|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
1-634 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1168.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 1 MEKQFDVICMGRVAVDLYSQQIGARLEDVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDT 80
Cdd:COG3892 2 RMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 81 SHLITDKDRLTALVLLGIKDRDTFPLIFYRDNCADMAITASDVDESYIASARCLAITGTHLSHPQTREAVLTALGYARRH 160
Cdd:COG3892 82 SGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARAH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 161 GVRTVLDIDYRPVLWGLTSLGDGETRFIAADKVTRELQEVLHLFDVIVGTEEEFHIAGGSTDTLRALEQVRGVSQATLVC 240
Cdd:COG3892 162 GGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLVC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 241 KRGALGCSVYPDTIPHRLDDGLTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAMP 320
Cdd:COG3892 242 KRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAMP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 321 SKIELDDYLSRAALVPRPDLDPRLNHLHRVTTRRREWPELCVMAFDHRSQLEEMAMQCGASLKRIPALKQLILQASREAA 400
Cdd:COG3892 322 TWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQVA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 401 SRAGLEGKAGLLCDGTFGQDALNAITGEGWWIGRPIELPGSRPLEMEHG-NIGTQLISWPQEHVVKCLVFFHPEDAHGLR 479
Cdd:COG3892 402 AGAGLRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGrDIGSQLVEWPQEHVVKCLVFYHPDDPAELR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 480 LEQEQKIAEVYHACCQSGHELLLEVILPATMPRSDELYLRAISRFYNLGIYPDWWKLPPLSSEGWTALSEIIERRDPHCR 559
Cdd:COG3892 482 LEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDDTVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAERDPYCR 561
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569245018 560 GVVILGLDAPAEQLRADFKAAAGQALVKGFAVGRTLFGDASRAWLKHDIDDAQLVARIRDNYLQLIAWWRERGHA 634
Cdd:COG3892 562 GVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQA 636
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
324-632 |
0e+00 |
|
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: 560.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 324 ELDDYLSRAALVPRPDLDPRLNHLHRVTTRRREWPELCVMAFDHRSQLEEMAMQCGASLKRIPALKQLILQASREAASRA 403
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 404 GLEGKAGLLCDGTFGQDALNAITGEGWWIGRPIELPGSRPLEMEHG-NIGTQLISWPQEHVVKCLVFFHPEDAHGLRLEQ 482
Cdd:pfam09863 81 GLQGGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGrSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 483 EQKIAEVYHACCQSGHELLLEVILPATMPRSDELYLRAISRFYNLGIYPDWWKLPPLSSEGWTALSEIIERRDPHCRGVV 562
Cdd:pfam09863 161 EAQLRELYDACRKSGHELLLEVIPPKDGPVDDETYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYCRGVV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 563 ILGLDAPAEQLRADFKAAAGQALVKGFAVGRTLFGDASRAWLKHDIDDAQLVARIRDNYLQLIAWWRERG 632
Cdd:pfam09863 241 ILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
4-329 |
1.42e-167 |
|
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: 480.56 E-value: 1.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 4 QFDVICMGRVAVDLYSQQIGARLEDVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHL 83
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 84 ITDKDRLTALVLLGIKDRDTFPLIFYRDNCADMAITASDVDESYIASARCLAITGTHLSHPQTREAVLTALGYARRHGVR 163
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 164 TVLDIDYRPVLWGltslgdgetrfiAADKVTRELQEVLHLFDVIVGTEEEFHIAGGSTDTLRALEQVRGVSQATLVCKRG 243
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 244 ALGCSVYpdtipHRLDDGLTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAMPSKI 323
Cdd:TIGR04382 229 PEGSLVY-----TGDGEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 2569245018 324 ELDDYL 329
Cdd:TIGR04382 304 ELEAFL 309
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
6-316 |
5.23e-82 |
|
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: 260.20 E-value: 5.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 6 DVICMGRVAVDLYSQQIGaRLEDVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLIT 85
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 86 DKDRLTALVLLGIKDRDTFPLIFYRDNCADMAITASDVDESYIASARCLAITGTHLS-HPQTREAVLTALGYARRHGVRT 164
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 165 VLDIDYRPVLWGltslgdgetrfiaADKVTRELQEVLHLFDVIVGTEEEFHIAGGSTDTLRALEQVRGVSQ--ATLVCKR 242
Cdd:cd01166 160 SFDLNYRPKLWS-------------AEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALgvKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569245018 243 GALGCSVYPDTIPHRlddgltVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCA 316
Cdd:cd01166 227 GAEGALVYTGGGRVF------VPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-325 |
1.04e-80 |
|
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: 257.12 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 6 DVICMGRVAVDLYSQ----QIGARLEDVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTS 81
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 82 HLITDKDRLTALVLLGIKDRDTFPLIFYRdnCADMAITASDVDESYIASARCLAITGTHLSHPQTREAVLTALGYARRHG 161
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 162 VRTVLDIDYRPVLWgltslgdgetrfiaaDKVTRELQEVLHLFDVIVGTEEEFHIAGGSTDTLRALEQVRGVSQATLVCK 241
Cdd:COG0524 159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 242 RGALGCSVYPDtiphrlDDGLTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAMPS 321
Cdd:COG0524 224 LGAEGALLYTG------GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 2569245018 322 KIEL 325
Cdd:COG0524 298 REEV 301
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
7-314 |
1.03e-49 |
|
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: 174.75 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 7 VICMGRVAVDLYSQQIGarleDVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITD 86
Cdd:cd01167 2 VVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 87 KDRLTALVLLGIK---DRdTFplIFYRDNCADMaITASDVDESYIASARCLaITGTH-LSHPQTREAVLTALGYARRHGV 162
Cdd:cd01167 78 PAAPTTLAFVTLDadgER-SF--EFYRGPAADL-LLDTELNPDLLSEADIL-HFGSIaLASEPSRSALLELLEAAKKAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 163 RTVLDIDYRPVLWgltslgdgetrfiAADKVTREL-QEVLHLFDVIVGTEEEFHIAGGSTDTLRALEQVRGVSQATLVCK 241
Cdd:cd01167 153 LISFDPNLRPPLW-------------RDEEEARERiAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 242 RGALGCSVYPDtiphrlDDGLTVTGVRVEVLNVLGAGDAFMSGLLRGYL-------NDEGWEQACRYANACGALVVSRHG 314
Cdd:cd01167 220 RGADGALLYTK------GGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLsrgllalDEDELAEALRFANAVGALTCTKAG 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-316 |
4.08e-41 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 151.34 E-value: 4.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 6 DVICMGRVAVDL--YSQQIGARLEDVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHL 83
Cdd:pfam00294 1 KVVVIGEANIDLigNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 84 ITDKDRLT--ALVLLGiKDRDTFpLIFYRDNCADMAITASDVDESYIASARCLAITGTHLSHpqTREAVLTALGYARRHG 161
Cdd:pfam00294 81 VIDEDTRTgtALIEVD-GDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLG--LPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 162 vrTVLDIDYRPVLWgltslgdgetrfiaadKVTRELQEVLHLFDVIVGTEEEFHIAGGST-----DTLRALEQVRGVSQA 236
Cdd:pfam00294 157 --GTFDPNLLDPLG----------------AAREALLELLPLADLLKPNEEELEALTGAKlddieEALAALHKLLAKGIK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 237 TLVCKRGALGCSVYpdtiphRLDDGLTVTGVR-VEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGC 315
Cdd:pfam00294 219 TVIVTLGADGALVV------EGDGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGA 292
|
.
gi 2569245018 316 A 316
Cdd:pfam00294 293 Q 293
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
7-333 |
4.46e-29 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 118.18 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 7 VICMGRVAVDLYSQQIGARLEDVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITD 86
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 87 KDRLTALVLLGIKDRDTFPLIFYRDNCADMAITASDVDESYIASARCLAITGTHLSHPQTREAVLTALGYARRHGVRTVL 166
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 167 DIDYRPVLWGltslgdgetrfiAADKVTRELQEVLHLFDVIVGTEEE--FHIAGGSTDTLRALEQVRGVSQATLVCKrGA 244
Cdd:PLN02323 173 DPNLRLPLWP------------SAEAAREGIMSIWDEADIIKVSDEEveFLTGGDDPDDDTVVKLWHPNLKLLLVTE-GE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 245 LGCSVYPDTIPHRlddgltVTGVRVEVLNVLGAGDAFMSGLL------RGYLNDEG-WEQACRYANACGALVVSRHGCAP 317
Cdd:PLN02323 240 EGCRYYTKDFKGR------VEGFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRFANACGAITTTERGAIP 313
|
330
....*....|....*.
gi 2569245018 318 AMPSKIELDDYLSRAA 333
Cdd:PLN02323 314 ALPTKEAVLKLLKKAV 329
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-315 |
2.90e-26 |
|
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: 108.94 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 6 DVICMGRVAVDLYSQQIGARLEDVSSFAK----YLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTS 81
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 82 HLITdkdrltalvllgiKDRDTFPLIFYRDNCADMAITAS----------DVDESYIASARCLAITGthlshpqtrEAVL 151
Cdd:cd01942 81 HVRV-------------VDEDSTGVAFILTDGDDNQIAYFypgamdelepNDEADPDGLADIVHLSS---------GPGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 152 TALGYARRHGVRTVLdIDYRPVLWGLTslgdgetrfiaadkvTRELQEVLHLFDVIVGTEEEFHIAggSTDT-LRALEQV 230
Cdd:cd01942 139 IELARELAAGGITVS-FDPGQELPRLS---------------GEELEEILERADILFVNDYEAELL--KERTgLSEAELA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 231 RGVsqATLVCKRGALGCSVYpdtiphrlDDGLTVTGVRVEVLNVL---GAGDAFMSGLLRGYLNDEGWEQACRYANACGA 307
Cdd:cd01942 201 SGV--RVVVVTLGPKGAIVF--------EDGEEVEVPAVPAVKVVdttGAGDAFRAGFLYGLLRGYDLEESLRLGNLAAS 270
|
....*...
gi 2569245018 308 LVVSRHGC 315
Cdd:cd01942 271 LKVERRGA 278
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
10-326 |
1.14e-24 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 104.63 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 10 MGRVAVDLYSqqigarlEDVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITDKDR 89
Cdd:PRK09434 8 LGDAVVDLIP-------EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 90 LTALVLLGIKDRDTFPLIFYRDNCADMAITASDVDE---------SYIAsarclaitgthLSHPQTREAVLTALGYARRH 160
Cdd:PRK09434 81 RTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLPPfrqgewlhlCSIA-----------LSAEPSRSTTFEAMRRIKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 161 GVRTVLDIDYRPVLWGLTSlgdgetrfiaadkvtrELQEVLH----LFDVIVGTEEEFHIAGGSTDTLRALEQVRGVSQA 236
Cdd:PRK09434 150 GGFVSFDPNLREDLWQDEA----------------ELRECLRqalaLADVVKLSEEELCFLSGTSQLEDAIYALADRYPI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 237 TLV-CKRGALGCSVYpdtiphrlDDG--LTVTGVRVEVLNVLGAGDAFMSGLLRG------YLNDEGWEQACRYANACGA 307
Cdd:PRK09434 214 ALLlVTLGAEGVLVH--------TRGqvQHFPAPSVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGA 285
|
330
....*....|....*....
gi 2569245018 308 LVVSRHGCAPAMPSKIELD 326
Cdd:PRK09434 286 LATTAKGAMTALPNRQELE 304
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
30-321 |
1.09e-23 |
|
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: 101.47 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 30 SSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITDKDRLT--ALVLLgikDRDtfpli 107
Cdd:cd01174 29 SSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTgtAVITV---DES----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 108 fyRDNC------ADMAITASDVD--ESYIASARCLAitgthLSHPQTREAVLTALGYARRHGVRTVLDidyrPVlwglts 179
Cdd:cd01174 101 --GENRivvvpgANGELTPADVDaaLELIAAADVLL-----LQLEIPLETVLAALRAARRAGVTVILN----PA------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 180 lgdgetrfiAADKVtreLQEVLHLFDVIVGTEEEFH-IAGGSTDTLRALEQVRGVSQA----TLVCKRGALGCSVYPDTI 254
Cdd:cd01174 164 ---------PARPL---PAELLALVDILVPNETEAAlLTGIEVTDEEDAEKAARLLLAkgvkNVIVTLGAKGALLASGGE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569245018 255 PHRlddgltVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAMPS 321
Cdd:cd01174 232 VEH------VPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
37-315 |
2.25e-23 |
|
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: 101.15 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 37 GGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTsHLITDKDRLTA--LVLLGIKDRDTFplifyrdnCA 114
Cdd:cd01168 55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPTGtcAVLVTPDAERTM--------CT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 115 DMAI----TASDVDESYIASARCLAITGTHLSHPQtrEAVLTALGYARRHGVRTVLDidyrpvlwgltsLGDgetRFIAa 190
Cdd:cd01168 126 YLGAanelSPDDLDWSLLAKAKYLYLEGYLLTVPP--EAILLAAEHAKENGVKIALN------------LSA---PFIV- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 191 DKVTRELQEVLHLFDVIVGTEEEFHIAGGSTDTLRaLEQVRGVSQA---TLVCKRGALGCSVYPDtiphrlDDGLTVTGV 267
Cdd:cd01168 188 QRFKEALLELLPYVDILFGNEEEAEALAEAETTDD-LEAALKLLALrcrIVVITQGAKGAVVVEG------GEVYPVPAI 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2569245018 268 RVE-VLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGC 315
Cdd:cd01168 261 PVEkIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGP 309
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
6-321 |
5.47e-19 |
|
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: 87.73 E-value: 5.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 6 DVICMGRVAVDLYsqqigARLEDV---------SSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQV 76
Cdd:cd01945 1 RVLGVGLAVLDLI-----YLVASFpggdgkivaTDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 77 GCDTSHLITDKDRLTAL--VLLGIKDRDTFPLIFYRDNCADMAITASDVDesyiaSARCLAITGtHLshpqtREAVLTAL 154
Cdd:cd01945 76 GVDTSFIVVAPGARSPIssITDITGDRATISITAIDTQAAPDSLPDAILG-----GADAVLVDG-RQ-----PEAALHLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 155 GYARRHGVRTVLDIDyrpvlwgltslgdgetrfIAADKVTRELqevLHLFDVIVGTEEEFHIAGGSTDTLrALEQVRGVS 234
Cdd:cd01945 145 QEARARGIPIPLDLD------------------GGGLRVLEEL---LPLADHAICSENFLRPNTGSADDE-ALELLASLG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 235 QATLVCKRGALGCSVYPDTIPHRlddglTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHG 314
Cdd:cd01945 203 IPFVAVTLGEAGCLWLERDGELF-----HVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLG 277
|
....*..
gi 2569245018 315 CAPAMPS 321
Cdd:cd01945 278 GRAGLPT 284
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
37-330 |
3.34e-14 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 73.75 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 37 GGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITDKDRLTalvllGIKdrdtfpLIFYRDNC--- 113
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGEST-----GVA------LIFVNDEGens 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 114 ------ADMAITASDVDESY--IASARCLAItgtHLSHPQtrEAVLTALGYARRHGVRTVLDidyrPVlwGLTSLGDget 185
Cdd:PRK11142 108 igihagANAALTPALVEAHRelIANADALLM---QLETPL--ETVLAAAKIAKQHGTKVILN----PA--PARELPD--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 186 rfiaadkvtrelqEVLHLFDVIVGTEEEFHIAGGST-----DTLRA---LEQvRGVsqATLVCKRGALG--CSVYpdtip 255
Cdd:PRK11142 174 -------------ELLALVDIITPNETEAEKLTGIRvedddDAAKAaqvLHQ-KGI--ETVLITLGSRGvwLSEN----- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569245018 256 hrlDDGLTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAMPSKIELDDYLS 330
Cdd:PRK11142 233 ---GEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
34-325 |
1.80e-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: 68.36 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 34 KYLGGSsGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTsHLITDKDRLTAlvllgIKDR------------ 101
Cdd:cd01172 37 IRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDT-DGIVDEGRPTT-----TKTRviarnqqllrvd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 102 --DTFPLifyRDNCADMAItasDVDESYIASARCLAIT----GThLShPQTREAVLTAlgyARRHGVRTVLDidyrpvlw 175
Cdd:cd01172 110 reDDSPL---SAEEEQRLI---ERIAERLPEADVVILSdygkGV-LT-PRVIEALIAA---ARELGIPVLVD-------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 176 gltSLGDGETRFIAADKVTRELQEVLHLFDVIVGTEEEFhiaggstdtLRALEQVRGVSQATLVC-KRGALGCSVYPDT- 253
Cdd:cd01172 171 ---PKGRDYSKYRGATLLTPNEKEAREALGDEINDDDEL---------EAAGEKLLELLNLEALLvTLGEEGMTLFERDg 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569245018 254 ----IPhrlddglTVTgvrVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAMPSKIEL 325
Cdd:cd01172 239 evqhIP-------ALA---KEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELLL 304
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
35-325 |
2.29e-12 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 68.30 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 35 YLGGSsGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITDKDRLTAL---VLLGIK-----DR-DTFP 105
Cdd:COG2870 54 RPGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTktrVIAGGQqllrlDFeDRFP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 106 LifyrdncaDMAITASDVD--ESYIASARCLAIT----GThLSHPQTREAVLTalgyARRHGVRTVLD---IDYrpvlwg 176
Cdd:COG2870 133 L--------SAELEARLLAalEAALPEVDAVILSdygkGV-LTPELIQALIAL----ARAAGKPVLVDpkgRDF------ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 177 ltslgdgeTRFIAADKVT---RELQEVLHLFDVivgTEEEFHIAGgstdtLRALEQVRGvsQATLVCkRGALGCSVY-PD 252
Cdd:COG2870 194 --------SRYRGATLLTpnlKEAEAAVGIPIA---DEEELVAAA-----AELLERLGL--EALLVT-RGEEGMTLFdAD 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569245018 253 TIPHRLDdgltvTGVRvEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAmpSKIEL 325
Cdd:COG2870 255 GPPHHLP-----AQAR-EVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLGTATV--SPEEL 319
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
7-314 |
1.61e-11 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 65.07 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 7 VICMGRVAVDLYSQQIGArledvssfakYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITd 86
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 87 KDRLTALVLLGIKDRDTfplIFYRDNCADMAITASDVDESYIASARCLAITGTHlSHPQTREAVLTALGYArrhGVRTVL 166
Cdd:cd01940 71 KEGENAVADVELVDGDR---IFGLSNKGGVAREHPFEADLEYLSQFDLVHTGIY-SHEGHLEKALQALVGA---GALISF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 167 DIDYRPVLWGLTSLGDG-ETRFIAADKVTRELQEVLhlfdvivgteeefhiaggsTDTLRAleqvRGVSqaTLVCKRGAL 245
Cdd:cd01940 144 DFSDRWDDDYLQLVCPYvDFAFFSASDLSDEEVKAK-------------------LKEAVS----RGAK--LVIVTRGED 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 246 GCSVYPDtiphrlDDGLTVTGVRVEVLNVLGAGDAFMSGLLRGYL-NDEGWEQACRYANACGALVVSRHG 314
Cdd:cd01940 199 GAIAYDG------AVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
7-314 |
1.72e-11 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 64.76 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 7 VICMGRVAVDLYsQQIGArledvssfaKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITD 86
Cdd:PRK09813 3 LATIGDNCVDIY-PQLGK---------AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 87 KDRlTALVLLGIKDRDTfplIF--YRDNC-ADMAITASDVDesYIASARCL--AITG-THLSHPQTREA-VLTALGYARR 159
Cdd:PRK09813 73 HGV-TAQTQVELHDNDR---VFgdYTEGVmADFALSEEDYA--WLAQYDIVhaAIWGhAEDAFPQLHAAgKLTAFDFSDK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 160 HG----VRTVLDIDYrpvlwgLTSLGDGETRFIaadkvtrelqevlhlfdvivgteeefhiaggsTDTLRAL-EQVRGVS 234
Cdd:PRK09813 147 WDsplwQTLVPHLDY------AFASAPQEDEFL--------------------------------RLKMKAIvARGAGVV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 235 QATLvckrGALGCSVYpdtiphrldDGLTVTG---VRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVS 311
Cdd:PRK09813 189 IVTL----GENGSIAW---------DGAQFWRqapEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQ 255
|
...
gi 2569245018 312 RHG 314
Cdd:PRK09813 256 YHG 258
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
42-331 |
3.53e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 64.77 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 42 NVAYGTARQGLRSSMLARVGdEHMGRFLREELNQVGCDTSHLITDKD-RlTALVLLGIKDRDTFPLifyrdNCADMAITA 120
Cdd:COG1105 40 NVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVPIEGEtR-INIKIVDPSDGTETEI-----NEPGPEISE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 121 SDVDE------SYIASARCLAITGthlSHPQ----TREAVLTALgyARRHGVRTVLDIDyrpvlwgltslgdGET-RFIA 189
Cdd:COG1105 113 EELEAllerleELLKEGDWVVLSG---SLPPgvppDFYAELIRL--ARARGAKVVLDTS-------------GEAlKAAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 190 ADKVT------RELQEvlhLFDVIVGTEEEFHIAGgstdtlRALeQVRGvsqATLVC----KRGALGcsVYPDTIphrld 259
Cdd:COG1105 175 EAGPDlikpnlEELEE---LLGRPLETLEDIIAAA------REL-LERG---AENVVvslgADGALL--VTEDGV----- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569245018 260 dgLTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGcaPAMPSKIELDDYLSR 331
Cdd:COG1105 235 --YRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELLAQ 302
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
54-324 |
6.80e-11 |
|
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: 63.75 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 54 SSMLARVGDE---------HMGRFLREELNQVGCDTS------------HLITDKDRLTALVLLGikdrdtfPLIfyRDN 112
Cdd:TIGR03168 42 ARVLARLGAEvvatgflggFTGEFIEALLAEEGIKNDfvevkgetrinvKIKESSGEETELNEPG-------PEI--SEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 113 CADMAITASdvdESYIASARCLAITGthlSHPQTRE----AVLTALgyARRHGVRTVLDIDYRPVLWGLtslgdgetrfi 188
Cdd:TIGR03168 113 ELEQLLEKL---RELLASGDIVVISG---SLPPGVPpdfyAQLIAI--ARKKGAKVILDTSGEALREAL----------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 189 aADKVT------RELQEvlhLFDVIVGTEEEFhiaggsTDTLRALeQVRGVsQATLVC--KRGALGCSVypdtiphrlDD 260
Cdd:TIGR03168 174 -AAKPFlikpnhEELEE---LFGRELKTLEEI------IEAAREL-LDRGA-ENVLVSlgADGALLVTK---------EG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569245018 261 GLTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAMPSKIE 324
Cdd:TIGR03168 233 ALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVE 296
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
31-325 |
4.36e-10 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 31 SFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITDKDRLTALVLLGIKDRDTFPLIFYR 110
Cdd:PTZ00292 46 SFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNEIVII 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 111 DNcADMAITASDVDESYIASARCLAITGTHLSHPQtrEAVLTALGYARRHGVRTVLDIDYRPvlwgltslgdgetrfiaA 190
Cdd:PTZ00292 126 PG-ANNALTPQMVDAQTDNIQNICKYLICQNEIPL--ETTLDALKEAKERGCYTVFNPAPAP-----------------K 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 191 DKVTRELQEVLHLFD-VIVGTEEEFHIAGG-STDTLRALE-----QVRGVSqaTLVCKRGALGCS-VYPDTIPhrlddgL 262
Cdd:PTZ00292 186 LAEVEIIKPFLKYVSlFCVNEVEAALITGMeVTDTESAFKaskelQQLGVE--NVIITLGANGCLiVEKENEP------V 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569245018 263 TVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHGCAPAMPSKIEL 325
Cdd:PTZ00292 258 HVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
2-307 |
7.53e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 61.39 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 2 EKQFDVICMGRVAVDL-----------------YSQQIGARLEDVSSFAkyLGGSSgNVAYGTARQGLRSSMLARVGDEH 64
Cdd:PLN02341 70 GKEIDVATLGNLCVDIvlpvpelpppsreerkaYMEELAASPPDKKSWE--AGGNC-NFAIAAARLGLRCSTIGHVGDEI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 65 MGRFLREELNQVGCDTSHLITDKDR----------LTALVLLGIKDRDTF---------PL---IFYRDNCADMAITASd 122
Cdd:PLN02341 147 YGKFLLDVLAEEGISVVGLIEGTDAgdsssasyetLLCWVLVDPLQRHGFcsradfgpePAfswISKLSAEAKMAIRQS- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 123 vdesyiasaRCLAITGTHLSHPQTrEAVLTALGYARRHGVRTVLDIDYRpvlwgltslgdGETRFIAADKVTRELQEVLH 202
Cdd:PLN02341 226 ---------KALFCNGYVFDELSP-SAIASAVDYAIDVGTAVFFDPGPR-----------GKSLLVGTPDERRALEHLLR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 203 LFDVIVGTEEEFHIAGGSTDTLRALEQV--RGVSQATLVCKRGALGcsvypdTIPHRLDDGLTVTGVRVEVLNVLGAGDA 280
Cdd:PLN02341 285 MSDVLLLTSEEAEALTGIRNPILAGQELlrPGIRTKWVVVKMGSKG------SILVTRSSVSCAPAFKVNVVDTVGCGDS 358
|
330 340
....*....|....*....|....*..
gi 2569245018 281 FMSGLLRGYLNDEGWEQACRYANACGA 307
Cdd:PLN02341 359 FAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
29-314 |
1.07e-09 |
|
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: 59.74 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 29 VSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVG-CDTSHLITDKDRLTALVLLGIKDRDTFplI 107
Cdd:cd01947 28 SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGdKHTVAWRDKPTRKTLSFIDPNGERTIT--V 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 108 FYRDNCADMAITA-SDVDESYIASARCLAitgTHLSHPQTREAVLTALGyarrhgvrtvldidyrpvlwgltslgdGETR 186
Cdd:cd01947 106 PGERLEDDLKWPIlDEGDGVFITAAAVDK---EAIRKCRETKLVILQVT---------------------------PRVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 187 FIaadkvtrELQEVLHLFDVIVGTEEEFHIAGGSTDTlrALEQVRgvsqaTLVCKRGALGCSVYPDTiphrldDGLTVTG 266
Cdd:cd01947 156 VD-------ELNQALIPLDILIGSRLDPGELVVAEKI--AGPFPR-----YLIVTEGELGAILYPGG------RYNHVPA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2569245018 267 VRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHG 314
Cdd:cd01947 216 KKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| PLN02967 |
PLN02967 |
kinase |
4-213 |
3.20e-09 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 59.67 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 4 QFDVICMGRVAVDLYSQQIGARLEDV----SSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCD 79
Cdd:PLN02967 206 QHAFVPSGRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 80 TSHLITDKDRLTALVLLGIKDRDTFPLIFYRDnCADMAITASDVDESYIASARCLAITGTHLSHPQTREAVLTALGYARR 159
Cdd:PLN02967 286 TRSVCIDGKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKK 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2569245018 160 HGVRTVLDIDYRPVLWGLTSlgdgETRFIaadkvtreLQEVLHLFDVIVGTEEE 213
Cdd:PLN02967 365 LGGVIFYDLNLPLPLWSSSE----ETKSF--------IQEAWNLADIIEVTKQE 406
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
7-311 |
4.19e-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: 58.09 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 7 VICMGRVAVDLYSQ-----QIGARLEDVSSFAkyLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTs 81
Cdd:cd01941 2 IVVIGAANIDLRGKvsgslVPGTSNPGHVKQS--PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 82 HLITDKDRLTALVLLgIKDRDTFPLIfyrdNCADMAI----TASDVD--ESYIASARCLAITGtHLShpqtREAVLTALG 155
Cdd:cd01941 79 RGIVFEGRSTASYTA-ILDKDGDLVV----ALADMDIyellTPDFLRkiREALKEAKPIVVDA-NLP----EEALEYLLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 156 YARRHGVRTVLDidyrPVlwgltslgdgetrfiAADKVTReLQEVLHLFDVIVGTEEEF-----HIAGGSTDTLRALEQV 230
Cdd:cd01941 149 LAAKHGVPVAFE----PT---------------SAPKLKK-LFYLLHAIDLLTPNRAELealagALIENNEDENKAAKIL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 231 RGVSQATLVCKRGA-------LGCSVYPDTIPHRLDDgltvtgvrvEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYAN 303
Cdd:cd01941 209 LLPGIKNVIVTLGAkgvllssREGGVETKLFPAPQPE---------TVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQ 279
|
....*...
gi 2569245018 304 ACGALVVS 311
Cdd:cd01941 280 AAAALTLE 287
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
124-290 |
1.27e-08 |
|
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: 55.18 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 124 DESYIASARCLAITGTHLShpqtREAVLTALGYARRHGVRTVLDIDYRpvlwgltslgdgetrfiAADKVTRELQEVLHL 203
Cdd:cd00287 51 VSVTLVGADAVVISGLSPA----PEAVLDALEEARRRGVPVVLDPGPR-----------------AVRLDGEELEKLLPG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 204 FDVIVGTEEEFHIAGG-----STDTLRALEQVRGVSQATLVCKRGALGCSVYpdtipHRLDDGLTVTGVRVEVLNVLGAG 278
Cdd:cd00287 110 VDILTPNEEEAEALTGrrdleVKEAAEAAALLLSKGPKVVIVTLGEKGAIVA-----TRGGTEVHVPAFPVKVVDTTGAG 184
|
170
....*....|..
gi 2569245018 279 DAFMSGLLRGYL 290
Cdd:cd00287 185 DAFLAALAAGLA 196
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
157-314 |
1.29e-08 |
|
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: 56.77 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 157 ARRHGVRTVLDIDYRPVLWGLTSLGDgetrFIAADkvTRELQEvlhLFDVIVGTEEefhiaggstDTLRALEQVRGVSQA 236
Cdd:cd01164 154 AREKGARVILDTSGEALLAALAAKPF----LIKPN--REELEE---LFGRPLGDEE---------DVIAAARKLIERGAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569245018 237 TLVCKRGALGcSVYPDTiphrlDDGLTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHG 314
Cdd:cd01164 216 NVLVSLGADG-ALLVTK-----DGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
60-323 |
8.97e-07 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 51.18 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 60 VGDEHMGRFLREELNQVGCDTsHLITDKDRLTAL--VLLGIKDRDTFPLIfYRDNCADMAITASDVDESYIASARCLAIT 137
Cdd:PTZ00247 89 VGDDRFAEILKEAAEKDGVEM-LFEYTTKAPTGTcaVLVCGKERSLVANL-GAANHLSAEHMQSHAVQEAIKTAQLYYLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 138 GTHLShpqTR-EAVLTALGYARRHGVRTVLdidyrpvlwGLTSLgdgetrFIAADkVTRELQEVLHLFDVIVGTEEEFHI 216
Cdd:PTZ00247 167 GFFLT---VSpNNVLQVAKHARESGKLFCL---------NLSAP------FISQF-FFERLLQVLPYVDILFGNEEEAKT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 217 AG-----GSTDTLR------ALEQVRGVSQATLVCKRGAlgcsvYPDTIPHRldDGLTVTGVRV----EVLNVLGAGDAF 281
Cdd:PTZ00247 228 FAkamkwDTEDLKEiaariaMLPKYSGTRPRLVVFTQGP-----EPTLIATK--DGVTSVPVPPldqeKIVDTNGAGDAF 300
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2569245018 282 MSGLLRGYLNDEGWEQACRYANACGALVVSRHGCA-PAMPSKI 323
Cdd:PTZ00247 301 VGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKPPFL 343
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
157-324 |
1.26e-06 |
|
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: 50.67 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 157 ARRHGVRTVLD---------IDYRPVLwgltslgdgetrfIAADKvtRELQEvlhLFDVIVGTEEEFhiaggsTDTLRAL 227
Cdd:TIGR03828 153 AREKGAKVILDtsgealrdgLKAKPFL-------------IKPND--EELEE---LFGRELKTLEEI------IEAAREL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 228 eQVRGVsQATLVcKRGALGcSVYPDTiphrlDDGLTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGA 307
Cdd:TIGR03828 209 -LDLGA-ENVLI-SLGADG-ALLVTK-----EGALFAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGS 279
|
170
....*....|....*..
gi 2569245018 308 LVVSRHGCAPAMPSKIE 324
Cdd:TIGR03828 280 AAAFSEGTGLPDPEDIE 296
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
29-314 |
6.80e-06 |
|
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: 48.19 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 29 VSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGcdTSHLITDKdrltalvllgikdrdtfplif 108
Cdd:cd01944 27 EAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEG--IEILLPPR--------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 109 YRDNCAD-MAITASDVDESYIASARCLAITGTHLSH---PQTREAVLTALGYARRHGVRTVLDIDYrpvlwgLTSLGDGE 184
Cdd:cd01944 84 GGDDGGClVALVEPDGERSFISISGAEQDWSTEWFAtltVAPYDYVYLSGYTLASENASKVILLEW------LEALPAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 185 TRFIAADKVTRE-----LQEVLHLFDVIVGTEEEFHIAGGSTDTLRALEQVRGVSQ--ATLVCKRGALGCSVY-PDTIPH 256
Cdd:cd01944 158 TLVFDPGPRISDipdtiLQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKtaAPVVVRLGSNGAWIRlPDGNTH 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2569245018 257 rlddglTVTGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHG 314
Cdd:cd01944 238 ------IIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
16-175 |
1.42e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 47.98 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 16 DLYSQQigARLE-DVSSFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELNQVGCDTSHLITDKDRLTALV 94
Cdd:PLN02543 152 DMYSQW--KMLQwDPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569245018 95 LLGIKDRDTFPLIFYR-DNCADMAITASDVDESYIASARCLAITGTHLSHPQTREAVLTALGYARRHGVRTVLDIDYRPV 173
Cdd:PLN02543 230 RMKIKFRDGGKMVAETvKEAAEDSLLASELNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLP 309
|
..
gi 2569245018 174 LW 175
Cdd:PLN02543 310 LW 311
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
271-314 |
6.19e-04 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 42.33 E-value: 6.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2569245018 271 VLNVLGAGDAFMSGLLRGYLNDEGWEQACRYANACGALVVSRHG 314
Cdd:cd01943 260 VVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| |
