|
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: 859.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIaKEDIKFISLSAQMH 82
Cdd:TIGR01314 1 YMIGVDIGTTSTKAVLFEENGKIVAKSSIGYPLYTPASGMAEENPEEIFEAVLVTIREVSINLED-EDEILFVSFSTQMH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYV 162
Cdd:TIGR01314 80 SLIAFDENWQPLTRLITWADNRAVKYAEQIKESKNGFDIYRRTGTPIHPMAPLSKIIWLEAEHPDIYQKAAKYLEIKGYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGV 242
Cdd:TIGR01314 160 FQRLFGTYKIDYSTASATGMFNLFELDWDKEALELTGIKESQLPKLVPTTEIEENLPHEYAKKMGIQSSTPFVIGASDGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 243 LSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYILDKDQYVIGGPVNNGGVVLRWLRDEILASEVETAKRL 322
Cdd:TIGR01314 240 LSNLGVNAIKKGEAAVTIGTSGAIRTVIDKPKTDEKGRIFCYALTKEHWVIGGPVNNGGDVLRWARDEIFDSEIETATRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 323 GVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:TIGR01314 320 GIDPYDVLTEIAARVSPGADGLLFHPYLAGERAPLWNANARGSFFGLTYSHKKEHMIRAALEGVIYNLYTVALALVEVMG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 403 ETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDFSVIKDMVGTTHAHEPNQETVAIY 482
Cdd:TIGR01314 400 DPLNMIQATGGFASSEVWRQMMSDIFEQEIVVPESYESSCLGACILGLKALGLIEDFSEVSTMVGTTETHTPIEKNFEIY 479
|
490 500
....*....|....*....|....*.
gi 488368810 483 QQLVTIFINISRSMTENYSDIANFQR 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: 675.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKedIKFISLSAQMH 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGE--VDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYV 162
Cdd:cd07770 79 SLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGV 242
Cdd:cd07770 159 LYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 243 LSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYILDKDQYVIGGPVNNGGVVLRWLRDEIlasevetakRL 322
Cdd:cd07770 239 LANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENRWLVGGAINNGGNVLDWLRDTL---------LL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 323 GVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:cd07770 310 SGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 403 EtPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDFSViKDMVGTTHAHEPNQETVAIY 482
Cdd:cd07770 390 P-VKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEA-DELVKIGKVVEPDPENHAIY 467
|
490
....*....|
gi 488368810 483 QQLVTIFINI 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: 567.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 2 KYMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQM 81
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 82 HSLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTY 161
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 162 VLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDG 241
Cdd:COG1070 161 LRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 242 VLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRI--FCYILDkDQYVIGGPVNNGGVVLRWLRDEILASEveta 319
Cdd:COG1070 241 AAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVhtFCHAVP-GRWLPMGATNNGGSALRWFRDLFADGE---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 320 krlgVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIE 399
Cdd:COG1070 316 ----LDDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 400 vMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDF-SVIKDMVGTTHAHEPNQET 478
Cdd:COG1070 392 -AGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLeEAAAAMVRVGETIEPDPEN 470
|
490 500
....*....|....*....|..
gi 488368810 479 VAIYQQLVTIFINISRSMTENY 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 |
7.57e-157 |
|
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: 455.44 E-value: 7.57e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQR-TGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTY 161
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLgGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 162 VLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDG 241
Cdd:cd07805 161 LNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 242 VLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYI-LDKDQYVIGGPVNNGGVVLRWLRDEILASEvetak 320
Cdd:cd07805 241 AAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLAsADPGRYLLAAEQETAGGALEWARDNLGGDE----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 321 RLGVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVyLALIEV 400
Cdd:cd07805 316 DLGADDYELLDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWL-LEALEK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 401 MNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPE-SYESSCLGACVLGMKALGEIDDFSVIKDMVGTTHAHEPNQETV 479
Cdd:cd07805 395 LTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPEnPQEAGALGAALLAAVGLGLLKSFDEAKALVKVEKVFEPDPENR 474
|
490
....*....|
gi 488368810 480 AIYQQLVTIF 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 |
1.44e-148 |
|
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: 433.89 E-value: 1.44e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGfELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTA--MFAdlKT 160
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGD-EILIITGNPPLPGFTLPKLLWLKENEPEIFARIRkiLLP--KD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 161 YVLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASD 240
Cdd:cd07808 158 YLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 241 GVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCY-ILDKDQYVIGGPVNNGGVVLRWLRDEILASEveta 319
Cdd:cd07808 238 NAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFpHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDR---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 320 krlgvDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIE 399
Cdd:cd07808 314 -----ESFDELDAEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 400 vMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDF-SVIKDMVGTTHAHEPNQET 478
Cdd:cd07808 389 -LGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLeEAAAACIKIEKTIEPDPER 467
|
490
....*....|....*
gi 488368810 479 VAIYQQLVTIFINIS 493
Cdd:cd07808 468 HEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-482 |
5.13e-128 |
|
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: 379.94 E-value: 5.13e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRandyadlieksyggfelyqrtgtpihpmsplskifwmrheepkifkqTAMFADLKTYV 162
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKR-----------------------------------------------TAKFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGV 242
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGDQQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 243 LSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYI-LDKDQYVIGGPVNNGGVVLRWLRDEILASEVEtAKR 321
Cdd:cd07779 194 CAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPsAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVA-EKE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 322 LGVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYLALIEVM 401
Cdd:cd07779 273 LGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRD-NLEAMEKA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 402 NETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDF-SVIKDMVGTTHAHEPNQETVA 480
Cdd:cd07779 352 GVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFeEAVKAMVRVTDTFEPDPENVA 431
|
..
gi 488368810 481 IY 482
Cdd:cd07779 432 IY 433
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-454 |
6.47e-128 |
|
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: 380.33 E-value: 6.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYV 162
Cdd:cd07804 81 ALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSL-GSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDG 241
Cdd:cd07804 161 VYKLTGEYVIDYSSaGNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 242 VLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEkgRIF-CYILDKDQYVIGGPVNNGGVVLRWLRDEILASEVETAK 320
Cdd:cd07804 241 AASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDP--RLWlDYHDIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 321 RLGVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVylalIEV 400
Cdd:cd07804 319 SGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHH----LEV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 488368810 401 MNE---TPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 454
Cdd:cd07804 395 IREaglPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-449 |
5.07e-127 |
|
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: 375.75 E-value: 5.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRAndyadlieksyggfelyqrtgtpihpmsplskifwmrheepkifkqtaMFADLKTYV 162
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGV 242
Cdd:cd00366 113 VFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 243 LSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYILDKDQYVIGGPVNNGGVVLRWLRDEILASEVETAKRL 322
Cdd:cd00366 193 AAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDAEYE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 323 GvdpydvLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYLALIEVMN 402
Cdd:cd00366 273 G------LDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRD-NLEILEELG 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 488368810 403 ETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLG 449
Cdd:cd00366 346 VKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-454 |
5.79e-116 |
|
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: 349.19 E-value: 5.79e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGiaKEDIKFISLSAQMH 82
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYV 162
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGV 242
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 243 LSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTD----EKGRIFCYILDKDQYVIGGPVnNGGVVLRWLRDEILASEVET 318
Cdd:cd07773 239 CAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDemlaEGGLSYGHHVPGGYYYLAGSL-PGGALLEWFRDLFGGDESDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 319 AKRlgvdpydvlTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVyLALI 398
Cdd:cd07773 318 AAA---------DELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLN-LEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488368810 399 EVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 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 |
9.30e-106 |
|
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: 324.27 E-value: 9.30e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMHSL 84
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 85 IAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYVLF 164
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 165 QLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGVLS 244
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 245 NLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRI--FCYILdKDQYVIGGPVNNGGVVLRWLRDEILASEVETakrl 322
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVhgFCHAL-PGGWLPMGVTLSATSSLEWFRELFGKEDVEA---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 323 gvdpydvLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:TIGR01312 316 -------LNELAEQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILREAGG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 403 ETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDFSVIKDMV-GTTHAHEPNQETVAI 481
Cdd:TIGR01312 389 IPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAVvKQTESVLPIAENVEA 468
|
....*...
gi 488368810 482 YQQLVTIF 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 |
3.59e-105 |
|
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: 321.81 E-value: 3.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYV 162
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSlGSATGMMNLEQLDWDNKALELLGIE--RNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASD 240
Cdd:cd07802 161 RYRLTGEISTDYT-DAGSSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 241 GVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYILDKDQYVIGGPVNNGGVVLRWLRDEILASEvetaK 320
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPGLYLIVEASPTSASNLDWFLDTLLGEE----K 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 321 RLGVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAplwNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEv 400
Cdd:cd07802 316 EAGGSDYDELDELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLV- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 488368810 401 mNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 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 |
4.96e-89 |
|
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: 279.49 E-value: 4.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAkeDIKFISLSAQMHSL 84
Cdd:cd07783 3 LGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 85 IAMNEDNQRLTENITWADNRANDYADLIEKSYGgfELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYVLF 164
Cdd:cd07783 81 VLVDREGEPLRPAIMYNDARAVAEAEELAEAAG--AVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 165 QL-YERFVIDYSlGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGVL 243
Cdd:cd07783 159 RLtGDRGVTDYN-NALKLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTTDSIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 244 SNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYILDKDQYVIGGPVNNGGVVLRWLrdeilasevetakrLG 323
Cdd:cd07783 238 AFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGDGYWLVGGASNTGGAVLRWF--------------FS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 324 VDPYDVLTQIASRvkPGAEGLIFHPY-LAGERAPLWNADARGSFfgLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMN 402
Cdd:cd07783 304 DDELAELSAQADP--PGPSGLIYYPLpLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLEELGA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488368810 403 ETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESyESSCLGACVLGMKAL 453
Cdd:cd07783 380 PPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-448 |
2.71e-87 |
|
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: 275.58 E-value: 2.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYD-ENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQM 81
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 82 HSLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQrTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTY 161
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLL-VGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 162 VLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERN---QLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGA 238
Cdd:cd07809 160 LNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDlrdLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 239 SDGVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRI--FCyilDKDqyviGG--PVNNG-GVVLRWLRdeila 313
Cdd:cd07809 240 GDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVatFC---DST----GGmlPLINTtNCLTAWTE----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 314 sevETAKRLGVDpYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWnADARGSFFGLTLS-HKKEHMIRAALEGVLYNLYt 392
Cdd:cd07809 308 ---LFRELLGVS-YEELDELAAQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLR- 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 488368810 393 vY-LALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVL 448
Cdd:cd07809 382 -YgLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQ 437
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-454 |
1.53e-81 |
|
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: 261.02 E-value: 1.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYV 162
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSLGSATgMMNLEQLDWDNKALELLGIE--RNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASD 240
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 241 GVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEK--GRIFCYIlDKDQYVIGGPVNNGGVVLRWLRDEILASEVET 318
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEgvGYTICLG-VPGRWLRAMANMAGTPNLDWFLRELGEVLKEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 319 AKRLGVDPYDVLTQIASRVKPGAEGLIFHPYL--AGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYla 396
Cdd:cd24121 319 AEPAGSDLFQDLEELAASSPPGAEGVLYHPYLspAGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCY-- 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 488368810 397 liEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 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; ... |
3-485 |
1.00e-77 |
|
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: 252.46 E-value: 1.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYD-ENGKFIMKHNIGYDLH--TPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSA 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGyiPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 80 QMHSLIAMNEDNQRLTENITWADNRANDYADLIEKSYG--GFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFAD 157
Cdd:cd07781 81 TSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHpaLEYYLAYYGGVYSSEWMWPKALWLKRNAPEVYDAAYTIVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 158 LKTYVLFQLYERFVIdySLGSAT--GMMNLEQLDWDNKALELLGIE----RNQLPQ-LVPTTHVLTGMKKRYATLMGIDE 230
Cdd:cd07781 161 ACDWINARLTGRWVR--SRCAAGhkWMYNEWGGGPPREFLAALDPGllklREKLPGeVVPVGEPAGTLTAEAAERLGLPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 231 QTPVIVGASDGVLSNLGVNSYQKGEVAVTIGTSgairtvinqpktdekgriFCYIL--DKDQYVIG--GPVNNG------ 300
Cdd:cd07781 239 GIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTS------------------TCHLMvsPKPVDIPGicGPVPDAvvpgly 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 301 ---------GVVLRWLRDEIlaseVETAKRLGVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTL 371
Cdd:cd07781 301 gleagqsavGDIFAWFVRLF----VPPAEERGDSIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 372 SHKKEHMIRAALEGVLYNLytvyLALIEVMNE---TPTTIKATGGFA-KSEIWRQMMADIFDTDLIVPESYESSCLGACV 447
Cdd:cd07781 377 GTTPAHIYRALLEATAFGT----RAIIERFEEagvPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAI 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 488368810 448 LGMKALGEIDDF-SVIKDMVGTTHAHEPNQETVAIYQQL 485
Cdd:cd07781 453 LAAVAAGVYADIeEAADAMVRVDRVYEPDPENHAVYEEL 491
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-247 |
1.30e-77 |
|
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: 243.78 E-value: 1.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYV 162
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 163 LFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGV 242
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQ 240
|
....*
gi 488368810 243 LSNLG 247
Cdd:pfam00370 241 AAAFG 245
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-454 |
8.55e-75 |
|
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: 243.28 E-value: 8.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGK--FIMKHNIGYdlHTPNV--DVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLS 78
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKivAIAYREWEY--YTDDDypDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 79 AQMHSLIAMNEDNQRL--TENItwaDNRANDYADLIEkSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFA 156
Cdd:cd07798 79 SQREGIVFLDKDGRELyaGPNI---DARGVEEAAEID-DEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIATVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 157 DLKTYVLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIV 236
Cdd:cd07798 155 SISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 237 GASDGVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIF--CYILDkDQYVI---GGPVnngGVVLRWLRDeI 311
Cdd:cd07798 235 GGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWtgCHLVP-GKWVLesnAGVT---GLNYQWLKE-L 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 312 LASEVEtakrlgvDPYDVLTQIASRVKPGAEGLI--FHPYLAGERAplwNADARGSFFGLTLSH----KKEHMIRAALEG 385
Cdd:cd07798 310 LYGDPE-------DSYEVLEEEASEIPPGANGVLafLGPQIFDARL---SGLKNGGFLFPTPLSaselTRGDFARAILEN 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488368810 386 VLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALG 454
Cdd:cd07798 380 IAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-465 |
1.87e-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: 1.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQR-LTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEP----KIFKQTAMFAD 157
Cdd:cd07769 81 TTVVWDKKTGKpLYNAIVWQDRRTADICEELKAKGLEERIREKTGLPLDPYFSATKIKWILDNVPgareRAERGELLFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 158 LKTYVLFQL--YERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLtGMKKRYATLMGIdeqtPV- 234
Cdd:cd07769 161 IDTWLIWKLtgGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVF-GYTDPEGLGAGI----PIa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 235 -IVGASDGVLsnLGVNSYQKGEVAVTIGTSGAIrtVIN---QPKTDEKGRI--FCYILDKD-QYVIGGPVNNGGVVLRWL 307
Cdd:cd07769 236 gILGDQQAAL--FGQGCFEPGMAKNTYGTGCFL--LMNtgeKPVPSKNGLLttIAWQIGGKvTYALEGSIFIAGAAIQWL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 308 RDEIL----ASEVETakrlgvdpydvltqIASRVkPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAAL 383
Cdd:cd07769 312 RDNLGliedAAETEE--------------LARSV-EDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAAL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 384 EGVLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDFSVIK 463
Cdd:cd07769 377 ESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELA 456
|
..
gi 488368810 464 DM 465
Cdd:cd07769 457 SL 458
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-485 |
3.21e-63 |
|
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: 214.12 E-value: 3.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYdLHTPNVDV-------SEENPDEIFDavlmTVKYIVRESGIAKEDIKFI 75
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREW-RHKEVPDVpgsmdfdTEKNWKLICE----CIREALKKAGIAPKSIAAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 76 SLSAQMHSLIAMNEDNQRLtenitWA----DNRANDYADLIEKSYGGFE--LYQRTG-TPihPMSPLSKIFWMRHEEPKI 148
Cdd:cd07775 76 STTSMREGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTLEeeVYRISGqTF--ALGAIPRLLWLKNNRPEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 149 FKQTAMFADLKTYVLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGI 228
Cdd:cd07775 149 YRKAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 229 DEQTPVIVGASDGVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKG--RIFCYILdKDQYVIGGPVNNGGVVLRW 306
Cdd:cd07775 229 KEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMniRVNCHVI-PDMWQAEGISFFPGLVMRW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 307 LRDEILASEVETAKRLGVDPYDVLTQIASRVKPGAEGL--IF----------HPylagerAPlwnadargSFFGLTLSHK 374
Cdd:cd07775 308 FRDAFCAEEKEIAERLGIDAYDLLEEMAKDVPPGSYGImpIFsdvmnyknwrHA------AP--------SFLNLDIDPE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 375 KehmiraalegvlYNLYTVYLALIE---------------VMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYE 439
Cdd:cd07775 374 K------------CNKATFFRAIMEnaaivsagnleriaeFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 488368810 440 SSCLGACVLGMKALGEIDDF-SVIKDMVGTTHAHEPNQETVAIYQQL 485
Cdd:cd07775 442 ATALGAAIAAGVGAGIYSSLeEAVESLVKWEREYLPNPENHEVYQDL 488
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-484 |
4.47e-60 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 205.98 E-value: 4.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 1 MKYMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGI--AKEDIKFISLS 78
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREkgPSFKIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 79 AQMHSLIAMNEDNQRLTEN-ITWADNRANDYADLIEKSYGGFELYQ-RTGTPIHPMSPLSKIFWMRHEEPKI----FKQT 152
Cdd:PTZ00294 81 NQRETVVAWDKVTGKPLYNaIVWLDTRTYDIVNELTKKYGGSNFFQkITGLPISTYFSAFKIRWMLENVPAVkdavKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 153 AMFADLKTYVLFQLYER--FVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTThvltgmkKRYATLMGidE 230
Cdd:PTZ00294 161 LLFGTIDTWLIWNLTGGksHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSS-------ENFGTISG--E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 231 QTPVIVG------ASDGVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIF---CYILDKDQ---YVIGGPVN 298
Cdd:PTZ00294 232 AVPLLEGvpitgcIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLttvCYQLGPNGptvYALEGSIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 299 NGGVVLRWLRDEilasevetakrLGV--DPYDVlTQIASRVKpGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKE 376
Cdd:PTZ00294 312 VAGAGVEWLRDN-----------MGLisHPSEI-EKLARSVK-DTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 377 HMIRAALEGVLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACV---LGMKAL 453
Cdd:PTZ00294 379 HIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALlagLAVGVW 458
|
490 500 510
....*....|....*....|....*....|..
gi 488368810 454 GEIDDF-SVIKDMVGTTHAHEPNQETVAIYQQ 484
Cdd:PTZ00294 459 KSLEEVkKLIRRSNSTFSPQMSAEERKAIYKE 490
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-475 |
1.87e-57 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 198.75 E-value: 1.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 1 MKYMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPN---VdvsEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISL 77
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQpgwV---EHDPEEIWESVLAVIREALAKAGISAEDIAAIGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 78 SaqmhsliamnedNQRLT------------EN-ITWADNRANDYAD-LIEKsyGGFELYQ-RTGTPIHPMSPLSKIFWM- 141
Cdd:COG0554 79 T------------NQRETtvvwdrktgkplYNaIVWQDRRTADICEeLKAD--GLEDLIReKTGLVLDPYFSATKIKWIl 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 142 RHEE---PKIFKQTAMFADLKTYVLFQLY--ERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLt 216
Cdd:COG0554 145 DNVPgarERAEAGELLFGTIDSWLIWKLTggKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVF- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 217 GmkkrYATLMGIDEQTPV--IVGASDGVLsnLGVNSYQKGEVAVTIGTSGAIrtVIN---QPKTDEKG---RIFCYILDK 288
Cdd:COG0554 224 G----ETDPDLFGAEIPIagIAGDQQAAL--FGQACFEPGMAKNTYGTGCFL--LMNtgdEPVRSKNGlltTIAWGLGGK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 289 DQYVIGGPVNNGGVVLRWLRDEI----LASEVETakrlgvdpydvltqIASRVKPgAEGLIFHPYLAGERAPLWNADARG 364
Cdd:COG0554 296 VTYALEGSIFVAGAAVQWLRDGLglidSAAESEA--------------LARSVED-NGGVYFVPAFTGLGAPYWDPDARG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 365 SFFGLTLSHKKEHMIRAALEGVLYNLYtvylALIEVMNE----TPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYES 440
Cdd:COG0554 361 AIFGLTRGTTRAHIARAALESIAYQTR----DVLDAMEAdsgiPLKELRVDGGASANDLLMQFQADILGVPVERPKVTET 436
|
490 500 510
....*....|....*....|....*....|....*
gi 488368810 441 SCLGACVLGMKALGEIDDFSVIKDMVGTTHAHEPN 475
Cdd:COG0554 437 TALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPQ 471
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-477 |
6.11e-57 |
|
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: 197.40 E-value: 6.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDN-QRLTENITWADNRANDYADLIEKSY-------GGFELYQRTGTPIH---------PMSPLSKIFWMRHEE 145
Cdd:cd07793 81 TFLTWDKKTgKPLHNFITWQDLRAAELCESWNRSLllkalrgGSKFLHFLTRNKRFlaasvlkfsTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 146 PK----IFKQTAMFADLKTYVLFQLYER--FVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTthvltgmk 219
Cdd:cd07793 161 PElkeaAEKGELLFGTIDTWLLWKLTGGkvHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDT-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 220 kryATLMGIDEqtPVIVGAS--------DGVLSNLGVNSYQKGEVAVTIGTSGAIRTVI-NQPKTDEKGrifCY------ 284
Cdd:cd07793 233 ---SGDFGSTD--PSIFGAEipitavvaDQQAALFGECCFDKGDVKITMGTGTFIDINTgSKPHASVKG---LYplvgwk 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 285 ILDKDQYVIGGPVNNGGVVLRWLRDEILASEVEtakrlgvdpydVLTQIASRVkPGAEGLIFHPYLAGERAPLWNADARG 364
Cdd:cd07793 305 IGGEITYLAEGNASDTGTVIDWAKSIGLFDDPS-----------ETEDIAESV-EDTNGVYFVPAFSGLQAPYNDPTACA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 365 SFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLG 444
Cdd:cd07793 373 GFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALG 452
|
490 500 510
....*....|....*....|....*....|...
gi 488368810 445 ACVLGMKALGEIDDFSVIKDMVGTTHAHEPNQE 477
Cdd:cd07793 453 AAFLAGLASGIWKSKEELKKLRKIEKIFEPKMD 485
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-489 |
4.70e-53 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 186.71 E-value: 4.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIakEDIKFISLSAQMHSL 84
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 85 IAMNEDNQRLTENITWADNRANDYADLIEKSYGgfELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAMFADLKTYVLF 164
Cdd:PRK15027 81 TLLDAQQRVLRPAILWNDGRCAQECALLEARVP--QSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 165 QLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIdEQTPVIVGASDGVLS 244
Cdd:PRK15027 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 245 NLGVNSYQKGEVAVTIGTSGAIRTV----INQPKTDEKGriFCYILDKdqyviggpvnnggvvlRWLRDEILASEVE--- 317
Cdd:PRK15027 238 AVGVGMVDANQAMLSLGTSGVYFAVsegfLSKPESAVHS--FCHALPQ----------------RWHLMSVMLSAAScld 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 318 -TAKRLGVDPYDVLTQIASRVKPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTvYLA 396
Cdd:PRK15027 300 wAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALAD-GMD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 397 LIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLivpeSYESS-----CLGACVLGMKALGEIDDFSVIKDMVGTTHA 471
Cdd:PRK15027 379 VVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQL----DYRTGgdvgpALGAARLAQIAANPEKSLIELLPQLPLEQS 454
|
490
....*....|....*...
gi 488368810 472 HEPNQETVAIYQQLVTIF 489
Cdd:PRK15027 455 HLPDAQRYAAYQPRRETF 472
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-446 |
2.43e-52 |
|
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: 183.58 E-value: 2.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 5 IGVDMGTTSTKAVLYD-ENGKFI--MKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESgiaKEDIKFISLSAQM 81
Cdd:cd07777 3 LGIDIGTTSIKAALLDlESGRILesVSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREY---LSDVTGIGITGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 82 HSLIAMNEDNQRLTENITWADNRANDyADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPkIFKQTAMFADLKTY 161
Cdd:cd07777 80 HGIVLWDEDGNPVSPLITWQDQRCSE-EFLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGP-LPSKADRAGTIGDY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 162 VLFQL--YERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLtGMkkryaTLMGIDEQTPVIVGAS 239
Cdd:cd07777 158 IVARLtgLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIV-GT-----LSSALPKGIPVYVALG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 240 DGVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYIldKDQYVIGGPVNNGGVVLRWLRDEIlaseVETA 319
Cdd:cd07777 232 DNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELSGSVEIRPFF--DGRYLLVAASLPGGRALAVLVDFL----REWL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 320 KRLGVDP-----YDVLTQIAsrVKPGAEGLIFHPYLAGERaplWNADARGSFFGLTLSH-KKEHMIRAALEGVLYNLYTV 393
Cdd:cd07777 306 RELGGSLsddeiWEKLDELA--ESEESSDLSVDPTFFGER---HDPEGRGSITNIGESNfTLGNLFRALCRGIAENLHEM 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 488368810 394 YLALIEVMNEtPTTIKATGGFA-KSEIWRQMMADIFDTDLIVPESYESSCLGAC 446
Cdd:cd07777 381 LPRLDLDLSG-IERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-475 |
8.20e-51 |
|
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: 180.76 E-value: 8.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTEN-ITWADNRANDYAD-LIEKSYGGFeLYQRTGTPIHPMSPLSKIFWM---------RHEEPKIfkq 151
Cdd:cd07786 81 TTVVWDRETGKPVYNaIVWQDRRTADICEeLKAEGHEEM-IREKTGLVLDPYFSATKIRWIldnvpgareRAERGEL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 152 taMFADLKTYVLFQLY--ERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLtgmkkRYATLMGID 229
Cdd:cd07786 157 --AFGTIDSWLIWKLTggKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVF-----GYTDPDLLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 230 EQTPV--IVGASDGVLsnLGVNSYQKGEVAVTIGTSGAIrtVIN---QPKTDEKG---RIFCYILDKDQYVIGGPVNNGG 301
Cdd:cd07786 230 AEIPIagIAGDQQAAL--FGQACFEPGMAKNTYGTGCFM--LMNtgeKPVRSKNGlltTIAWQLGGKVTYALEGSIFIAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 302 VVLRWLRDEIL----ASEVETakrlgvdpydvltqIASRVkPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEH 377
Cdd:cd07786 306 AAVQWLRDGLGliesAAETEA--------------LARSV-PDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAH 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 378 MIRAALEGVLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVL-GMKAlGEI 456
Cdd:cd07786 371 IARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLaGLAV-GLW 449
|
490
....*....|....*....
gi 488368810 457 DDFSVIKDMVGTTHAHEPN 475
Cdd:cd07786 450 KSLDELAKLWQVDRRFEPS 468
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
7-469 |
1.18e-50 |
|
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: 180.41 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 7 VDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIV---RESGIAKEDIKFISLSAQMHS 83
Cdd:cd07792 6 IDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVeklKALGISPSDIKAIGITNQRET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 84 LIAMN-EDNQRLTENITWADNRANDYAD-LIEKSYGGFELYQR-TGTPIHPMSPLSKIFWMRHEEPKIFKQ----TAMFA 156
Cdd:cd07792 86 TVVWDkSTGKPLYNAIVWLDTRTSDTVEeLSAKTPGGKDHFRKkTGLPISTYFSAVKLRWLLDNVPEVKKAvddgRLLFG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 157 DLKTYVLFQL-----YERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKryATLMGI--- 228
Cdd:cd07792 166 TVDSWLIWNLtggknGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIAS--GPLAGVpis 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 229 ----DEQtpvivGASdgvlsnLGVNSYQKGEVAVTIGT----------------SGAIRTVinqpktdekgrifCYILDK 288
Cdd:cd07792 244 gclgDQQ-----AAL------VGQGCFKPGEAKNTYGTgcfllyntgeepvfskHGLLTTV-------------AYKLGP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 289 DQ---YVIGGPVNNGGVVLRWLRDEIL----ASEVETakrlgvdpydvltqIASRVkPGAEGLIFHPYLAGERAPLWNAD 361
Cdd:cd07792 300 DAppvYALEGSIAIAGAAVQWLRDNLGiissASEVET--------------LAASV-PDTGGVYFVPAFSGLFAPYWRPD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 362 ARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESS 441
Cdd:cd07792 365 ARGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETT 444
|
490 500 510
....*....|....*....|....*....|.
gi 488368810 442 CLGACV---LGMKALGEIDDFSVIKDMVGTT 469
Cdd:cd07792 445 ALGAAIaagLAVGVWKSLDELKSLNEGGRTV 475
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-474 |
5.91e-45 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 165.00 E-value: 5.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 2 KYMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQM 81
Cdd:PRK00047 5 KYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 82 HSLIAMNEDNQRLTEN-ITWADNRANDYAD-LIEKSYGGFeLYQRTGTPIHPMSPLSKIFWM---------RHEEPKifk 150
Cdd:PRK00047 85 ETTVVWDKETGRPIYNaIVWQDRRTADICEeLKRDGYEDY-IREKTGLVIDPYFSGTKIKWIldnvegareRAEKGE--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 151 qtAMFADLKTYVLFQLY--ERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVltgmkkrYA---TL 225
Cdd:PRK00047 161 --LLFGTIDTWLVWKLTggKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEV-------YGktnPY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 226 MGIDEQTPVIVGASDGVLSNLGVNSYQKGEVAVTIGTSGAIrtVIN---QPKTDEKG---RIFCYILDKDQYVIGGPVNN 299
Cdd:PRK00047 232 GFFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFM--LMNtgeKAVKSENGlltTIAWGIDGKVVYALEGSIFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 300 GGVVLRWLRDEIL----ASEVETAkrlgvdpydvltqiASRVKpGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKK 375
Cdd:PRK00047 310 AGSAIQWLRDGLKiisdASDSEAL--------------ARKVE-DNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 376 EHMIRAALEGVLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGE 455
Cdd:PRK00047 375 EHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGF 454
|
490
....*....|....*....
gi 488368810 456 IDDFSVIKDMVGTTHAHEP 474
Cdd:PRK00047 455 WKDLDELKEQWKIDRRFEP 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-485 |
4.90e-44 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 162.87 E-value: 4.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 1 MKYMIGVDMGTTSTKAVLYDENGKFIM------KHnigydLHTPNVDVSEEnpdeiFDA------VLMTVKYIVRESGIA 68
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAvgqaewRH-----LAVPDVPGSME-----FDLeknwqlACQCIRQALQKAGIP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 69 KEDIKFISLSAQMHSLIAMNEDNQRLtenitWA----DNRANDYADLIEKSYGGFE--LYQRTGTPIhPMSPLSKIFWMR 142
Cdd:PRK10939 72 ASDIAAVSATSMREGIVLYDRNGTEI-----WAcanvDARASREVSELKELHNNFEeeVYRCSGQTL-ALGALPRLLWLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 143 HEEPKIFKQTAMFADLKTYVLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRY 222
Cdd:PRK10939 146 HHRPDIYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 223 ATLMGIDEQTPVIVGASDGVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKG--RIFCyildkdqYVIGGPVNN- 299
Cdd:PRK10939 226 AAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMniRINP-------HVIPGMVQAe 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 300 -----GGVVLRWLRDEILASEVETAKRLGVDPYDVLTQIASRVKPGAEGLI------------FHPylagerAPlwnada 362
Cdd:PRK10939 299 sisffTGLTMRWFRDAFCAEEKLLAERLGIDAYSLLEEMASRVPVGSHGIIpifsdvmrfkswYHA------AP------ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 363 rgSFFGLTL----SHKKEhMIRAALEgvlyNLYTVY---LALIEVM-NETPTTIKATGGFAKSEIWRQMMADIFDTDLIV 434
Cdd:PRK10939 367 --SFINLSIdpekCNKAT-LFRALEE----NAAIVSacnLQQIAAFsGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKV 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 488368810 435 PESYESSCLGACVLGMKALGEIDDFS-VIKDMVGTTHAHEPNQETVAIYQQL 485
Cdd:PRK10939 440 PVVKEATALGCAIAAGVGAGIYSSLAeTGERLVRWERTFEPNPENHELYQEA 491
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
7-469 |
7.57e-43 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 159.48 E-value: 7.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 7 VDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLM----TVKYIVRESGIAKEDIKFISLSAQMH 82
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTciakALEKAAAKGHNVDSGLKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTEN-ITWADNRANDYADLIEK--SYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPK----IFKQTAMF 155
Cdd:PLN02295 85 TTVAWSKSTGRPLYNaIVWMDSRTSSICRRLEKelSGGRKHFVETCGLPISTYFSATKLLWLLENVDAvkeaVKSGDALF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 156 ADLKTYVLFQL-----YERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLmGIDe 230
Cdd:PLN02295 165 GTIDSWLIWNLtggasGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWPLA-GVP- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 231 qtpvIVGA-SDGVLSNLGvNSYQKGEVAVTIGTSGAIrtVIN---QPKTDEKGRI--FCYILDKD---QYVIGGPVNNGG 301
Cdd:PLN02295 243 ----IAGClGDQHAAMLG-QRCRPGEAKSTYGTGCFI--LLNtgeEVVPSKHGLLttVAYKLGPDaptNYALEGSVAIAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 302 VVLRWLRDEI----LASEVETakrlgvdpydvltqIASRVkPGAEGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEH 377
Cdd:PLN02295 316 AAVQWLRDNLgiikSASEIEA--------------LAATV-DDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 378 MIRAALEGVLYNLYTVYLALI-----EVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACV---LG 449
Cdd:PLN02295 381 IARAVLESMCFQVKDVLDAMRkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYaagLA 460
|
490 500
....*....|....*....|
gi 488368810 450 MKALGEIDDFSVIKDMVGTT 469
Cdd:PLN02295 461 VGLWTEEEIFASEKWKNTTT 480
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
3-499 |
6.73e-35 |
|
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: 137.28 E-value: 6.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQMh 82
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATC- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNEDNQRLTEN---------ITWADNRANDYADLIEKSygGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTA 153
Cdd:cd07782 80 SLVVLDAEGKPVSVSpsgddernvILWMDHRAVEEAERINAT--GHEVLKYVGGKISPEMEPPKLLWLKENLPETWAKAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 154 MFADLKTYVLFQ----------------LYERFVidyslGSATGmmnleqldWDNKALELLGIE------RNQLPQ--LV 209
Cdd:cd07782 158 HFFDLPDFLTWKatgsltrslcslvckwTYLAHE-----GSEGG--------WDDDFFKEIGLEdlvednFAKIGSvvLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 210 PTTHVLTGMKKRYATLMGIDEQTPVIVGASD------GVLS-NLGVNSYQKGEV----AVTIGTSGairtvinqpktdek 278
Cdd:cd07782 225 PGEPVGGGLTAEAAKELGLPEGTPVGVSLIDahagglGTLGaDVGGLPCEADPLtrrlALICGTSS-------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 279 grifCYIL--DKDQYVIG--GP----------VNNGG-----VVLrwlrDEILASEV------ETAKRLGVDPYDVLT-- 331
Cdd:cd07782 291 ----CHMAvsPEPVFVPGvwGPyysamlpglwLNEGGqsatgALL----DHIIETHPaypelkEEAKAAGKSIYEYLNer 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 332 --QIASRVKPGAEGLI----FHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIraalegVLYnLYTV-YLAL-----IE 399
Cdd:cd07782 363 leQLAEEKGLPLAYLTrdlhVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLA------LLY-LATLqALAYgtrhiIE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 400 VMNE---TPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGeidDFSVIKD-MVGTTHAH--- 472
Cdd:cd07782 436 AMNAaghKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASG---DFPSLWDaMAAMSGPGkvv 512
|
570 580
....*....|....*....|....*..
gi 488368810 473 EPNQETVAIYQQLVTIFinisRSMTEN 499
Cdd:cd07782 513 EPNEELKKYHDRKYEVF----LKMYED 535
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
256-453 |
1.15e-33 |
|
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: 126.29 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 256 VAVTIGTSGAIRTVINQPKTDEKGRI--FCYILDKDQYVIGGPVNNGGVVLRWLRDEILASEVETAKRlGVDPYDVLTQI 333
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWgpYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAG-NVESLAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 334 ASRVKPGaeGLIFHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPTTIKATGG 413
Cdd:pfam02782 80 AAVAPAG--GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488368810 414 FAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKAL 453
Cdd:pfam02782 158 GSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
3-485 |
1.75e-31 |
|
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: 127.29 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYDENGKFIMKHNIGYD-----LHTPNVDVSEENPDEIFDAVLMTVKYI------VRESGIAKED 71
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDsdlpeYGTKGGVHRDGDGGEVTSPVLMWVEALdlllekLKAAGFDFSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 72 IKFISLSAQMH----------SLIAMNEDNQRLTENI----------TWADNRANDYADLIEKSYGGFE-LYQRTGTPIH 130
Cdd:cd07776 81 VKAISGSGQQHgsvywskgaeSALANLDPSKSLAEQLegafsvpdspIWMDSSTTKQCRELEKAVGGPEaLAKLTGSRAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 131 PMSPLSKIFWMRHEEPKIFKQTA-------MFADLktyvlfqLYERFV-IDYSLGSATGMMNLEQLDWDNKALELLGIE- 201
Cdd:cd07776 161 ERFTGPQIAKIAQTDPEAYENTErislvssFLASL-------LLGRYApIDESDGSGMNLMDIRSRKWSPELLDAATAPd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 202 -RNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGVLSNLGVNSyQKGEVAVTIGTSGAIRTVINQPKTDEKGR 280
Cdd:cd07776 234 lKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTSDTVFLVLDEPKPGPEGH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 281 IFCYILDKDQYVIGGPVNNGGVVLRWLRDEILASEvetakrlgvdpYDVLTQIASRVKPGAEGLIFHPYLAGE------R 354
Cdd:cd07776 313 VFANPVDPGSYMAMLCYKNGSLARERVRDRYAGGS-----------WEKFNELLESTPPGNNGNLGLYFDEPEitppvpG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 355 APLWNADARGSFFGLTlshkKEHMIRAALEGVLYNLYtVYLALIEvMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIV 434
Cdd:cd07776 382 GGRRFFGDDGVDAFFD----PAVEVRAVVESQFLSMR-LHAERLG-SDIPPTRILATGGASANKAILQVLADVFGAPVYT 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 488368810 435 PESYESSCLGACVLGMKALGEIDDFSVIKDMVGTTH-----AHEPNQETVAIYQQL 485
Cdd:cd07776 456 LDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAeepklVAEPDPEAAEVYDKL 511
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-489 |
6.52e-30 |
|
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: 122.73 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVLYD-ENGKFIMKHNIGY-DLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSAQ 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYyQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 81 MhSLIAMNEDNQRLTEN---------ITWADNRANDYADLIEKSYGGfELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQ 151
Cdd:cd07768 81 C-SLAIFDREGTPLMALipypnednvIFWMDHSAVNEAQWINMQCPQ-QLLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 152 TAMFADLKTYVLFQLYERFVidYSLGSATGMMNL--EQLDWDN---KALELLGIERNQ---LPQLVPTTHVLTGMKKRYA 223
Cdd:cd07768 159 HFHIFDLHDYIAYELTRLYE--WNICGLLGKENLdgEESGWSSsffKNIDPRLEHLTTtknLPSNVPIGTTSGVALPEMA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 224 TLMGIDEQTPVIVGASDGVLSNLGVNS-YQKGEVAVTIGTSGA--IRTVINQPKTDEKGrIFCYILDKDQYVIGGPVNNG 300
Cdd:cd07768 237 EKMGLHPGTAVVVSCIDAHASWFAVASpHLETSLFMIAGTSSChmYGTTISDRIPGVWG-PFDTIIDPDYSVYEAGQSAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 301 GVVLRWL-RDEILASEVETAKRLGVDPYDVLTQIASRVKP---GAEGLIFHPYLAGERAPLWNADARGSFFGLTLS---H 373
Cdd:cd07768 316 GKLIEHLfESHPCARKFDEALKKGADIYQVLEQTIRQIEKnngLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDtsmL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 374 KKEHMIRAALEGVLYNLYtvylALIEVMNETPTTIK---ATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGM 450
Cdd:cd07768 396 NLTYKYIAILEALAFGTR----LIIDTFQNEGIHIKelrASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAK 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 488368810 451 KALGEIDDFSVIK------DMVGTTHAHEPNqETVAIYQQLVTIF 489
Cdd:cd07768 472 VAAGKKQLADSITeadisnDRKSETFEPLAY-RLGADYILLYKLL 515
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-485 |
6.14e-28 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 116.28 E-value: 6.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 1 MKYMIGVDMGTTSTKAVLYDENGKFIMKHnigydlHTPN-VDVSEENPD-EI--FDAVLMTVKYIVRE--SGIAKEDIKF 74
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARA------STPNaSDIAAENSDwHQwsLDAILQRFADCCRQinSELTECHIRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 75 ISLSAQMHSLIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQTAM 154
Cdd:PRK10331 75 ITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 155 FADLKTYVLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGIDEQTPV 234
Cdd:PRK10331 155 WLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 235 IVGASDGVLSNLGVNSyQKGEVAVTIGTSGAIRTVINQPKTDekgRIFCYI-----LDKD--------QYVIGGpvnngg 301
Cdd:PRK10331 235 ISAGHDTQFALFGSGA-GQNQPVLSSGTWEILMVRSAQVDTS---LLSQYAgstceLDSQsglynpgmQWLASG------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 302 vVLRWLRDEILASEvetakrlgvDPYDVLTQIASRVKPGAEGLIFHPYLAGERaplwnadaRGSFFGLTLSHKKEHMIRA 381
Cdd:PRK10331 305 -VLEWVRKLFWTAE---------TPYQTMIEEARAIPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHFYRA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 382 ALEGVLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDDFSV 461
Cdd:PRK10331 367 ALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQ 446
|
490 500
....*....|....*....|....*
gi 488368810 462 IKDMVGTT-HAHEPnQETVAIYQQL 485
Cdd:PRK10331 447 ARAQMKYQyRYFYP-QTEPEFIEEV 470
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-485 |
5.06e-23 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 102.23 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 1 MKYMIGVDMGTTSTKAVLYD-ENGKFIMKH-------NIGYDLHTPNvDVSEENPDEIFDAVLMTVKYIVRESGIAKEDI 72
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDcATGEELATAvveyphwVKGRYLDLPP-NQALQHPLDYIESLEAAIPAVLKEAGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 73 KFISLSAQMHSLIAMNEDNQRLTENITWADN-----------RANDYADLIEK--SYGGFELYQR-TGTPIHPMSPLSKI 138
Cdd:PRK04123 81 VGIGVDFTGSTPAPVDADGTPLALLPEFAENphamvklwkdhTAQEEAEEINRlaHERGEADLSRyIGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 139 FWMRHEEPKIFKQTAMF---ADLKTYVLFQLYERFVIDYSLGSAtGMMNLEQLDWDN-------KAL--ELLGIERNQLP 206
Cdd:PRK04123 161 LHVLREDPAVYEAAASWveaCDWVVALLTGTTDPQDIVRSRCAA-GHKALWHESWGGlpsadffDALdpLLARGLRDKLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 207 -QLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGVLSNLGVNSyQKGEVAVTIGTSgairtvinqpkTdekgrifCYI 285
Cdd:PRK04123 240 tETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTS-----------T-------CDI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 286 L--DKDQYVIG--GPVNNG---------------GVVLRWLRDEIL-ASEVETAKRLGVDPYDVLTQIASRVKPGAEGLI 345
Cdd:PRK04123 301 LlaDKQRAVPGicGQVDGSivpgligyeagqsavGDIFAWFARLLVpPEYKDEAEARGKQLLELLTEAAAKQPPGEHGLV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 346 FHPYLAGERAPLWNADARGSFFGLTLSHKKEHMIRAALEGvlynlyTVY--LALIEVMNETPTTIK---ATGGFA-KSEI 419
Cdd:PRK04123 381 ALDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEA------TAFgtRAIMECFEDQGVPVEeviAAGGIArKNPV 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488368810 420 WRQMMADIFDTDLIVPESYESSCLGACVLGMKALGEIDD-FSVIKDM-VGTTHAHEPNQETVAIYQQL 485
Cdd:PRK04123 455 LMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDiPEAQQAMaSPVEKTYQPDPENVARYEQL 522
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
3-469 |
1.32e-20 |
|
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: 94.52 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 3 YMIGVDMGTTSTKAVL--YDEnGKFIMKhnigyDLHT-PNVDVSEENP-----DEIFDAVLMTVKYIVRESGiakeDIKF 74
Cdd:cd07771 1 NYLAVDLGASSGRVILgsLDG-GKLELE-----EIHRfPNRPVEINGHlywdiDRLFDEIKEGLKKAAEQGG----DIDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 75 ISLS--AQMHSLIamNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWMRHEEPKIFKQT 152
Cdd:cd07771 71 IGIDtwGVDFGLL--DKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 153 A---MFADLKTYVLFQlyeRFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLPQLVPTTHVLTGMKKRYATLMGID 229
Cdd:cd07771 149 DkllMLPDLLNYLLTG---EKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 230 EqTPVIVGAS-D---GVLSNLGVNsyqKGEVAVTIGTSGAIRTVINQPKTDEKGRIFCYildkdqyviggpVNNGGV--- 302
Cdd:cd07771 226 G-IPVIAVAShDtasAVAAVPAED---EDAAFISSGTWSLIGVELDEPVITEEAFEAGF------------TNEGGAdgt 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 303 --VLR-----WLRDEILAsevETAKRLGVDPYDVLTQIASRVKPgaEGLIFHPylageraplwnADARgsFF-------- 367
Cdd:cd07771 290 irLLKnitglWLLQECRR---EWEEEGKDYSYDELVALAEEAPP--FGAFIDP-----------DDPR--FLnpgdmpea 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 368 --------GLTLSHKKEHMIRAALEGVLYNLYTVYLALIEVMNETPTTIKATGGFAKSEIWRQMMADIfdTDLIV---PE 436
Cdd:cd07771 352 iraycretGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADA--TGLPViagPV 429
|
490 500 510
....*....|....*....|....*....|...
gi 488368810 437 syESSCLGACVLGMKALGEIDDFSVIKDMVGTT 469
Cdd:cd07771 430 --EATAIGNLLVQLIALGEIKSLEEGRELVRNS 460
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
5-445 |
1.87e-09 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 60.17 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFIMKHNIGYDLHTPNV--------DVSEENpdEIFDAVLMTVKYIVRESG-IAKEDIKF- 74
Cdd:PLN02669 11 LGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHYgtkdgvyrDPKVNG--RIVSPTLMWVEALDLLLQkLAKEKFPFh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 75 ----ISLSAQMH--------------------SLIAMNEDNQRLTENITWADNRANDYADLIEKSYGG-FELYQRTGTPI 129
Cdd:PLN02669 89 kvvaISGSGQQHgsvywrkgasavlksldpskSLVAQLQDAFSTKDSPIWMDSSTTKQCREIEEAVGGaAELSKLTGSRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 130 HP--MSP-LSKIFWmrhEEPKIFKQTAMFADLKTYVLFQLYERFV-IDYSLGSATGMMNLEQLDWDNKALELL--GIERn 203
Cdd:PLN02669 169 YErfTGPqIRKIYE---TQPEVYHDTERISLVSSFMASLLVGDYAsIDETDGAGMNLMDIEKRCWSKAALEATapGLEE- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 204 QLPQLVPTTHVLTGMKKRYATLMGIDEQTPVIVGASDGVLSNLGVNSYQKGEVAVTIGTSGAIRTVINQPKTDEKGRIFC 283
Cdd:PLN02669 245 KLGKLAPAHAVAGKIHPYFVQRFGFSSNCLVVQWSGDNPNSLAGLTLSTPGDLAISLGTSDTVFGITREPQPSLEGHVFP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 284 YILDKDQYVIGGPVNNGGVVLRWLRDeilasevETAKRlgvdPYDVLTQIASRVKPGAEGLIFHPYLAGE-RAPLWNADA 362
Cdd:PLN02669 325 NPVDPESYMVMLCYKNGSLTREDIRN-------RCADG----SWDVFNKLLEQTPPLNGGKLGFYYKEHEiLPPLPVGFH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 363 R---GSFFGLTLSHKKEHM---------IRAALEGVLYNLYtvylALIEV--MNETPTTIKATGGFAKSEIWRQMMADIF 428
Cdd:PLN02669 394 RyilENFSGEALDGLVEEEvgefdppseVRAIIEGQFLSMR----AHAERfgMPVPPKRIIATGGASANQSILKLIASIF 469
|
490
....*....|....*..
gi 488368810 429 DTDLIVPESYESSCLGA 445
Cdd:PLN02669 470 GCDVYTVQRPDSASLGA 486
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-448 |
3.35e-09 |
|
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: 58.81 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 7 VDMGTTSTKAVLYDENGKFImkhnigYDLHTPNVDVSE-----ENPDEIFDAVLMTVKYIVREsgiakEDIKFISLSAQM 81
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVL------AERSTPNPEIEEdgypcEDVEAIWEWLLDSLAELAKR-----HRIDAINFTTHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 82 HSLIAMNEDNQRLT-----ENITWADNRANDYADlieksYGGFElyqRTGTPIHPMSpLS---KIFWMRHEEPKIFKQTA 153
Cdd:cd07772 74 ATFALLDENGELALpvydyEKPIPDEINEAYYAE-----RGPFE---ETGSPPLPGG-LNlgkQLYWLKREKPELFARAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 154 MFADLKTYVLFQLYERFVIDY-SLGSATGMMNLEQLDWdNKALELLGIERnQLPQLVPTTHVLTGMKKRYATLMGIDEQT 232
Cdd:cd07772 145 TILPLPQYWAWRLTGKAASEItSLGCHTDLWDFEKNEY-SSLVKKEGWDK-LFPPLRKAWEVLGPLRPDLARRTGLPKDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 233 PVIVGASDgvlSNLGVNSYQKGE----VAVTIGT-------SGAIRTVINQPKTDekgrIFCYILdkdqyVIGGPvnngg 301
Cdd:cd07772 223 PVGCGIHD---SNAALLPYLAAGkepfTLLSTGTwciamnpGNDLPLTELDLARD----CLYNLD-----VFGRP----- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 302 vvlrwlrdeilaseVETAKRLGVDPYDVLTQIASRVKPGAEGLIFHP-YLAGERAPLWNADARGSFFGLTLSHKKEHMIR 380
Cdd:cd07772 286 --------------VKTARFMGGREYERLVERIAKSFPQLPSLADLAkLLARGTFALPSFAPGGGPFPGSGGRGVLSAFP 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488368810 381 AALEgvLYNLYTVYLAL-----IEVMNETPTTIKATGGFAKSEIWRQMMADIFDTDLIVPESYES-SCLGACVL 448
Cdd:cd07772 352 SAEE--AYALAILYLALmtdyaLDLLGSGVGRIIVEGGFAKNPVFLRLLAALRPDQPVYLSDDSEgTALGAALL 423
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-79 |
3.82e-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: 51.82 E-value: 3.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488368810 1 MKYMIGVDMGTTSTKAVLYDENGKFIMKHNIGYDlhtpnvdvSEENPDEIFDAVLMTVKYIVRESGIAKEDIKFISLSA 79
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTP--------AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGV 74
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
62-206 |
8.38e-07 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 51.26 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 62 VRESGIAKEDIKFISLSAQMhslIAMNEDNQRLTENITWADNRANDYADLIEKSYGGFELYQRTGTPIHPMSPLSKIFWM 141
Cdd:PRK10640 49 VCEEGIRIDSIGIDTWGVDY---VLLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRAL 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488368810 142 RHEEPKIFKQTAMFADLKTYVLFQLYERFVIDYSLGSATGMMNLEQLDWDNKALELLGIERNQLP 206
Cdd:PRK10640 126 TEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFG 190
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
1-75 |
7.29e-06 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 47.41 E-value: 7.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488368810 1 MKYMIGVDMGTTSTKAVLYDENGKFIMKHnigYDLHTPNvdvSEENPDEIFDAVLmtvkyivRESGIAKEDIKFI 75
Cdd:COG1924 2 GMIYLGIDIGSTTTKAVLLDEDGEILASA---YLPTGGD---PLEAAKEALKELL-------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 |
5.82e-05 |
|
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: 44.84 E-value: 5.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFIMKHNI--GYDlhtpnvdvSEENPDEIFDAVLmtvkyivRESGIAKEDIKFI 75
Cdd:cd24036 2 AGIDVGSTTTKAVILDDKGKILGKAVIrtGTD--------PEKTAERALEEAL-------EEAGLSREDIEYI 59
|
|
| ASKHA_NBD_benz_CoA_BcrD_BadG |
cd24105 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ... |
5-76 |
1.96e-04 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar proteins; benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit D of benzoyl-CoA reductase.
Pssm-ID: 466955 Cd Length: 256 Bit Score: 42.96 E-value: 1.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFIMKHN--IGYDLhtpnvdvsEENPDEIFDAVLmtvkyivRESGIAKEDIKFIS 76
Cdd:cd24105 2 AGIDVGSGYTKAVIMDDGEKILAKRVerTRQRD--------EEVAREAYNEAL-------EEAGLKRDDIAYVA 60
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
5-77 |
7.87e-04 |
|
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.
Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 41.57 E-value: 7.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFIMKHNIGYD-LHTPNVDVSEENPDEIFDAVLmtvkyivRESGIAKEDIKFISL 77
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAIAGSAnFESVGVEAAERNLKDAITEAL-------EEAGLKLDDIEYMFL 67
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-166 |
1.32e-03 |
|
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: 41.24 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFI--MKHNIGYDLHTPNVDVSEENPDEIFDAVLMTVKYIVRESGIAKedIKFISLSAQMh 82
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLatSERPISYKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYI--VSGIGVSATC- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 83 SLIAMNED--------------NQRLTENIT-WADNRANDYADLIEKSYGGFELYQRTGTPIHPMSpLSKIFWM----RH 143
Cdd:cd07778 80 SMVVMQRDsdtsylvpynviheKSNPDQDIIfWMDHRASEETQWLNNILPDDILDYLGGGFIPEMA-IPKLKYLidliKE 158
|
170 180
....*....|....*....|...
gi 488368810 144 EEPKIFkqtaMFADLKTYVLFQL 166
Cdd:cd07778 159 DTFKKL----EVFDLHDWISYML 177
|
|
| ASKHA_NBD_BcrAD_BadFG-like |
cd24002 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ... |
5-74 |
2.28e-03 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ATPase 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, Methanocaldococcus jannaschii protein MJ0800, and Aquifex aeolicus hypothetical protein O66634, are also includes in this family. The members of the O66634-like group contain two copies of the BcrAD/BadFG-like region suggesting that they may structurally dimerize. The BcrAD/BadFG-like ATPase 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: 466852 [Multi-domain] Cd Length: 255 Bit Score: 39.72 E-value: 2.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFimkHNIGYDLHTPNVDVSEENPDEIFDAVLMtvkyivrESGIAKEDIKF 74
Cdd:cd24002 2 LGLDIGSTTSKAVLLDEGKNI---VATEYERSGTGTSGPIEAVKKTLEKFLL-------EKGVKEEDIAC 61
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| ASKHA_NBD_benz_CoA_BcrA_BadF |
cd24104 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ... |
4-75 |
3.29e-03 |
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nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar proteins; Benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit A of benzoyl-CoA reductase.
Pssm-ID: 466954 Cd Length: 253 Bit Score: 39.20 E-value: 3.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488368810 4 MIGVDMGTTSTKAVLYDENGKFimkhnIGYDLHT--PNVDVSEENpdeIFDAVLmtvkyivRESGIAKEDIKFI 75
Cdd:cd24104 1 AAGVDVGSTQTKAVIIDEDGEI-----VGRGLTNtgANVVVAAER---AFREAI-------EEAGIKEEEVEYV 59
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| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
5-70 |
5.48e-03 |
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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: 38.60 E-value: 5.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488368810 5 IGVDMGTTSTKAVLYDENGKFIMKHNIgydlHTPnvdvSEENPDEIFDAVLMTVKYIVRESGIAKE 70
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERV----PTP----AEEGPEAVLDRIAELIEELLAEAGVRER 58
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| DDE_Tnp_IS66_C |
pfam13817 |
IS66 C-terminal element; |
316-339 |
7.65e-03 |
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IS66 C-terminal element;
Pssm-ID: 433500 Cd Length: 39 Bit Score: 34.29 E-value: 7.65e-03
10 20
....*....|....*....|....*...
gi 488368810 316 VETAKRLGVDPY----DVLTQIASRVKP 339
Cdd:pfam13817 3 IETAKLNGLDPYayltDVLERLPDHHPA 30
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