|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
3-639 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1137.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 3 TQQKRLDVICIGRIAVDLYGQQIGARLEDMSTFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGAD 82
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 83 TECLITDKTRLTGLVILGIKDQDTFPLVFYRDNCADMGLTPEDIQEDYIASSRAVAVTGTHLSHPDTRAAVLKALDIARR 162
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 163 HGLRTALDIDYRPVLWGLTSLGDGETRFIESSHVTQQLQEVLHYFDLVVGTEEEFHIAGGSTDTLTALKNVRQATKATLV 242
Cdd:COG3892 161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 243 CKRGALGCVVLEGEIPTSWEQTKLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCAPAM 322
Cdd:COG3892 241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 323 PTKAELDDFLSRDKEVKRPDLDSRLNHLHRVTTRKQQWPELCVFAFDHRKQLVDMANEAGVDTTRLPELKTLLLRAAQEA 402
Cdd:COG3892 321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 403 ATEAGLDRRSGILADTTFGQSTLNAITGKGWWIGRPIEMPGSRPLRLEHG-NIGSQLVDWPQEHVVKCLVFYHPHDSAEL 481
Cdd:COG3892 401 AAGAGLRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGrDIGSQLVEWPQEHVVKCLVFYHPDDPAEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 482 RKEQDELILDVWQGCNKTGHELLLEVILPENNPDkQESYYLEMLSHFYSLGIQPDWWKLPPLSLESWQAISGLIEQQDPW 561
Cdd:COG3892 481 RLEQEAQLRRLYDACRRSGHELLLEVIPPKDGPV-DDDTVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAERDPY 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2265705738 562 CRGILILGLDAPEEKLKAGFAAAAQAPWVKGFAVGRTIFGQPSRQWLQGELNDEALIAEVKGNYLRLIDYWREVRPAT 639
Cdd:COG3892 560 CRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQAA 637
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
327-636 |
3.60e-180 |
|
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: 512.60 E-value: 3.60e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 327 ELDDFLSRDKEVKRPDLDSRLNHLHRVTTRKQQWPELCVFAFDHRKQLVDMANEAGVDTTRLPELKTLLLRAAQEAATEA 406
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 407 GLDRRSGILADTTFGQSTLNAITGKGWWIGRPIEMPGSRPLRLEHG-NIGSQLVDWPQEHVVKCLVFYHPHDSAELRKEQ 485
Cdd:pfam09863 81 GLQGGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGrSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 486 DELILDVWQGCNKTGHELLLEVILPENNPDKqESYYLEMLSHFYSLGIQPDWWKLPPLSLESWQAISGLIEQQDPWCRGI 565
Cdd:pfam09863 161 EAQLRELYDACRKSGHELLLEVIPPKDGPVD-DETYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYCRGV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265705738 566 LILGLDAPEEKLKAGFAAAAQAPWVKGFAVGRTIFGQPSRQWLQGELNDEALIAEVKGNYLRLIDYWREVR 636
Cdd:pfam09863 240 VILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
7-332 |
2.32e-163 |
|
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: 469.77 E-value: 2.32e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 7 RLDVICIGRIAVDLYGQQIGARLEDMSTFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECL 86
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 87 ITDKTRLTGLVILGIKDQDTFPLVFYRDNCADMGLTPEDIQEDYIASSRAVAVTGTHLSHPDTRAAVLKALDIARRHGLR 166
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 167 TALDIDYRPVLWGltslgdgetrfiESSHVTQQLQEVLHYFDLVVGTEEEFHIAGGSTDTLTALKNVRQATKATLVCKRG 246
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 247 ALGCVVLEGEiPTSWEqtklQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCAPAMPTKA 326
Cdd:TIGR04382 229 PEGSLVYTGD-GEGVE----VPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 2265705738 327 ELDDFL 332
Cdd:TIGR04382 304 ELEAFL 309
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
9-328 |
1.14e-85 |
|
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: 270.22 E-value: 1.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 9 DVICIGRIAVDLYGQ----QIGARLEDMSTFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTE 84
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 85 CLITDKTRLTGLVILGIKDQDTFPLVFYRdnCADMGLTPEDIQEDYIASSRAVAVTGTHLSHPDTRAAVLKALDIARRHG 164
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 165 LRTALDIDYRPVLWgltslgdgetrfiesSHVTQQLQEVLHYFDLVVGTEEEFHIAGGSTDTLTALKNVRQATKATLVCK 244
Cdd:COG0524 159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 245 RGALGCVVLEGEiptsweQTKLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCAPAMPT 324
Cdd:COG0524 224 LGAEGALLYTGG------EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 2265705738 325 KAEL 328
Cdd:COG0524 298 REEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-319 |
8.89e-84 |
|
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: 264.82 E-value: 8.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 9 DVICIGRIAVDLYGQQIGaRLEDMSTFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECLIT 88
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 89 DKTRLTGLVILGIKDQDTFPLVFYRDNCADMGLTPEDIQEDYIASSRAVAVTGTHLS-HPDTRAAVLKALDIARRHGLRT 167
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 168 ALDIDYRPVLWGLtslgdGETRfiesshvtQQLQEVLHYFDLVVGTEEEFHIAGGSTDTLTALKNVRQATK--ATLVCKR 245
Cdd:cd01166 160 SFDLNYRPKLWSA-----EEAR--------EALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALgvKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265705738 246 GALGCVVLEGeiptswEQTKLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCA 319
Cdd:cd01166 227 GAEGALVYTG------GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
10-317 |
1.22e-47 |
|
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: 169.35 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 10 VICIGRIAVDLYGQQIGARLedmsTFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECLITD 89
Cdd:cd01167 2 VVCFGEALIDFIPEGSGAPE----TFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 90 KTRLTGLVILGIKDQD--TFplVFYRDNCADMGLTPEdIQEDYIASSRAVaVTGTH-LSHPDTRAAVLKALDIARRHGLR 166
Cdd:cd01167 78 PAAPTTLAFVTLDADGerSF--EFYRGPAADLLLDTE-LNPDLLSEADIL-HFGSIaLASEPSRSALLELLEAAKKAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 167 TALDIDYRPVLWgltslGDGETRFiesshvtQQLQEVLHYFDLVVGTEEEFHIAGGSTDTLTALKNVRQATKATLVCKRG 246
Cdd:cd01167 154 ISFDPNLRPPLW-----RDEEEAR-------ERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 247 ALGCVVL----EGEIPtsweqtklqsGVRVEVLNVLGAGDAFMSGLLRG-------WLNDESWEQACRYANACGALVVSR 315
Cdd:cd01167 222 ADGALLYtkggVGEVP----------GIPVEVVDTTGAGDAFVAGLLAQllsrgllALDEDELAEALRFANAVGALTCTK 291
|
..
gi 2265705738 316 HG 317
Cdd:cd01167 292 AG 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
9-319 |
9.07e-44 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 158.66 E-value: 9.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 9 DVICIGRIAVDLYGQQIGARLEDM--STFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECL 86
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELVrvSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 87 ITDKTRLTGL-VILGIKDQDTFpLVFYRDNCADMGLTPEDIQEDYIASSRAVAVTGTHLshPDTRAAVLKALDIARRHGl 165
Cdd:pfam00294 81 VIDEDTRTGTaLIEVDGDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISGSLP--LGLPEATLEELIEAAKNG- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 166 rTALDIDYRPVLWGltslgdgetrfiesshVTQQLQEVLHYFDLVVGTEEEFHIAGGST-----DTLTALKNVRQATKAT 240
Cdd:pfam00294 157 -GTFDPNLLDPLGA----------------AREALLELLPLADLLKPNEEELEALTGAKlddieEALAALHKLLAKGIKT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2265705738 241 LVCKRGALGCVVLEGEiptswEQTKLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCA 319
Cdd:pfam00294 220 VIVTLGADGALVVEGD-----GEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
7-318 |
1.10e-29 |
|
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: 119.64 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 7 RLDVICIGRIAVDL-----------YGQQIG-ARLEDMSTF--------SKYL-GGSSGNVAYGTAIQGLKSGMLARVGD 65
Cdd:cd01168 1 RYDVLGLGNALVDIlaqvddaflekLGLKKGdMILADMEEQeellaklpVKYIaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 66 EHMGRFLREELQRVGADTECLITDKTRlTG--LVILGIKDQDTfpLVFYRDNCADmgLTPEDIQEDYIASSRAVAVTGTH 143
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTRYQVQPDGP-TGtcAVLVTPDAERT--MCTYLGAANE--LSPDDLDWSLLAKAKYLYLEGYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 144 LSHPDtrAAVLKALDIARRHGLRTALDIdyrpvlwgltSLGDGETRFiesshvTQQLQEVLHYFDLVVGTEEEFHIAGGS 223
Cdd:cd01168 156 LTVPP--EAILLAAEHAKENGVKIALNL----------SAPFIVQRF------KEALLELLPYVDILFGNEEEAEALAEA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 224 --TDTLTALKNVRQATKATLVCKRGALGCVVLEGE----IPTSWEqtklqsgvrVEVLNVLGAGDAFMSGLLRGWLNDES 297
Cdd:cd01168 218 etTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGevypVPAIPV---------EKIVDTNGAGDAFAGGFLYGLVQGEP 288
|
330 340
....*....|....*....|.
gi 2265705738 298 WEQACRYANACGALVVSRHGC 318
Cdd:cd01168 289 LEECIRLGSYAAAEVIQQLGP 309
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
9-318 |
3.61e-28 |
|
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: 114.33 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 9 DVICIGRIAVDLYGQQIGARLEDMSTFSK----YLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTE 84
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 85 CLITDKTRLTGLVILGIKDQDTFPLVFYRDncADMGLTPEDIqEDYIASSRAVavtgthlsHPDTRAAVLKALDIARRHG 164
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDNQIAYFYPG--AMDELEPNDE-ADPDGLADIV--------HLSSGPGLIELARELAAGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 165 LRTALDidyrP--VLWGLTslGDGETRFIESSHVtqqlqevlhyfdlVVGTEEEFHIAggstDTLTALKNVRQATKA-TL 241
Cdd:cd01942 150 ITVSFD----PgqELPRLS--GEELEEILERADI-------------LFVNDYEAELL----KERTGLSEAELASGVrVV 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2265705738 242 VCKRGALGCVVLEGEiptswEQTKLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGC 318
Cdd:cd01942 207 VVTLGPKGAIVFEDG-----EEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
40-329 |
3.74e-27 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 111.95 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 40 GGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECLITDKTRLTGLVILGIKDQDTFPLVFYRDNCADM 119
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 120 GLTPEDI----QEDY-----IAssravavtgthLSHPDTRAAVLKALDIARRHGLRTALDIDYRPVLWGLTSlgdgETRf 190
Cdd:PRK09434 108 FLQPQDLppfrQGEWlhlcsIA-----------LSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWQDEA----ELR- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 191 iesshvtQQLQEVLHYFDLVVGTEEEFHIAGGSTDTLTALKNVRQATKATLV-CKRGALG-CVVLEGeiptsweQTKLQS 268
Cdd:PRK09434 172 -------ECLRQALALADVVKLSEEELCFLSGTSQLEDAIYALADRYPIALLlVTLGAEGvLVHTRG-------QVQHFP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2265705738 269 GVRVEVLNVLGAGDAFMSGLLRG------WLNDESWEQACRYANACGALVVSRHGCAPAMPTKAELD 329
Cdd:PRK09434 238 APSVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
10-337 |
6.11e-27 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 112.02 E-value: 6.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 10 VICIGRIAVDLYGQQIGARLEDMSTFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECLITD 89
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 90 KTRLTGLVILGIKDQDTFPLVFYRDNCADMGLTPEDIQEDYIASSRAVAVTGTHLSHPDTRAAVLKALDIARRHGLRTAL 169
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 170 DIDYRPVLW--------GLTSLGDgETRFIESSHVtqqlqevlhyfdlvvgtEEEFHIAGGSTDTLTALKNVRQATKATL 241
Cdd:PLN02323 173 DPNLRLPLWpsaeaareGIMSIWD-EADIIKVSDE-----------------EVEFLTGGDDPDDDTVVKLWHPNLKLLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 242 VCKrGALGCV----VLEGEIPtsweqtklqsGVRVEVLNVLGAGDAFMSGLL------RGWLNDES-WEQACRYANACGA 310
Cdd:PLN02323 235 VTE-GEEGCRyytkDFKGRVE----------GFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRFANACGA 303
|
330 340
....*....|....*....|....*..
gi 2265705738 311 LVVSRHGCAPAMPTKAELDDFLSRDKE 337
Cdd:PLN02323 304 ITTTERGAIPALPTKEAVLKLLKKAVA 330
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
9-324 |
7.55e-25 |
|
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: 104.94 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 9 DVICIGRIAVDLYgqqigARLEDM---------STFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRV 79
Cdd:cd01174 1 KVVVVGSINVDLV-----TRVDRLpkpgetvlgSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 80 GADTECLITDKTRLTGL-VIlgIKDQDtfplvfyRDNC------ADMGLTPEDI--QEDYIASSRAVavtGTHLSHPDtr 150
Cdd:cd01174 76 GIDVSYVEVVVGAPTGTaVI--TVDES-------GENRivvvpgANGELTPADVdaALELIAAADVL---LLQLEIPL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 151 AAVLKALDIARRHGLRTALDidyrpvlwgltslgdgetrfieSSHVTQQLQEVLHYFDLVVGTEEEFHIAGGSTDT---- 226
Cdd:cd01174 142 ETVLAALRAARRAGVTVILN----------------------PAPARPLPAELLALVDILVPNETEAALLTGIEVTdeed 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 227 -LTALKNVRQATKATLVCKRGALGCVVLEGEiptsweQTKLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYA 305
Cdd:cd01174 200 aEKAARLLLAKGVKNVIVTLGAKGALLASGG------EVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFA 273
|
330
....*....|....*....
gi 2265705738 306 NACGALVVSRHGCAPAMPT 324
Cdd:cd01174 274 NAAAALSVTRPGAQPSIPT 292
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
9-328 |
1.29e-15 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 9 DVICIGRIAVDLYG-----QQIGARLEDMStFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADT 83
Cdd:PTZ00292 17 DVVVVGSSNTDLIGyvdrmPQVGETLHGTS-FHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 84 ECLITDKTRLTGL--VILGIKDQDTFPLVFYRDNCAdmgLTPEDI--QEDYIASSRAVAVTGTHLSHPDTraavLKALDI 159
Cdd:PTZ00292 96 SFVSRTENSSTGLamIFVDTKTGNNEIVIIPGANNA---LTPQMVdaQTDNIQNICKYLICQNEIPLETT----LDALKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 160 ARRHGLRTALDIDYRPvlwgltslgdgetrfieSSHVTQQLQEVLHYFDLVVGTEEEFHIAGGSTdtLTALKNVRQATKA 239
Cdd:PTZ00292 169 AKERGCYTVFNPAPAP-----------------KLAEVEIIKPFLKYVSLFCVNEVEAALITGME--VTDTESAFKASKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 240 TL-------VCKRGALGCVVLEGEIPTSWEQtklqsGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALV 312
Cdd:PTZ00292 230 LQqlgvenvIITLGANGCLIVEKENEPVHVP-----GKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAIS 304
|
330
....*....|....*.
gi 2265705738 313 VSRHGCAPAMPTKAEL 328
Cdd:PTZ00292 305 VTRHGTQSSYPHPSEL 320
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
9-324 |
1.39e-15 |
|
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: 77.72 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 9 DVICIGRIAVDLYgqqigARLEDMSTFS-KYL--------GGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRV 79
Cdd:cd01945 1 RVLGVGLAVLDLI-----YLVASFPGGDgKIVatdyavigGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 80 GADTECLITDKTRLTGL-VILGIKDQDTFPLVFYRDNCADMGLTPEDIqedyIASSRAVAVTGtHLshpdtRAAVLKALD 158
Cdd:cd01945 76 GVDTSFIVVAPGARSPIsSITDITGDRATISITAIDTQAAPDSLPDAI----LGGADAVLVDG-RQ-----PEAALHLAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 159 IARRHGLRTALDIDyrpvlwgltslGDGETrfiesshvtqQLQEVLHYFDLVVGTEEEFHIAGGSTDTLtALKNVRQATK 238
Cdd:cd01945 146 EARARGIPIPLDLD-----------GGGLR----------VLEELLPLADHAICSENFLRPNTGSADDE-ALELLASLGI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 239 ATLVCKRGALGCVVLEgeiptswEQTKLQSGV--RVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRH 316
Cdd:cd01945 204 PFVAVTLGEAGCLWLE-------RDGELFHVPafPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGL 276
|
....*...
gi 2265705738 317 GCAPAMPT 324
Cdd:cd01945 277 GGRAGLPT 284
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
67-334 |
5.04e-14 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 73.25 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 67 HMGRFLREELQRVGADTECL-ITDKTRlTGLVILGIKDQDTFPLVFYrdncadmG--LTPEDIQE------DYIASSRAV 137
Cdd:COG1105 61 FTGEFIEELLDEEGIPTDFVpIEGETR-INIKIVDPSDGTETEINEP-------GpeISEEELEAllerleELLKEGDWV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 138 AVTGthlSHP-----DTRAAVLKaldIARRHGLRTALDidyrpvlwglTSlgdGETrfiesshvtqqLQEVLHY-FDLVV 211
Cdd:COG1105 133 VLSG---SLPpgvppDFYAELIR---LARARGAKVVLD----------TS---GEA-----------LKAALEAgPDLIK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 212 GTEEEF-HIAGGSTDTLTALknVRQATKatlVCKRGAlGCVVL----EGEIPTSWEQTKLQSGVRVEVLNVLGAGDAFMS 286
Cdd:COG1105 183 PNLEELeELLGRPLETLEDI--IAAARE---LLERGA-ENVVVslgaDGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2265705738 287 GLLRGWLNDESWEQACRYANACGALVVSRHGcaPAMPTKAELDDFLSR 334
Cdd:COG1105 257 GFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELLAQ 302
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
40-333 |
5.15e-13 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 70.28 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 40 GGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECLITDKTRLTGLVILGIKDQDtfplvfyrDNC--- 116
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEG--------ENSigi 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 117 ---ADMGLTPEDIQEDY--IASSRAVAVtgtHLSHPdtRAAVLKALDIARRHGLRTALDidyrPVlwGLTSLGDgetrfi 191
Cdd:PRK11142 111 hagANAALTPALVEAHRelIANADALLM---QLETP--LETVLAAAKIAKQHGTKVILN----PA--PARELPD------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 192 esshvtqqlqEVLHYFDLVVGTEEEfhiaggsTDTLT--ALKNVRQATKATLVCKRGALGCVVL----EGEIPTSWEQTK 265
Cdd:PRK11142 174 ----------ELLALVDIITPNETE-------AEKLTgiRVEDDDDAAKAAQVLHQKGIETVLItlgsRGVWLSENGEGQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2265705738 266 LQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCAPAMPTKAELDDFLS 333
Cdd:PRK11142 237 RVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
59-334 |
2.23e-12 |
|
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: 68.37 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 59 MLARVGDE---------HMGRFLREELQRVGADTECL-ITDKTRLTglVILGIKDQDTFPLVFYrdncadmG--LTPEDI 126
Cdd:TIGR03168 44 VLARLGAEvvatgflggFTGEFIEALLAEEGIKNDFVeVKGETRIN--VKIKESSGEETELNEP-------GpeISEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 127 QE------DYIASSRAVAVTGthlSHP---DTRAAVlKALDIARRHGLRTALD---------IDYRPVLwgltslgdget 188
Cdd:TIGR03168 115 EQlleklrELLASGDIVVISG---SLPpgvPPDFYA-QLIAIARKKGAKVILDtsgealreaLAAKPFL----------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 189 rfIESSHvtqqlQEVLHYFDLVVGTEEEfhiaggstdtltalknVRQATKATLvcKRGAlGCVVL----EGEIPTSWEQT 264
Cdd:TIGR03168 180 --IKPNH-----EELEELFGRELKTLEE----------------IIEAARELL--DRGA-ENVLVslgaDGALLVTKEGA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 265 KLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGcaPAMPTKAELDDFLSR 334
Cdd:TIGR03168 234 LKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLPDPEDVEELLDQ 301
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
10-314 |
2.99e-12 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 67.72 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 10 VICIGRIAVDLYGQ-----QIGARLEDMSTFSkyLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTE 84
Cdd:cd01941 2 IVVIGAANIDLRGKvsgslVPGTSNPGHVKQS--PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 85 CLITDKTRlTGlvilgikdqdTFPLVFYRDN-----CADMG----LTPEDIQ--EDYIASSRAVAVTGtHLSHPdtraAV 153
Cdd:cd01941 80 GIVFEGRS-TA----------SYTAILDKDGdlvvaLADMDiyelLTPDFLRkiREALKEAKPIVVDA-NLPEE----AL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 154 LKALDIARRHGLRTALDidyrPVlwgltslgdgetrfieSSHVTQQLQEVLHYFDLVVGTEEEF-----HIAGGSTDTLT 228
Cdd:cd01941 144 EYLLALAAKHGVPVAFE----PT----------------SAPKLKKLFYLLHAIDLLTPNRAELealagALIENNEDENK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 229 ALKNVRQATKATLVCKRGALGcVVLEGEIPTSWEQTKLQSGVRvEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANAC 308
Cdd:cd01941 204 AAKILLLPGIKNVIVTLGAKG-VLLSSREGGVETKLFPAPQPE-TVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAA 281
|
....*.
gi 2265705738 309 GALVVS 314
Cdd:cd01941 282 AALTLE 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
10-328 |
5.79e-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: 66.81 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 10 VICIGRIAVD--LYGQQIGARLE------DMSTFSKYLGGSsGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGA 81
Cdd:cd01172 2 VLVVGDVILDeyLYGDVERISPEapvpvvKVEREEIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 82 DTEcLITDKTRLT---------GLVILGIKDQDTFPLvfyrdncadmgltPEDIQEdyiassRAVAVTGTHLSHPD---- 148
Cdd:cd01172 81 DTD-GIVDEGRPTttktrviarNQQLLRVDREDDSPL-------------SAEEEQ------RLIERIAERLPEADvvil 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 149 --------TRAAVLKALDIARRHGLRTALDidyrpvlwgltSLGDGETRFIESSHVTQQLQEVLHYFDLVVGTEEEFhia 220
Cdd:cd01172 141 sdygkgvlTPRVIEALIAAARELGIPVLVD-----------PKGRDYSKYRGATLLTPNEKEAREALGDEINDDDEL--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 221 ggstdtLTALKNVRQATKATLVC-KRGALGCVVLEGE-----IPTsweqtklqsgVRVEVLNVLGAGDAFMSGLLRGWLN 294
Cdd:cd01172 207 ------EAAGEKLLELLNLEALLvTLGEEGMTLFERDgevqhIPA----------LAKEVYDVTGAGDTVIATLALALAA 270
|
330 340 350
....*....|....*....|....*....|....
gi 2265705738 295 DESWEQACRYANACGALVVSRHGCAPAmpTKAEL 328
Cdd:cd01172 271 GADLEEAAFLANAAAGVVVGKVGTAPV--TPKEL 302
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
10-317 |
1.28e-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: 65.45 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 10 VICIGRIAVDLYGQQIGArledmstfskYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTE-CLIt 88
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDIShCRV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 89 dKTRLTGLVILGIKDQDTfplVFYRDN---CADMGLTPEDIQedYIASSRAVavtgtHLSHPDTRAAVLKALDIARRHGL 165
Cdd:cd01940 71 -KEGENAVADVELVDGDR---IFGLSNkggVAREHPFEADLE--YLSQFDLV-----HTGIYSHEGHLEKALQALVGAGA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 166 RTALDIDYRpvlwgltslgdgetrfiessHVTQQLQEVLHYFDLVVGTEEEFhiagGSTDTLTALKNVRQATKATLVCKR 245
Cdd:cd01940 140 LISFDFSDR--------------------WDDDYLQLVCPYVDFAFFSASDL----SDEEVKAKLKEAVSRGAKLVIVTR 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2265705738 246 GALGCVVLEGEIPTSWeqtklqSGVRVEVLNVLGAGDAFMSGLLRGWL-NDESWEQACRYANACGALVVSRHG 317
Cdd:cd01940 196 GEDGAIAYDGAVFYSV------APRPVEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
10-317 |
3.91e-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: 63.98 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 10 VICIGRIAVDLYGQ-----QIGARLEdMSTFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTE 84
Cdd:cd01947 2 IAVVGHVEWDIFLSldappQPGGISH-SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 85 CLITDK-TRLTGLVIlgikDQDTFPLVFY-RDNCADMGLTPEdiqedyIASSRAVAVTGthlshpdtrAAVLK-ALDIAR 161
Cdd:cd01947 81 VAWRDKpTRKTLSFI----DPNGERTITVpGERLEDDLKWPI------LDEGDGVFITA---------AAVDKeAIRKCR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 162 RHGLrtaldidyrpVLWGLTslgdGETRFIESSHVTQQlqevlhyFDLVVGTEEEFhiAGGSTDTLTALKNVRqatkaTL 241
Cdd:cd01947 142 ETKL----------VILQVT----PRVRVDELNQALIP-------LDILIGSRLDP--GELVVAEKIAGPFPR-----YL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 242 VCKRGALGCVVLEG----EIPTsweqtklqsgVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHG 317
Cdd:cd01947 194 IVTEGELGAILYPGgrynHVPA----------KKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
137-293 |
1.27e-09 |
|
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: 58.26 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 137 VAVTGTHLSHPD----TRAAVLKALDIARRHGLRTALDidyrpvlwgltsLGDGETRFIEsshvtQQLQEVLHYFDLVVG 212
Cdd:cd00287 53 VTLVGADAVVISglspAPEAVLDALEEARRRGVPVVLD------------PGPRAVRLDG-----EELEKLLPGVDILTP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 213 TEEEFHIAGGSTDTLTALKNVRQATKA-----TLVCKRGALGCVVL-----EGEIPTsweqtklqsgVRVEVLNVLGAGD 282
Cdd:cd00287 116 NEEEAEALTGRRDLEVKEAAEAAALLLskgpkVVIVTLGEKGAIVAtrggtEVHVPA----------FPVKVVDTTGAGD 185
|
170
....*....|.
gi 2265705738 283 AFMSGLLRGWL 293
Cdd:cd00287 186 AFLAALAAGLA 196
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
10-317 |
3.41e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 58.21 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 10 VICIGRIAVDLYgQQIGarledmstfSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECLITD 89
Cdd:PRK09813 3 LATIGDNCVDIY-PQLG---------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 90 KTRlTGLVILGIKDQDTfplVF--YRDNC-ADMGLTPEDIqeDYIASSRAVaVTGThLSHPDtraAVLKALdiaRRHGLR 166
Cdd:PRK09813 73 HGV-TAQTQVELHDNDR---VFgdYTEGVmADFALSEEDY--AWLAQYDIV-HAAI-WGHAE---DAFPQL---HAAGKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 167 TALDIDYRPvlwgltslgdgetrfieSSHVTQQLQEVLHYfdlvvgteeEFHIAGGSTDTLtalknvRQATKAtlVCKRG 246
Cdd:PRK09813 139 TAFDFSDKW-----------------DSPLWQTLVPHLDY---------AFASAPQEDEFL------RLKMKA--IVARG 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265705738 247 ALGCVVLEGEIPT-SWEQTKLQSG--VRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHG 317
Cdd:PRK09813 185 AGVVIVTLGENGSiAWDGAQFWRQapEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
68-317 |
5.34e-09 |
|
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: 57.93 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 68 MGRFLREELQRVGADTECL-ITDKTRlTGLVILGIKDQDTfplvfyRDNCADMGLTPEDIQ------EDYIASSRAVAVT 140
Cdd:cd01164 63 TGDFFEALLKEEGIPDDFVeVAGETR-INVKIKEEDGTET------EINEPGPEISEEELEalleklKALLKKGDIVVLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 141 GTHLSH--PDTRAAVLKaldIARRHGLRTALDIDYRPvlwgltslgdgetrfiesshvtqqLQEVLHYF-DLVVGTEEEF 217
Cdd:cd01164 136 GSLPPGvpADFYAELVR---LAREKGARVILDTSGEA------------------------LLAALAAKpFLIKPNREEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 218 H-IAGGSTDTLTALKNVrqatkATLVCKRGAlGCVVL----EGEIPTSWEQTKLQSGVRVEVLNVLGAGDAFMSGLLRGW 292
Cdd:cd01164 189 EeLFGRPLGDEEDVIAA-----ARKLIERGA-ENVLVslgaDGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGL 262
|
250 260
....*....|....*....|....*
gi 2265705738 293 LNDESWEQACRYANACGALVVSRHG 317
Cdd:cd01164 263 AQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
157-334 |
1.71e-08 |
|
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: 56.44 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 157 LDIARRHGLRTALD---------IDYRPVLwgltslgdgetrfIESSHvtqqlQEVLHYFDLVVGTEEEFhiaggstdTL 227
Cdd:TIGR03828 150 IALAREKGAKVILDtsgealrdgLKAKPFL-------------IKPND-----EELEELFGRELKTLEEI--------IE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 228 TALKNVRQATKATLVcKRGALGCVVLEGEiptsweQTKLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANA 307
Cdd:TIGR03828 204 AARELLDLGAENVLI-SLGADGALLVTKE------GALFAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVA 276
|
170 180
....*....|....*....|....*..
gi 2265705738 308 CGALVVSRHGcaPAMPTKAELDDFLSR 334
Cdd:TIGR03828 277 AGSAAAFSEG--TGLPDPEDIEELLPQ 301
|
|
| PLN02967 |
PLN02967 |
kinase |
14-216 |
3.08e-07 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 53.51 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 14 GRIAVDLYGQQIGARLEDM----STFSKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTECLITD 89
Cdd:PLN02967 213 GRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCID 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 90 KTRLTGLVILGIKDQDTFPLVFYRDnCADMGLTPEDIQEDYIASSRAVAVTGTHLSHPDTRAAVLKALDIARRHGLRTAL 169
Cdd:PLN02967 293 GKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFY 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2265705738 170 DIDYRPVLWgltslgdgetrfiESSHVTQQL-QEVLHYFDLVVGTEEE 216
Cdd:PLN02967 372 DLNLPLPLW-------------SSSEETKSFiQEAWNLADIIEVTKQE 406
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
40-324 |
3.89e-07 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 52.63 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 40 GGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADteclITDKTRLTGlvilgiKDQDTFplvfyrdncadm 119
Cdd:PRK09954 93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVN----VSGCIRLHG------QSTSTY------------ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 120 gLTPEDIQEDYIassraVAVTGTHLSHPDTRAAVLKALDIARRHGLRTAlDIDYRP--VLWGLTsLGDGETRFIE--SSH 195
Cdd:PRK09954 151 -LAIANRQDETV-----LAINDTHILQQLTPQLLNGSRDLIRHAGVVLA-DCNLTAeaLEWVFT-LADEIPVFVDtvSEF 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 196 VTQQLQEVLHYFDLVVGTEEEFHIAGGS-----TDTLTALKNV-RQATKATLVC-KRGALGCVVLEGE--IPTSWEQTKL 266
Cdd:PRK09954 223 KAGKIKHWLAHIHTLKPTQPELEILWGQaitsdADRNAAVNALhQQGVQQIFVYlPDESVFCSEKDGEqfLLTAPAHTTV 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2265705738 267 QSgvrvevlnvLGAGDAFMSGLLRGWLNDESWEQACRYANACGALvvSRHGCAPAMPT 324
Cdd:PRK09954 303 DS---------FGADDGFMAGLVYSFLEGYSFRDSARFAMACAAI--SRASGSLNNPT 349
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
37-317 |
2.06e-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: 49.73 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 37 KYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGadTECLITDKTRLTGLVILGIKDQD---TFpLVFYR 113
Cdd:cd01944 32 SYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEG--IEILLPPRGGDDGGCLVALVEPDgerSF-ISISG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 114 dncADMGLTPEDIQEDYIASSRAVAVTGTHLSHPDTRAAVLKAL--DIARRhglrTALDIDYRPVLwglTSLGDGEtrfi 191
Cdd:cd01944 109 ---AEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWleALPAG----TTLVFDPGPRI---SDIPDTI---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 192 esshvtqqLQEVLHYFDLVVGTEEEFHIAGGSTDTLTALKNVR--QATKATLVCKRGALGCVVLEGEiptswEQTKLQSG 269
Cdd:cd01944 175 --------LQALMAKRPIWSCNREEAAIFAERGDPAAEASALRiyAKTAAPVVVRLGSNGAWIRLPD-----GNTHIIPG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2265705738 270 VRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHG 317
Cdd:cd01944 242 FKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
197-323 |
1.07e-04 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 45.02 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 197 TQQLQEVLHYFDLVVGTEEEFHIAG-----GSTDTLTALKNVRQATKAT------LVCKRGALG-CVVLEGEIpTSWEQT 264
Cdd:PTZ00247 205 FERLLQVLPYVDILFGNEEEAKTFAkamkwDTEDLKEIAARIAMLPKYSgtrprlVVFTQGPEPtLIATKDGV-TSVPVP 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 265 KLQSGvrvEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVSRHGCA-PAMP 323
Cdd:PTZ00247 284 PLDQE---KIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKP 340
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
227-336 |
1.54e-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: 44.25 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 227 LTALKNVRQATKAT--LVCKRGALGCVVL-EGEIPTSW------EQTKlqsgvrveVLNVLGAGDAFMSGLLRGWLNDES 297
Cdd:cd01943 212 LQALLFSGILQDPGggVVLRCGKLGCYVGsADSGPELWlpayhtKSTK--------VVDPTGGGNSFLGGFAAGLALTKS 283
|
90 100 110
....*....|....*....|....*....|....*....
gi 2265705738 298 WEQACRYANACGALVVSRHGcapaMPtkaELDDFLSRDK 336
Cdd:cd01943 284 IDEACIYGSVAASFAIEQVG----LP---RLTKVEGEEL 315
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
270-314 |
3.63e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 43.05 E-value: 3.63e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2265705738 270 VRVEVLNVLGAGDAFMSGLLRGWLNDESWEQACRYANACGALVVS 314
Cdd:PRK09850 244 IKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
153-313 |
9.44e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 38.62 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 153 VLKALDIARRHGLRTALDI-------DYRPVLwgltslgdgeTRFIESSHVtqqlqevlhyfDLVVGTEEEFH--IAGGS 223
Cdd:PLN02379 193 IEAAIRLAKQEGLSVSLDLasfemvrNFRSPL----------LQLLESGKI-----------DLCFANEDEARelLRGEQ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265705738 224 T-DTLTALKNVRQATKATLVcKRGALGCVVLEGEiptswEQTKLQSGVRVEVLNVLGAGDAFMSGLLRGWLNDESWEQAC 302
Cdd:PLN02379 252 EsDPEAALEFLAKYCNWAVV-TLGSKGCIARHGK-----EVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECC 325
|
170
....*....|.
gi 2265705738 303 RYANACGALVV 313
Cdd:PLN02379 326 KVGACSGGSVV 336
|
|
| |
