFCSEKDGE--QFLLTAPAHT-----TVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAI--SRASGSLNNPT 349
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
247-341 |
4.02e-07 |
|
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: 52.19 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 247 VVKRGAlgcsviEGSIpaAIDDAPTFKGE--RIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHAcs 324
Cdd:TIGR03168 217 LVSLGA------DGAL--LVTKEGALKATppKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG-- 286
|
90
....*....|....*..
gi 501316684 325 AAMPTPAELDHWFSGTR 341
Cdd:TIGR03168 287 TGLPDPEDVEELLDQVT 303
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
217-321 |
7.31e-07 |
|
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: 51.27 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 217 TEEEFFIAGGAPNDLmASLRAVREISSAVLVVKRGALGCSVIEgsipaAIDDAPTFKGERIEVLNVLGAGDAFMSGLMAS 296
Cdd:cd01944 190 EEAAIFAERGDPAAE-ASALRIYAKTAAPVVVRLGSNGAWIRL-----PDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAG 263
|
90 100
....*....|....*....|....*
gi 501316684 297 LLRGKDWAESTKVANACGAIVVSRH 321
Cdd:cd01944 264 LAKGMSLADAVLLANAAAAIVVTRS 288
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
229-321 |
8.13e-06 |
|
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: 47.91 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 229 NDLMASLRAVREISSAVLVVKRGAlgcsviEGSIPAAIDDAPTFKGERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTK 308
Cdd:cd01164 200 EDVIAAARKLIERGAENVLVSLGA------DGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALR 273
|
90
....*....|...
gi 501316684 309 VANACGAIVVSRH 321
Cdd:cd01164 274 LAVAAGSATAFSP 286
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
202-319 |
2.25e-05 |
|
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: 46.95 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 202 LQLQQVLSQFDMLVGTEEEFFIAGGAPNDLMASLRavreiSSAVLVVKRGALGCSV-IEGSIPaaIDDAPTFKGERIEVL 280
Cdd:cd01943 189 EEAARLLGLPTSEPSSDEEKEAVLQALLFSGILQD-----PGGGVVLRCGKLGCYVgSADSGP--ELWLPAYHTKSTKVV 261
|
90 100 110
....*....|....*....|....*....|....*....
gi 501316684 281 NVLGAGDAFMSGLMASLLRGKDWAEstkvANACGAIVVS 319
Cdd:cd01943 262 DPTGGGNSFLGGFAAGLALTKSIDE----ACIYGSVAAS 296
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
218-341 |
3.27e-05 |
|
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: 46.43 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 218 EEEFFIAGGAPNDLMASLRAVREISSA---VLVVKRGAlgcsviEGSIpaAIDDAPTFKGE--RIEVLNVLGAGDAFMSG 292
Cdd:TIGR03828 185 EELEELFGRELKTLEEIIEAARELLDLgaeNVLISLGA------DGAL--LVTKEGALFAQppKGEVVSTVGAGDSMVAG 256
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 501316684 293 LMASLLRGKDWAESTKVANACGAIVVSRHAcsAAMPTPAELDHWFSGTR 341
Cdd:TIGR03828 257 FLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDIEELLPQVT 303
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
204-306 |
5.64e-05 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 45.53 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 204 LQQVLSQFDMLVGTEEEFFIAGGAPNdLMASLRAVREISSAVLVVKRGALGCSVIEGSipaAIDDAPTFKGEriEVLNVL 283
Cdd:cd01946 157 LKKVLAKVDVVIINDGEARQLTGAAN-LVKAARLILAMGPKALIIKRGEYGALLFTDD---GYFAAPAYPLE--SVFDPT 230
|
90 100
....*....|....*....|...
gi 501316684 284 GAGDAFMSGLMASLLRGKDWAES 306
Cdd:cd01946 231 GAGDTFAGGFIGYLASQKDTSEA 253
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
203-298 |
7.14e-05 |
|
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: 44.39 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 203 QLQQVLSQFDMLVGTEEEFFIAGGAPNDLM----ASLRAVREISSAVLVVKRGALGCSVIEGsiPAAIDDAPTFKgerIE 278
Cdd:cd00287 102 ELEKLLPGVDILTPNEEEAEALTGRRDLEVkeaaEAAALLLSKGPKVVIVTLGEKGAIVATR--GGTEVHVPAFP---VK 176
|
90 100
....*....|....*....|
gi 501316684 279 VLNVLGAGDAFMSGLMASLL 298
Cdd:cd00287 177 VVDTTGAGDAFLAALAAGLA 196
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
273-334 |
1.09e-04 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 44.48 E-value: 1.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501316684 273 KGERIEVLNV-----LGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAAMPTPAELD 334
Cdd:PRK11142 234 EGQRVPGFRVqavdtIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEID 300
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
203-324 |
9.21e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 41.94 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 203 QLQQVLSQFDMLVGTEEEFFIAGgapNDLMASLRAVREISS--AVLVVKRGALGCSVI--EGSIPA--AIDDA----PTF 272
Cdd:PTZ00247 207 RLLQVLPYVDILFGNEEEAKTFA---KAMKWDTEDLKEIAAriAMLPKYSGTRPRLVVftQGPEPTliATKDGvtsvPVP 283
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 501316684 273 KGERIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACS 324
Cdd:PTZ00247 284 PLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCT 335
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
42-319 |
1.04e-03 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 41.51 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 42 TLGGSSGNMAFGVARLGLKSAMISRVGNEQMGRFLTETLAREGCDVSQVQIDPQRLTAQvLLALKDRDTFPLLFMRenca 121
Cdd:PRK09850 38 TPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSS-YLSLLDNTGEMLVAIN---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 122 DMAIDAAlIDESFIAQCRALaITGTHLstpgtrraslaalaaarrhgVVRVLDIDYRPVLWGLtpRGAGENRYVPD---A 198
Cdd:PRK09850 113 DMNISNA-ITAEYLAQHREF-IQRAKV--------------------IVADCNISEEALAWIL--DNAANVPVFVDpvsA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 199 EVTLQLQQVLSQFDMLVGTEEEFFIAGGAP----NDLMASLRAVREISSAVLVVKRGALGcsVIEGSIPAAIDDAPTFKg 274
Cdd:PRK09850 169 WKCVKVRDRLNQIHTLKPNRLEAETLSGIAlsgrEDVAKVAAWFHQHGLNRLVLSMGGDG--VYYSDISGESGWSAPIK- 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 501316684 275 erIEVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVS 319
Cdd:PRK09850 246 --TNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
229-318 |
1.45e-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: 40.85 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 229 NDLMASLRAVREISSAVLVVKRGALGCSVIEGSIPAAIddaPTFKgerIEVLNVLGAGDAFMSGLMASLLRGKDWAESTK 308
Cdd:cd01937 170 STPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTI---PASK---KDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAE 243
|
90
....*....|
gi 501316684 309 VANACGAIVV 318
Cdd:cd01937 244 FAAAAAAKFI 253
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
284-324 |
2.20e-03 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 40.85 E-value: 2.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 501316684 284 GAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACS 324
Cdd:PLN02548 284 GAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCT 324
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
35-320 |
4.87e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 39.79 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 35 DTRSFSMTLGGSSGNMAFGVARLGLKS--------AMISRVGNEQMGRFLTETLAREG-CDVSQVQIDPQRLTAQVLLAL 105
Cdd:PLN02813 117 DGCSYKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANvHFLSQPVKDGTTGTVIVLTTP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 106 KDRDTFplLFMRENCADMAIDAALidESFIAQCRALAITGTHLSTPGTRRASLAALAAARRHGV-VRVLDID------YR 178
Cdd:PLN02813 197 DAQRTM--LSYQGTSSTVNYDSCL--ASAISKSRVLVVEGYLWELPQTIEAIAQACEEAHRAGAlVAVTASDvscierHR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 179 PVLWGLTPRGAgenryvpdaevtlqlqqvlsqfDMLVGTEEEFFIAGGAPNDlMASLRAVREISSAVLVVkrgalgcSVI 258
Cdd:PLN02813 273 DDFWDVMGNYA----------------------DILFANSDEARALCGLGSE-ESPESATRYLSHFCPLV-------SVT 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501316684 259 EGSIPAAIddapTFKGERIEV-------LNVLGAGDAFMSGLMASLLRG-KDWAESTKVANACGAIVVSR 320
Cdd:PLN02813 323 DGARGSYI----GVKGEAVYIppspcvpVDTCGAGDAYAAGILYGLLRGvSDLRGMGELAARVAATVVGQ 388
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
278-333 |
6.36e-03 |
|
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: 39.43 E-value: 6.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 501316684 278 EVLNVLGAGDAFMSGLMASLLRGKDWAESTKVANACGAIVVSRHACSAAmpTPAEL 333
Cdd:PRK11316 255 EVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGTSTV--SPIEL 308
|
|
| |
