|
Name |
Accession |
Description |
Interval |
E-value |
| gntK_FGGY |
TIGR01314 |
gluconate kinase, FGGY type; Gluconate is derived from glucose in two steps. This model ... |
3-508 |
0e+00 |
|
gluconate kinase, FGGY type; Gluconate is derived from glucose in two steps. This model describes one form of gluconate kinase, belonging to the FGGY family of carbohydrate kinases. Gluconate kinase phosphoryates gluconate for entry into the Entner-Douderoff pathway. [Energy metabolism, Sugars]
Pssm-ID: 130381 [Multi-domain] Cd Length: 505 Bit Score: 873.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIaKEDIKLISFSAQMH 82
Cdd:TIGR01314 1 YMIGVDIGTTSTKAVLFEENGKIVAKSSIGYPLYTPASGMAEENPEEIFEAVLVTIREVSINLED-EDEILFVSFSTQMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYI 162
Cdd:TIGR01314 80 SLIAFDENWQPLTRLITWADNRAVKYAEQIKESKNGFDIYRRTGTPIHPMAPLSKIIWLEAEHPDIYQKAAKYLEIKGYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGV 242
Cdd:TIGR01314 160 FQRLFGTYKIDYSTASATGMFNLFELDWDKEALELTGIKESQLPKLVPTTEIEENLPHEYAKKMGIQSSTPFVIGASDGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 243 LSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTENHYVIGGPVNNGGVILRWLRDELLASEVETAKRL 322
Cdd:TIGR01314 240 LSNLGVNAIKKGEAAVTIGTSGAIRTVIDKPKTDEKGRIFCYALTKEHWVIGGPVNNGGDVLRWARDEIFDSEIETATRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 323 GVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMN 402
Cdd:TIGR01314 320 GIDPYDVLTEIAARVSPGADGLLFHPYLAGERAPLWNANARGSFFGLTYSHKKEHMIRAALEGVIYNLYTVALALVEVMG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 403 ETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGEIEDFSVIEDMVGTTHHHEPNPDTVQIY 482
Cdd:TIGR01314 400 DPLNMIQATGGFASSEVWRQMMSDIFEQEIVVPESYESSCLGACILGLKALGLIEDFSEVSTMVGTTETHTPIEKNFEIY 479
|
490 500
....*....|....*....|....*.
gi 488409258 483 QQLVSIFINLSRSLEDHYTEIAAFQR 508
Cdd:TIGR01314 480 REISPIFINLSRSLLAEYEQIADFQR 505
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-492 |
0e+00 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 707.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVreADIAKEDIKLISFSAQMH 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVL--AKLGGGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYI 162
Cdd:cd07770 79 SLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGV 242
Cdd:cd07770 159 LYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 243 LSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTENHYVIGGPVNNGGVILRWLRDELlasevetakRL 322
Cdd:cd07770 239 LANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENRWLVGGAINNGGNVLDWLRDTL---------LL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 323 GVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMN 402
Cdd:cd07770 310 SGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 403 EtPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGEIEDFSViEDMVGTTHHHEPNPDTVQIY 482
Cdd:cd07770 390 P-VKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEA-DELVKIGKVVEPDPENHAIY 467
|
490
....*....|
gi 488409258 483 QQLVSIFINL 492
Cdd:cd07770 468 AELYERFKKL 477
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-500 |
0e+00 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 597.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 2 KYMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQM 81
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 82 HSLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSY 161
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 162 ILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDG 241
Cdd:COG1070 161 LRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 242 VLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLtENHYVIGGPVNNGGVILRWLRDELLASEveta 319
Cdd:COG1070 241 AAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVhtFCHAV-PGRWLPMGATNNGGSALRWFRDLFADGE---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 320 krlgVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIE 399
Cdd:COG1070 316 ----LDDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 400 vMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGEIEDF-SVIEDMVGTTHHHEPNPDT 478
Cdd:COG1070 392 -AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLeEAAAAMVRVGETIEPDPEN 470
|
490 500
....*....|....*....|..
gi 488409258 479 VQIYQQLVSIFINLSRSLEDHY 500
Cdd:COG1070 471 VAAYDELYERYRELYPALKPLF 492
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-489 |
2.63e-162 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 469.31 E-value: 2.63e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQR-TGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSY 161
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLgGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 162 ILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDG 241
Cdd:cd07805 161 LNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 242 VLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYV-LTENHYVIGGPVNNGGVILRWLRDELLASEvetak 320
Cdd:cd07805 241 AAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLAsADPGRYLLAAEQETAGGALEWARDNLGGDE----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 321 RLGVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVyLALIEV 400
Cdd:cd07805 316 DLGADDYELLDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWL-LEALEK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 401 MNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPE-SYESSCLGACVLGLLALGEIEDFSVIEDMVGTTHHHEPNPDTV 479
Cdd:cd07805 395 LTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPEnPQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENR 474
|
490
....*....|
gi 488409258 480 QIYQQLVSIF 489
Cdd:cd07805 475 ARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-493 |
1.71e-160 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 464.32 E-value: 1.71e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKqHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYI 162
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEA-RLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGV 242
Cdd:cd07808 160 RYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 243 LSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLtENHYVIGGPVNNGGVILRWLRDELLASEvetak 320
Cdd:cd07808 240 AAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLhtFPHAV-PGKWYAMGVTLSAGLSLRWLRDLFGPDR----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 321 rlgvDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEv 400
Cdd:cd07808 314 ----ESFDELDAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKE- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 401 MNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGEIEDF-SVIEDMVGTTHHHEPNPDTV 479
Cdd:cd07808 389 LGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLeEAAAACIKIEKTIEPDPERH 468
|
490
....*....|....
gi 488409258 480 QIYQQLVSIFINLS 493
Cdd:cd07808 469 EAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-482 |
1.08e-137 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 404.59 E-value: 1.08e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRashyaerlnkqhhglniyqrtgtpihpmsplakifwmkheqpeifqhTAYFLDIKSYI 162
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKR-----------------------------------------------TAKFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGV 242
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 243 LSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYV-LTENHYVIGGPVNNGGVILRWLRDELLASEVEtAKR 321
Cdd:cd07779 194 CAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPsAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVA-EKE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 322 LGVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTvYLALIEVM 401
Cdd:cd07779 273 LGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRD-NLEAMEKA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 402 NETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGEIEDF-SVIEDMVGTTHHHEPNPDTVQ 480
Cdd:cd07779 352 GVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFeEAVKAMVRVTDTFEPDPENVA 431
|
..
gi 488409258 481 IY 482
Cdd:cd07779 432 IY 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-449 |
1.26e-136 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 400.40 E-value: 1.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRAshyaerlnkqhhglniyqrtgtpihpmsplakifwmkheqpeifqhtaYFLDIKSYI 162
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGV 242
Cdd:cd00366 113 VFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 243 LSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRtDYKGRIFC-YVLTENHYVIGGPVNNGGVILRWLRDELLASEVETAKR 321
Cdd:cd00366 193 AAALGAGVVEPGDAVDSTGTSSVLSVCTDEPV-PPDPRLLNrCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDAEY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 322 LGvdpydvLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTvYLALIEVM 401
Cdd:cd00366 272 EG------LDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRD-NLEILEEL 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 488409258 402 NETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLG 449
Cdd:cd00366 345 GVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-454 |
5.97e-132 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 390.35 E-value: 5.97e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYI 162
Cdd:cd07804 81 ALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASAT-GLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDG 241
Cdd:cd07804 161 VYKLTGEYVIDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 242 VLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDykGRIFC-YVLTENHYVIGGPVNNGGVILRWLRDELLASEVETAK 320
Cdd:cd07804 241 AASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTD--PRLWLdYHDIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 321 RLGVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVylalIEV 400
Cdd:cd07804 319 SGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHH----LEV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 488409258 401 MNE---TPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALG 454
Cdd:cd07804 395 IREaglPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-454 |
5.69e-126 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 375.00 E-value: 5.69e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREAdiAKEDIKLISFSAQMH 82
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA--GPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYI 162
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGV 242
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 243 LSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTD----YKGRIFCYVLTENHYVIGGPVnNGGVILRWLRDELLASEVET 318
Cdd:cd07773 239 CAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDemlaEGGLSYGHHVPGGYYYLAGSL-PGGALLEWFRDLFGGDESDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 319 AKRlgvdpydvlTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVyLALI 398
Cdd:cd07773 318 AAA---------DELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLN-LEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488409258 399 EVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALG 454
Cdd:cd07773 388 EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
5-489 |
1.25e-111 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 339.68 E-value: 1.25e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 5 IGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMHSL 84
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 85 VAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYILH 164
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 165 QLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGVLS 244
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 245 NLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLTENHYVIGgPVNNGGVILRWLRDELLASEVETakrl 322
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVhgFCHALPGGWLPMG-VTLSATSSLEWFRELFGKEDVEA---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 323 gvdpydvLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMN 402
Cdd:TIGR01312 316 -------LNELAEQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILREAGG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 403 ETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGEIEDFSVIEDMV-GTTHHHEPNPDTVQI 481
Cdd:TIGR01312 389 IPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAVvKQTESVLPIAENVEA 468
|
....*...
gi 488409258 482 YQQLVSIF 489
Cdd:TIGR01312 469 YEELYERY 476
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
3-454 |
6.24e-109 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 331.44 E-value: 6.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYI 162
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASaTGLFNLEKLDWDDEVLDLLGIS--RDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASD 240
Cdd:cd07802 161 RYRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 241 GVLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTENHYVIGGPVNNGGVILRWLRDELLASEvetaK 320
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSASNLDWFLDTLLGEE----K 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 321 RLGVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAplwNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEv 400
Cdd:cd07802 316 EAGGSDYDELDELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLV- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 488409258 401 mNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALG 454
Cdd:cd07802 392 -ARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
5-453 |
6.65e-98 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 302.22 E-value: 6.65e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 5 IGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAkeDIKLISFSAQMHSL 84
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 85 VAVNAAHQRLTESITWADNRASHYAERLNKqhHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYILH 164
Cdd:cd07783 81 VLVDREGEPLRPAIMYNDARAVAEAEELAE--AAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 165 QLFDTFVI-DHSMASATGlFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGVL 243
Cdd:cd07783 159 RLTGDRGVtDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 244 SNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVLTENHYVIGGPVNNGGVILRWLrdellasevetakrLG 323
Cdd:cd07783 238 AFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGDGYWLVGGASNTGGAVLRWF--------------FS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 324 VDPYDVLTKIASRvtPGAEGLIFHPY-LAGERAPLWNADARGSFfgLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMN 402
Cdd:cd07783 304 DDELAELSAQADP--PGPSGLIYYPLpLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLEELGA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488409258 403 ETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESyESSCLGACVLGLLAL 453
Cdd:cd07783 380 PPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-454 |
1.49e-91 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 286.37 E-value: 1.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYD-EHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQM 81
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 82 HSLVAVNAAHQRLTESITWADNRASHYAERLNKQHhGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSY 161
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELTEAL-GGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 162 ILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISR---DQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGA 238
Cdd:cd07809 160 LNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRdlrDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 239 SDGVLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLteNHYViggPVNNG-GVILRWLRdellase 315
Cdd:cd07809 240 GDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVatFCDST--GGML---PLINTtNCLTAWTE------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 316 vETAKRLGVDpYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWnADARGSFFGLTLS-HQKEHMIRAALEGVLFNLYtvY 394
Cdd:cd07809 308 -LFRELLGVS-YEELDELAAQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLR--Y 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409258 395 -LALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALG 454
Cdd:cd07809 383 gLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-454 |
8.99e-90 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 282.21 E-value: 8.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYI 162
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASATgLFNLEKLDWDDEVLDLLGIS--RDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASD 240
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 241 GVLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYK--GRIFCYVLtENHYVIGGPVNNGGVILRWLRDELLASEVET 318
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEgvGYTICLGV-PGRWLRAMANMAGTPNLDWFLRELGEVLKEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 319 AKRLGVDPYDVLTKIASRVTPGAEGLIFHPYL--AGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYla 396
Cdd:cd24121 319 AEPAGSDLFQDLEELAASSPPGAEGVLYHPYLspAGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCY-- 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 488409258 397 liEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALG 454
Cdd:cd24121 397 --EHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-498 |
6.17e-84 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 268.64 E-value: 6.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYD-EHGQFIMKHHIGYPLH--TPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSA 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGyiPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 80 QMHSLVAVNAAHQRLTESITWADNRASHYAERLNKQHH--GLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLD 157
Cdd:cd07781 81 TSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHpaLEYYLAYYGGVYSSEWMWPKALWLKRNAPEVYDAAYTIVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 158 IKSYILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGIS----RDQLPQ-LVSTTHILKGMKKRYATLMGIDENT 232
Cdd:cd07781 161 ACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGllklREKLPGeVVPVGEPAGTLTAEAAERLGLPAGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 233 PVIVGASDGVLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPrTDYKGriFCYV----LTENHYVI-GGPVNNGGvILRWL 307
Cdd:cd07781 241 PVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKP-VDIPG--ICGPvpdaVVPGLYGLeAGQSAVGD-IFAWF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 308 RDELlaseVETAKRLGVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVL 387
Cdd:cd07781 317 VRLF----VPPAEERGDSIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 388 FNLytvyLALIEVMNE---TPNKIKATGGFA-KSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGEIEDF-SVI 462
Cdd:cd07781 393 FGT----RAIIERFEEagvPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIeEAA 468
|
490 500 510
....*....|....*....|....*....|....*.
gi 488409258 463 EDMVGTTHHHEPNPDTVQIYQQLVSIFINLSRSLED 498
Cdd:cd07781 469 DAMVRVDRVYEPDPENHAVYEELYALYKELYDALGP 504
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-454 |
1.89e-82 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 262.93 E-value: 1.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNV--DISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQ 80
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDypDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 81 MHSLVAVNAAHQRL--TESItwaDNRASHYAERLNKQHhGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDI 158
Cdd:cd07798 81 REGIVFLDKDGRELyaGPNI---DARGVEEAAEIDDEF-GEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIATVLSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 159 KSYILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGA 238
Cdd:cd07798 157 SDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVVGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 239 SDGVLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIF--CYVLtENHYVI---GGPVnngGVILRWLRDELLA 313
Cdd:cd07798 237 ADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWtgCHLV-PGKWVLesnAGVT---GLNYQWLKELLYG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 314 SevetakrlGVDPYDVLTKIASRVTPGAEGLI--FHPYLAGERAplwNADARGSF-FGLTLSHQ---KEHMIRAALEGVL 387
Cdd:cd07798 313 D--------PEDSYEVLEEEASEIPPGANGVLafLGPQIFDARL---SGLKNGGFlFPTPLSASeltRGDFARAILENIA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409258 388 FNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALG 454
Cdd:cd07798 382 FAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-247 |
4.72e-81 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 252.64 E-value: 4.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYI 162
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 163 LHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGV 242
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQ 240
|
....*
gi 488409258 243 LSNLG 247
Cdd:pfam00370 241 AAAFG 245
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-485 |
2.25e-69 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 230.30 E-value: 2.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYpLHT--PNVDIS-----EENPDELFDavlmTVKYVVREADIAKEDIKLI 75
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREW-RHKevPDVPGSmdfdtEKNWKLICE----CIREALKKAGIAPKSIAAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 76 SFSAQMHSLVAVNAAHQRLtesitWA----DNRASHYAERLNKQHHGL--NIYQRTG-TPihPMSPLAKIFWMKHEQPEI 148
Cdd:cd07775 76 STTSMREGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTLeeEVYRISGqTF--ALGAIPRLLWLKNNRPEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 149 FQHTAYFLDIKSYILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGI 228
Cdd:cd07775 149 YRKAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 229 DENTPVIVGASDGVLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKG--RIFCYVLtENHYVIGGPVNNGGVILRW 306
Cdd:cd07775 229 KEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMniRVNCHVI-PDMWQAEGISFFPGLVMRW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 307 LRDELLASEVETAKRLGVDPYDVLTKIASRVTPGAEGL--IF----------HPylagerAPlwnadargSFFGLTL--- 371
Cdd:cd07775 308 FRDAFCAEEKEIAERLGIDAYDLLEEMAKDVPPGSYGImpIFsdvmnyknwrHA------AP--------SFLNLDIdpe 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 372 SHQKEHMIRAALEGVLFNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLL 451
Cdd:cd07775 374 KCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGV 453
|
490 500 510
....*....|....*....|....*....|....*
gi 488409258 452 ALGEIEDF-SVIEDMVGTTHHHEPNPDTVQIYQQL 485
Cdd:cd07775 454 GAGIYSSLeEAVESLVKWEREYLPNPENHEVYQDL 488
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-454 |
2.05e-66 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 222.34 E-value: 2.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQR-LTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWM---------KHEQPEifqht 152
Cdd:cd07769 81 TTVVWDKKTGKpLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWIldnvpgareRAERGE----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 153 AYFLDIKSYILHQL--FDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILkGMKKRYATLMGIde 230
Cdd:cd07769 156 LLFGTIDTWLIWKLtgGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVF-GYTDPEGLGAGI-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 231 ntPV--IVGASDGVLsnLGVNSYRKGEVAVTIGT-------SGairtviDKPRTDYKGRI--FCYVLTEN-HYVIGGPVN 298
Cdd:cd07769 233 --PIagILGDQQAAL--FGQGCFEPGMAKNTYGTgcfllmnTG------EKPVPSKNGLLttIAWQIGGKvTYALEGSIF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 299 NGGVILRWLRDELL----ASEVEtakrlgvdpydvltKIASRVtPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQ 374
Cdd:cd07769 303 IAGAAIQWLRDNLGliedAAETE--------------ELARSV-EDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTT 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 375 KEHMIRAALEGVLFNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALG 454
Cdd:cd07769 368 KAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVG 447
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-477 |
6.54e-62 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 210.30 E-value: 6.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 1 MKYMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPN---VdisEENPDELFDAVLMTVKYVVREADIAKEDIklisf 77
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQpgwV---EHDPEEIWESVLAVIREALAKAGISAEDI----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 78 saqmhslVAVNAAHQR-------------LTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWM--- 141
Cdd:COG0554 74 -------AAIGITNQRettvvwdrktgkpLYNAIVWQDRRTADICEELKADGLEDLIREKTGLVLDPYFSATKIKWIldn 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 142 ------KHEQPEIFqhtayFLDIKSYILHQLfdT----FVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVST 211
Cdd:COG0554 147 vpgareRAEAGELL-----FGTIDSWLIWKL--TggkvHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 212 THILkGMKKRYATLMGIdentPV--IVGASDGVLsnLGVNSYRKGEVAVTIGTSGAIRTVI-DKPRTDYKGrifcyVLT- 287
Cdd:COG0554 220 SEVF-GETDPDLFGAEI----PIagIAGDQQAAL--FGQACFEPGMAKNTYGTGCFLLMNTgDEPVRSKNG-----LLTt 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 288 -------ENHYVIGGPVNNGGVILRWLRDEL----LASEVETakrlgvdpydvltkIASRVtPGAEGLIFHPYLAGERAP 356
Cdd:COG0554 288 iawglggKVTYALEGSIFVAGAAVQWLRDGLglidSAAESEA--------------LARSV-EDNGGVYFVPAFTGLGAP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 357 LWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYtvylALIEVMNE----TPNKIKATGGFAKSEVWRQMMADIFDTKL 432
Cdd:COG0554 353 YWDPDARGAIFGLTRGTTRAHIARAALESIAYQTR----DVLDAMEAdsgiPLKELRVDGGASANDLLMQFQADILGVPV 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 488409258 433 IVPESYESSCLGACVLGLLALGEIEDFSVIEDMVGTTHHHEPNPD 477
Cdd:COG0554 429 ERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQMD 473
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-463 |
7.60e-62 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 210.60 E-value: 7.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 1 MKYMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVR--EADIAKEDIKLISFS 78
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKklREKGPSFKIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 79 AQMHSLVAVNAAHQR-LTESITWADNRASHYAERLNKQHHGLNIYQ-RTGTPIHPMSPLAKIFWMKHEQPEI----FQHT 152
Cdd:PTZ00294 81 NQRETVVAWDKVTGKpLYNAIVWLDTRTYDIVNELTKKYGGSNFFQkITGLPISTYFSAFKIRWMLENVPAVkdavKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 153 AYFLDIKSYILHQL--FDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTThilkgmkKRYATLMGID- 229
Cdd:PTZ00294 161 LLFGTIDTWLIWNLtgGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSS-------ENFGTISGEAv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 230 ---ENTPVIVGASDGVLSNLGVNSYRKGEVAVTIGTSGAIRTVI-DKPRTDYKGRI--FCYVLTENH---YVIGGPVNNG 300
Cdd:PTZ00294 234 pllEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTgTEIVFSKHGLLttVCYQLGPNGptvYALEGSIAVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 301 GVILRWLRDEL----LASEVEtakrlgvdpydvltKIASRVtPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKE 376
Cdd:PTZ00294 314 GAGVEWLRDNMglisHPSEIE--------------KLARSV-KDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 377 HMIRAALEGVLFNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALG-- 454
Cdd:PTZ00294 379 HIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGvw 458
|
490
....*....|
gi 488409258 455 -EIEDFSVIE 463
Cdd:PTZ00294 459 kSLEEVKKLI 468
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-497 |
2.29e-56 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 195.86 E-value: 2.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNA-AHQRLTESITWADNRASHYAERLNK-------------------QHHGLNIYQRTGTPIHPMSPLAKIFwMK 142
Cdd:cd07793 81 TFLTWDKkTGKPLHNFITWQDLRAAELCESWNRslllkalrggskflhfltrNKRFLAASVLKFSTAHVSIRLLWIL-QN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 143 HE--QPEIFQHTAYFLDIKSYILHQL--FDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHIlkgm 218
Cdd:cd07793 160 NPelKEAAEKGELLFGTIDTWLLWKLtgGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGD---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 219 kkryatlMGIDEntPVIVGAS--------DGVLSNLGVNSYRKGEVAVTIGTSgairTVID-----KPRTDYKGrifCYV 285
Cdd:cd07793 236 -------FGSTD--PSIFGAEipitavvaDQQAALFGECCFDKGDVKITMGTG----TFIDintgsKPHASVKG---LYP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 286 LT------ENHYVIGGPVNNGGVILRWLRDELLASEVEtakrlgvdpydVLTKIASRVtPGAEGLIFHPYLAGERAPLWN 359
Cdd:cd07793 300 LVgwkiggEITYLAEGNASDTGTVIDWAKSIGLFDDPS-----------ETEDIAESV-EDTNGVYFVPAFSGLQAPYND 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 360 ADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYE 439
Cdd:cd07793 368 PTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTE 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 488409258 440 SSCLGACVLGLLALGEIEDFSVIEDMVGTTHHHEPNPDtvqiYQQLVSIFINLSRSLE 497
Cdd:cd07793 448 MSALGAAFLAGLASGIWKSKEELKKLRKIEKIFEPKMD----NEKREELYKNWKKAVK 501
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-496 |
3.75e-54 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 189.79 E-value: 3.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 5 IGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIakEDIKLISFSAQMHSL 84
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 85 VAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNiyQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYILH 164
Cdd:PRK15027 81 TLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSR--VITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 165 QLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIdENTPVIVGASDGVLS 244
Cdd:PRK15027 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 245 NLGVNSYRKGEVAVTIGTSGAIRTVID----KPRTDYKGriFCYVLTEnhyviggpvnnggvilRW-LRDELL--ASEVE 317
Cdd:PRK15027 238 AVGVGMVDANQAMLSLGTSGVYFAVSEgflsKPESAVHS--FCHALPQ----------------RWhLMSVMLsaASCLD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 318 TAKRL-GVDPYDVLTKIASRVTPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTvYLA 396
Cdd:PRK15027 300 WAAKLtGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALAD-GMD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 397 LIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLivpeSYESS-----CLGACVLGLLALGEIEDFSVIEDMVGTTHH 471
Cdd:PRK15027 379 VVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQL----DYRTGgdvgpALGAARLAQIAANPEKSLIELLPQLPLEQS 454
|
490 500
....*....|....*....|....*
gi 488409258 472 HEPNPDTVQIYQQLVSIFINLSRSL 496
Cdd:PRK15027 455 HLPDAQRYAAYQPRRETFRRLYQQL 479
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-475 |
9.04e-54 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 188.47 E-value: 9.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMH 82
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQR-LTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWM---------KHEQPEIFqht 152
Cdd:cd07786 81 TTVVWDRETGKpVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLVLDPYFSATKIRWIldnvpgareRAERGELA--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 153 ayFLDIKSYILHQLFD--TFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILkGMKKRYATLMGIde 230
Cdd:cd07786 158 --FGTIDSWLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVF-GYTDPDLLGAEI-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 231 ntPV--IVGASDGVLsnLGVNSYRKGEVAVTIGTSGAIRTVI-DKPRTDYKGrifcyVLTENHYVIGGPVN--------N 299
Cdd:cd07786 233 --PIagIAGDQQAAL--FGQACFEPGMAKNTYGTGCFMLMNTgEKPVRSKNG-----LLTTIAWQLGGKVTyalegsifI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 300 GGVILRWLRDELL----ASEVETakrlgvdpydvltkIASRVtPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHQK 375
Cdd:cd07786 304 AGAAVQWLRDGLGliesAAETEA--------------LARSV-PDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 376 EHMIRAALEGVLFNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGE 455
Cdd:cd07786 369 AHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGL 448
|
490 500
....*....|....*....|
gi 488409258 456 IEDFSVIEDMVGTTHHHEPN 475
Cdd:cd07786 449 WKSLDELAKLWQVDRRFEPS 468
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-452 |
2.25e-53 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 186.27 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 5 IGVDIGTTSTKSVLYDEHGQ---FIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADiakEDIKLISFSAQM 81
Cdd:cd07777 3 LGIDIGTTSIKAALLDLESGrilESVSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYL---SDVTGIGITGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 82 HSLVAVNAAHQRLTESITWADNRASHyAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPeIFQHTAYFLDIKSY 161
Cdd:cd07777 80 HGIVLWDEDGNPVSPLITWQDQRCSE-EFLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGP-LPSKADRAGTIGDY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 162 ILHQL--FDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILkGMkkryaTLMGIDENTPVIVGAS 239
Cdd:cd07777 158 IVARLtgLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIV-GT-----LSSALPKGIPVYVALG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 240 DGVLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCYVltENHYVIGGPVNNGGVILRWLRDELlaseVETA 319
Cdd:cd07777 232 DNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELSGSVEIRPFF--DGRYLLVAASLPGGRALAVLVDFL----REWL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 320 KRLGVDP-----YDVLTKIASRvtPGAEGLIFHPYLAGERaplWNADARGSFFGLTLSHQK-EHMIRAALEGVLFNLYTV 393
Cdd:cd07777 306 RELGGSLsddeiWEKLDELAES--EESSDLSVDPTFFGER---HDPEGRGSITNIGESNFTlGNLFRALCRGIAENLHEM 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 394 YLALIEVMNEtPNKIKATGGFA-KSEVWRQMMADIFDTKLIVPESYESSCLGACvlgLLA 452
Cdd:cd07777 381 LPRLDLDLSG-IERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA---LLA 436
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
7-454 |
9.21e-53 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 186.19 E-value: 9.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 7 VDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVV---READIAKEDIKLISFSAQMHS 83
Cdd:cd07792 6 IDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVeklKALGISPSDIKAIGITNQRET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 84 LVAVNAAH-QRLTESITWADNRASHYAERLNKQH-HGLNIYQR-TGTPIHPMSPLAKIFWMKHEQPEIFQ----HTAYFL 156
Cdd:cd07792 86 TVVWDKSTgKPLYNAIVWLDTRTSDTVEELSAKTpGGKDHFRKkTGLPISTYFSAVKLRWLLDNVPEVKKavddGRLLFG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 157 DIKSYILHQL-----FDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKryatlmGIDEN 231
Cdd:cd07792 166 TVDSWLIWNLtggknGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIAS------GPLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 232 TPVivgasDGVL-----SNLGVNSYRKGEVAVTIGT----------------SGAIRTVidkprtdykgrifCYVLTEN- 289
Cdd:cd07792 240 VPI-----SGCLgdqqaALVGQGCFKPGEAKNTYGTgcfllyntgeepvfskHGLLTTV-------------AYKLGPDa 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 290 --HYVIGGPVNNGGVILRWLRDELL----ASEVETakrlgvdpydvltkIASRVtPGAEGLIFHPYLAGERAPLWNADAR 363
Cdd:cd07792 302 ppVYALEGSIAIAGAAVQWLRDNLGiissASEVET--------------LAASV-PDTGGVYFVPAFSGLFAPYWRPDAR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 364 GSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCL 443
Cdd:cd07792 367 GTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTAL 446
|
490
....*....|.
gi 488409258 444 GACVLGLLALG 454
Cdd:cd07792 447 GAAIAAGLAVG 457
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-485 |
3.07e-47 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 171.73 E-value: 3.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 1 MKYMIGVDIGTTSTKSVLYDEHGQFIM------KHhigypLHTPNVDISEEnpdelFDA------VLMTVKYVVREADIA 68
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAvgqaewRH-----LAVPDVPGSME-----FDLeknwqlACQCIRQALQKAGIP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 69 KEDIKLISFSAQMHSLVAVNAAHQRLtesitWA----DNRASHYAERLNKQHHGL--NIYQRTGTPIhPMSPLAKIFWMK 142
Cdd:PRK10939 72 ASDIAAVSATSMREGIVLYDRNGTEI-----WAcanvDARASREVSELKELHNNFeeEVYRCSGQTL-ALGALPRLLWLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 143 HEQPEIFQHTAYFLDIKSYILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRY 222
Cdd:PRK10939 146 HHRPDIYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 223 ATLMGIDENTPVIVGASDGVLSNLGVNSYRKGEVAVTIGTSGAIRTVIDKPRTDYKGRIFCyvlteNHYVIGGPVNN--- 299
Cdd:PRK10939 226 AAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNIRI-----NPHVIPGMVQAesi 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 300 ---GGVILRWLRDELLASEVETAKRLGVDPYDVLTKIASRVTPGAEGLI------------FHPylagerAPlwnadarg 364
Cdd:PRK10939 301 sffTGLTMRWFRDAFCAEEKLLAERLGIDAYSLLEEMASRVPVGSHGIIpifsdvmrfkswYHA------AP-------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 365 SFFGLTLSHQ---KEHMIRAALEGVLFnLYTVYLALIEVM-NETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYES 440
Cdd:PRK10939 367 SFINLSIDPEkcnKATLFRALEENAAI-VSACNLQQIAAFsGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEA 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 488409258 441 SCLGACVLGLLALGEIEDFS-VIEDMVGTTHHHEPNPDTVQIYQQL 485
Cdd:PRK10939 446 TALGCAIAAGVGAGIYSSLAeTGERLVRWERTFEPNPENHELYQEA 491
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
7-469 |
2.65e-45 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 166.03 E-value: 2.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 7 VDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKED----IKLISFSAQMH 82
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNvdsgLKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQR-LTESITWADNRASHYAERLNKQHHG--LNIYQRTGTPIHPMSPLAKIFWMKHEQPE----IFQHTAYF 155
Cdd:PLN02295 85 TTVAWSKSTGRpLYNAIVWMDSRTSSICRRLEKELSGgrKHFVETCGLPISTYFSATKLLWLLENVDAvkeaVKSGDALF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 156 LDIKSYILHQL-----FDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLmgide 230
Cdd:PLN02295 165 GTIDSWLIWNLtggasGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLA----- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 231 NTPVIVGASDGVLSNLGvNSYRKGEVAVTIGTS----------------GAIRTVIDKPRTDYKGrifcyvltenHYVIG 294
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLG-QRCRPGEAKSTYGTGcfillntgeevvpskhGLLTTVAYKLGPDAPT----------NYALE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 295 GPVNNGGVILRWLRDEL----LASEVETakrlgvdpydvltkIASRVtPGAEGLIFHPYLAGERAPLWNADARGSFFGLT 370
Cdd:PLN02295 309 GSVAIAGAAVQWLRDNLgiikSASEIEA--------------LAATV-DDTGGVYFVPAFSGLFAPRWRDDARGVCVGIT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 371 LSHQKEHMIRAALEGVLFNLYTVYLALI-----EVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGA 445
Cdd:PLN02295 374 RFTNKAHIARAVLESMCFQVKDVLDAMRkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGA 453
|
490 500
....*....|....*....|....*..
gi 488409258 446 CVLGLLALG---EIEDFSVIEDMVGTT 469
Cdd:PLN02295 454 AYAAGLAVGlwtEEEIFASEKWKNTTT 480
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-474 |
3.87e-45 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 165.38 E-value: 3.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 2 KYMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIklisfsaqm 81
Cdd:PRK00047 5 KYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 82 hslVAVNAAHQRLT-------------ESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFW-MKH---- 143
Cdd:PRK00047 76 ---AAIGITNQRETtvvwdketgrpiyNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWiLDNvega 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 144 -EQPEifQHTAYFLDIKSYILHQLFD--TFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHIlkgmkk 220
Cdd:PRK00047 153 rERAE--KGELLFGTIDTWLVWKLTGgkVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEV------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 221 rYA---TLMGIDENTPVIVGASDGVLSNLGVNSYRKGEVAVTIGT-------SGairtviDKPRTDYKGrifcyVLTENH 290
Cdd:PRK00047 225 -YGktnPYGFFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTgcfmlmnTG------EKAVKSENG-----LLTTIA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 291 YVIGGPVN--------NGGVILRWLRDELL----ASEVETAkrlgvdpydvltkiASRVtPGAEGLIFHPYLAGERAPLW 358
Cdd:PRK00047 293 WGIDGKVVyalegsifVAGSAIQWLRDGLKiisdASDSEAL--------------ARKV-EDNDGVYVVPAFTGLGAPYW 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 359 NADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESY 438
Cdd:PRK00047 358 DSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVA 437
|
490 500 510
....*....|....*....|....*....|....*.
gi 488409258 439 ESSCLGACVLGLLALGEIEDFSVIEDMVGTTHHHEP 474
Cdd:PRK00047 438 ETTALGAAYLAGLAVGFWKDLDELKEQWKIDRRFEP 473
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
3-492 |
5.40e-36 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 140.36 E-value: 5.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQMh 82
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATC- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 83 SLVAVNAAHQRLTES---------ITWADNRASHYAERLNKQHHglNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTA 153
Cdd:cd07782 80 SLVVLDAEGKPVSVSpsgddernvILWMDHRAVEEAERINATGH--EVLKYVGGKISPEMEPPKLLWLKENLPETWAKAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 154 YFLDIKSYILHQ-----------LFDTFVIDHSMASATGlfnlekldWDDEVL------DLLGISRDQLPQLVST--THI 214
Cdd:cd07782 158 HFFDLPDFLTWKatgsltrslcsLVCKWTYLAHEGSEGG--------WDDDFFkeigleDLVEDNFAKIGSVVLPpgEPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 215 LKGMKKRYATLMGIDENTPVIVGASD------GVLS-NLGVNSYRKGEV----AVTIGTSGAIRTVIDKPRT------DY 277
Cdd:cd07782 230 GGGLTAEAAKELGLPEGTPVGVSLIDahagglGTLGaDVGGLPCEADPLtrrlALICGTSSCHMAVSPEPVFvpgvwgPY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 278 KGRIFC-YVLTEnhyviGGPVNNGGVIlrwlrDELLASEV------ETAKRLGVDPYDVLTKI----ASRVTPGAEGLI- 345
Cdd:cd07782 310 YSAMLPgLWLNE-----GGQSATGALL-----DHIIETHPaypelkEEAKAAGKSIYEYLNERleqlAEEKGLPLAYLTr 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 346 ---FHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIR---AALEGvlfnlytvyLAL-----IEVMNETPNKIK---AT 411
Cdd:cd07782 380 dlhVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQA---------LAYgtrhiIEAMNAAGHKIDtifMC 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 412 GGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGeieDFSVIED-MVGTTHHH---EPNPDTVQIYQQLVS 487
Cdd:cd07782 451 GGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASG---DFPSLWDaMAAMSGPGkvvEPNEELKKYHDRKYE 527
|
....*
gi 488409258 488 IFINL 492
Cdd:cd07782 528 VFLKM 532
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-485 |
2.87e-35 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 137.47 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 1 MKYMIGVDIGTTSTKSVLYDEHGQFIMKHHigyplhTPN-VDISEENPDEL---FDAVLMTVKYVVRE--ADIAKEDIKL 74
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARAS------TPNaSDIAAENSDWHqwsLDAILQRFADCCRQinSELTECHIRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 75 ISFSAQMHSLVAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAY 154
Cdd:PRK10331 75 ITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 155 FLDIKSYILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISRDQLPQLVSTTHILKGMKKRYATLMGIDENTPV 234
Cdd:PRK10331 155 WLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 235 IVGASDGVLSNLGVNSYRKGEVAvtigTSGA-----IRTVIDKPR--TDYKGrifcyvLTENHYVIGGPVNNG------G 301
Cdd:PRK10331 235 ISAGHDTQFALFGSGAGQNQPVL----SSGTweilmVRSAQVDTSllSQYAG------STCELDSQSGLYNPGmqwlasG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 302 ViLRWLRDELLASEvetakrlgvDPYDVLTKIASRVTPGAEGLIFHPYLAGERaplwnadaRGSFFGLTLSHQKEHMIRA 381
Cdd:PRK10331 305 V-LEWVRKLFWTAE---------TPYQTMIEEARAIPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHFYRA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 382 ALEGVLFNLYTVYLALIEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLALGEiedFSV 461
Cdd:PRK10331 367 ALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGE---FSS 443
|
490 500
....*....|....*....|....*...
gi 488409258 462 IED----MVGTTHHHEPNPDtVQIYQQL 485
Cdd:PRK10331 444 PEQaraqMKYQYRYFYPQTE-PEFIEEV 470
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
256-453 |
4.91e-34 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 127.06 E-value: 4.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 256 VAVTIGTSGAIRTVIDKPRTDYKGRI--FCYVLTENHYVIGGPVNNGGVILRWLRDELLASEVETAKRlGVDPYDVLTKI 333
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWgpYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAG-NVESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 334 ASRVTPGaeGLIFHPYLAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMNETPNKIKATGG 413
Cdd:pfam02782 80 AAVAPAG--GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488409258 414 FAKSEVWRQMMADIFDTKLIVPESYESSCLGACVLGLLAL 453
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-464 |
1.85e-31 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 127.36 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYD-EHGQFIMKHHIGY-PLHTPNVDISEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSAQ 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYyQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 81 MhSLVAVNAAHQRLTES---------ITWADNRASHYAERLNKQHHGLnIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQH 151
Cdd:cd07768 81 C-SLAIFDREGTPLMALipypnednvIFWMDHSAVNEAQWINMQCPQQ-LLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 152 TAYFLDIKSYILHQLfdTFVIDHSMASATGLFNLEKLD--WDDEVLDLLGISRDQL------PQLVSTTHILKGMKKRYA 223
Cdd:cd07768 159 HFHIFDLHDYIAYEL--TRLYEWNICGLLGKENLDGEEsgWSSSFFKNIDPRLEHLtttknlPSNVPIGTTSGVALPEMA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 224 TLMGIDENTPVIVGASDGVLSNLGVNS-YRKGEVAVTIGTSGAirtvidkprtdykgriFCYVLTENHYVIG--GPVNNG 300
Cdd:cd07768 237 EKMGLHPGTAVVVSCIDAHASWFAVASpHLETSLFMIAGTSSC----------------HMYGTTISDRIPGvwGPFDTI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 301 ---------------GVILRWL-RDELLASEVETAKRLGVDPYDVLTKIASRVTP---GAEGLIFHPYLAGERAPLWNAD 361
Cdd:cd07768 301 idpdysvyeagqsatGKLIEHLfESHPCARKFDEALKKGADIYQVLEQTIRQIEKnngLSIHILTLDMFFGNRSEFADPR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 362 ARGSFFGLTLS---HQKEHMIRAALEGVLFNLYtvylALIEVMNETPNKIK---ATGGFAKSEVWRQMMADIFDTKLIVP 435
Cdd:cd07768 381 LKGSFIGESLDtsmLNLTYKYIAILEALAFGTR----LIIDTFQNEGIHIKelrASGGQAKNERLLQLIALVTNVAIIKP 456
|
490 500
....*....|....*....|....*....
gi 488409258 436 ESYESSCLGACVLGLLALGEIEDFSVIED 464
Cdd:cd07768 457 KENMMGILGAAVLAKVAAGKKQLADSITE 485
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
3-485 |
9.42e-26 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 110.34 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 3 YMIGVDIGTTSTKSVLYDEHGQFIMKHHIGY----P-LHTPNVDISEENPDELFDAVLMTVKYV------VREADIAKED 71
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFdsdlPeYGTKGGVHRDGDGGEVTSPVLMWVEALdlllekLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 72 IKLISFSAQMH----------SLVAVNAAHQRLTESI----------TWADNRASHYAERLNKQHHG-LNIYQRTGTPIH 130
Cdd:cd07776 81 VKAISGSGQQHgsvywskgaeSALANLDPSKSLAEQLegafsvpdspIWMDSSTTKQCRELEKAVGGpEALAKLTGSRAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 131 ---PMSPLAKIFwmkHEQPEIFQHTAyfldiksyILHqLFDTFV----------IDHSMASATGLFNLEKLDWDDEVLDL 197
Cdd:cd07776 161 erfTGPQIAKIA---QTDPEAYENTE--------RIS-LVSSFLaslllgryapIDESDGSGMNLMDIRSRKWSPELLDA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 198 LGIS--RDQLPQLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGVLSNLGVNSyRKGEVAVTIGTSGAIRTVIDKPRT 275
Cdd:cd07776 229 ATAPdlKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTSDTVFLVLDEPKP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 276 DYKGRIFCYVLTENHYVIGGPVNNGGVILRWLRDellasevetakRLGVDPYDVLTKIASRVTPGAEGLIFHPYLAGE-- 353
Cdd:cd07776 308 GPEGHVFANPVDPGSYMAMLCYKNGSLARERVRD-----------RYAGGSWEKFNELLESTPPGNNGNLGLYFDEPEit 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 354 ----RAPLWNADARGSFFGLTLSHQkehmIRAALEGVLFNLYtVYLALIEvMNETPNKIKATGGFAKSEVWRQMMADIFD 429
Cdd:cd07776 377 ppvpGGGRRFFGDDGVDAFFDPAVE----VRAVVESQFLSMR-LHAERLG-SDIPPTRILATGGASANKAILQVLADVFG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409258 430 TKLIVPESYESSCLGACVLGLLALGEIEDFSVIEDMVGTTH-----HHEPNPDTVQIYQQL 485
Cdd:cd07776 451 APVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAeepklVAEPDPEAAEVYDKL 511
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-485 |
1.84e-24 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 106.85 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 1 MKYMIGVDIGTTSTKSVLYD-EHGQFIMKHHIGYPLHT------PNVDISEENPDELFDAVLMTVKYVVREADIAKEDIK 73
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWVkgryldLPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 74 LISFSAQMHSLVAVNAAHQRLTESITWADN-----------RASHYAERLNKQHH--GLNIYQR-TGTPIHPMSPLAKIF 139
Cdd:PRK04123 82 GIGVDFTGSTPAPVDADGTPLALLPEFAENphamvklwkdhTAQEEAEEINRLAHerGEADLSRyIGGIYSSEWFWAKIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 140 WMKHEQPEIFQHTAYFLDIKSYILHQLFDTFVIDH-----------SM--ASATGLFNLEKLDWDDEVLDllGISRDQLP 206
Cdd:PRK04123 162 HVLREDPAVYEAAASWVEACDWVVALLTGTTDPQDivrsrcaaghkALwhESWGGLPSADFFDALDPLLA--RGLRDKLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 207 -QLVSTTHILKGMKKRYATLMGIDENTPVIVGASDGVLSNLGVNSyRKGEVAVTIGTSGAIRTVIDKPRTdYKGrifcyv 285
Cdd:PRK04123 240 tETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTSTCDILLADKQRA-VPG------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 286 ltenhyvIGGPVNNG---------------GVILRWLRDELL-ASEVETAKRLGVDPYDVLTKIASRVTPGAEGLIFHPY 349
Cdd:PRK04123 312 -------ICGQVDGSivpgligyeagqsavGDIFAWFARLLVpPEYKDEAEARGKQLLELLTEAAAKQPPGEHGLVALDW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 350 LAGERAPLWNADARGSFFGLTLSHQKEHMIRAALEGVLFNLYtvylALIEVMNE--TP-NKIKATGGFA-KSEVWRQMMA 425
Cdd:PRK04123 385 FNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTR----AIMECFEDqgVPvEEVIAAGGIArKNPVLMQIYA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409258 426 DIFDTKLIVPESYESSCLGACVLGLLALGEIEDF--------SVIEDMvgtthhHEPNPDTVQIYQQL 485
Cdd:PRK04123 461 DVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIpeaqqamaSPVEKT------YQPDPENVARYEQL 522
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
121-469 |
5.34e-19 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 89.51 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 121 IYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYILHQLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGI 200
Cdd:cd07771 117 LYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 201 SRDQLPQLVSTTHILkGMKKRYATLMGIDENTPVIVGAS-D---GVLSnlgVNSYRKGEVAVTIGTSGAIRTVIDKPRTD 276
Cdd:cd07771 197 PRDLFPPIVPPGTVL-GTLKPEVAEELGLKGIPVIAVAShDtasAVAA---VPAEDEDAAFISSGTWSLIGVELDEPVIT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 277 YKGRIFCYvltenhyviggpVNNGGV-----ILR-----WLRDELLAsevETAKRLGVDPYDVLTKIASRVTPgaEGLIF 346
Cdd:cd07771 273 EEAFEAGF------------TNEGGAdgtirLLKnitglWLLQECRR---EWEEEGKDYSYDELVALAEEAPP--FGAFI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 347 HPylageraplwnADARgsFF----------------GLTLSHQKEHMIRAALEGVLFNLYTVYLALIEVMNETPNKIKA 410
Cdd:cd07771 336 DP-----------DDPR--FLnpgdmpeairaycretGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHI 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409258 411 TGGFAKSEVWRQMMADIfdTKLIV---PEsyESSCLGACVLGLLALGEIEDFSVIEDMVGTT 469
Cdd:cd07771 403 VGGGSRNALLCQLTADA--TGLPViagPV--EATAIGNLLVQLIALGEIKSLEEGRELVRNS 460
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-448 |
5.30e-13 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 70.75 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 7 VDIGTTSTKSVLYDEHGQFIMKhhigypLHTPNVDISE-----ENPDELFDAVLMTVKYVVREADIAKediklISFSAQM 81
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAE------RSTPNPEIEEdgypcEDVEAIWEWLLDSLAELAKRHRIDA-----INFTTHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 82 HSLVAVNAAHQRLT-----ESITWADNRASHYAERLNkqhhglniYQRTGTPIHP-MSPLAK-IFWMKHEQPEIFQHTAY 154
Cdd:cd07772 74 ATFALLDENGELALpvydyEKPIPDEINEAYYAERGP--------FEETGSPPLPgGLNLGKqLYWLKREKPELFARAKT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 155 FLDIKSYILHQLFDTFVIDHSMASA-TGLFNLEKLDWDDEVLDlLGISRdQLPQLVSTTHILKGMKKRYATLMGIDENTP 233
Cdd:cd07772 146 ILPLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEYSSLVKK-EGWDK-LFPPLRKAWEVLGPLRPDLARRTGLPKDIP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 234 VIVGASDgvlSNLGVNSYRKGE----VAVTIGT-------SGAIRTVIDKPRTDykgrIFCYVLtenhyVIGGPVNN--- 299
Cdd:cd07772 224 VGCGIHD---SNAALLPYLAAGkepfTLLSTGTwciamnpGNDLPLTELDLARD----CLYNLD-----VFGRPVKTarf 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 300 -GGVILrwlrdELLasevetAKRLGVDPYDVLTKIASRVTPGAEGLIFHPYLAGERaplWNADARGSFFGLTLSHQKEHm 378
Cdd:cd07772 292 mGGREY-----ERL------VERIAKSFPQLPSLADLAKLLARGTFALPSFAPGGG---PFPGSGGRGVLSAFPSAEEA- 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409258 379 iRAALegvlfnlyTVYLAL-----IEVMNETPNKIKATGGFAKSEVWRQMMADIFDTKLIVPESYES-SCLGACVL 448
Cdd:cd07772 357 -YALA--------ILYLALmtdyaLDLLGSGVGRIIVEGGFAKNPVFLRLLAALRPDQPVYLSDDSEgTALGAALL 423
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
85-202 |
2.09e-10 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 62.81 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 85 VAVNAAHQRLTESITWADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSPLAKIFWMKHEQPEIFQHTAYFLDIKSYILH 164
Cdd:PRK10640 69 VLLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSY 148
|
90 100 110
....*....|....*....|....*....|....*...
gi 488409258 165 QLFDTFVIDHSMASATGLFNLEKLDWDDEVLDLLGISR 202
Cdd:PRK10640 149 RLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPK 186
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-166 |
3.65e-07 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 52.79 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 5 IGVDIGTTSTKSVLYDEHGQFI--MKHHIGYPLHTPNVDISEENPDELFDAVL-MTVKYVVREADIAkedIKLISFSA-- 79
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLatSERPISYKQDPKDLWFVTQSSTEIWKAIKtALKELIEELSDYI---VSGIGVSAtc 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409258 80 ----------QMHsLVAVNAAH--QRLTESIT-WADNRASHYAERLNKQHHGLNIYQRTGTPIHPMSpLAKIFWMKHEQP 146
Cdd:cd07778 80 smvvmqrdsdTSY-LVPYNVIHekSNPDQDIIfWMDHRASEETQWLNNILPDDILDYLGGGFIPEMA-IPKLKYLIDLIK 157
|
170 180
....*....|....*....|
gi 488409258 147 EIFQHTAYFLDIKSYILHQL 166
Cdd:cd07778 158 EDTFKKLEVFDLHDWISYML 177
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-79 |
8.17e-07 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 50.67 E-value: 8.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409258 1 MKYMIGVDIGTTSTKSVLYDEHGQFIMKHHIGYPlhtpnvdiSEENPDELFDAVLMTVKYVVREADIAKEDIKLISFSA 79
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTP--------AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGV 74
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
1-75 |
1.02e-03 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 40.86 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409258 1 MKYMIGVDIGTTSTKSVLYDEHGQFIMKHHI---GYPLhtpnvdiseENPDELFDAVLmtvkyvvREADIAKEDIKLI 75
Cdd:COG1924 2 GMIYLGIDIGSTTTKAVLLDEDGEILASAYLptgGDPL---------EAAKEALKELL-------EEAGLKREDIAGV 63
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
5-75 |
3.86e-03 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 39.06 E-value: 3.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409258 5 IGVDIGTTSTKSVLYDEHGQfIMKHHIGYPLHtpnvdiseeNPDELFDAVLmtvKYVVREADIAKEDIKLI 75
Cdd:cd24036 2 AGIDVGSTTTKAVILDDKGK-ILGKAVIRTGT---------DPEKTAERAL---EEALEEAGLSREDIEYI 59
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
5-70 |
6.31e-03 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 38.21 E-value: 6.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409258 5 IGVDIGTTSTKSVLYDEHGQFIMKHHIGYPlhtpnvdiSEENPDELFDAVLMTVKYVVREADIAKE 70
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTP--------AEEGPEAVLDRIAELIEELLAEAGVRER 58
|
|
| DDE_Tnp_IS66_C |
pfam13817 |
IS66 C-terminal element; |
316-339 |
7.71e-03 |
|
IS66 C-terminal element;
Pssm-ID: 433500 Cd Length: 39 Bit Score: 34.29 E-value: 7.71e-03
10 20
....*....|....*....|....*...
gi 488409258 316 VETAKRLGVDPY----DVLTKIASRVTP 339
Cdd:pfam13817 3 IETAKLNGLDPYayltDVLERLPDHHPA 30
|
|
| |
