|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-441 |
1.05e-143 |
|
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: 419.95 E-value: 1.05e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVN----IRAVLAAAG----PVDAIAIANQGES 74
Cdd:cd07769 2 ILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENtlevIREALAKAGisasDIAAIGITNQRET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAVSGEALSPVIVWQDARTAQTLAALppSATHLSKEI---CGLPLDPYFSASKLAWLVRHNPAVAEAKAAGRLRLG 151
Cdd:cd07769 82 TVVWDKKTGKPLYNAIVWQDRRTADICEEL--KAKGLEERIrekTGLPLDPYFSATKIKWILDNVPGARERAERGELLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 152 TTDAFFLDRLT--SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI------EGTPIRVSIV 223
Cdd:cd07769 160 TIDTWLIWKLTggKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTdpeglgAGIPIAGILG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 224 DQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGR-PSTGELLPTIAWQMQGaPAVFAIEGGVYDAGAAVEWAK-KIGLY 301
Cdd:cd07769 240 DQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPvPSKNGLLTTIAWQIGG-KVTYALEGSIFIAGAAIQWLRdNLGLI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 302 AENAELDWFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEA---ASAVAP 378
Cdd:cd07769 319 EDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAmekDSGIKL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799427 379 igDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI---------DVAAMRRETEIFAPD 441
Cdd:cd07769 399 --KELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLavgfwkdldELASLWQVDKRFEPS 468
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
3-462 |
1.81e-140 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 412.15 E-value: 1.81e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVN----IRAVLAAAG----PVDAIAIANQGES 74
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESvlavIREALAKAGisaeDIAAIGITNQRET 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAVSGEALSPVIVWQDARTAQTLAALppSATHLSKEI---CGLPLDPYFSASKLAWLVRHNPAVAEAKAAGRLRLG 151
Cdd:COG0554 85 TVVWDRKTGKPLYNAIVWQDRRTADICEEL--KADGLEDLIrekTGLVLDPYFSATKIKWILDNVPGARERAEAGELLFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 152 TTDAFFLDRLT--SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSIE------GTPIRVSIV 223
Cdd:COG0554 163 TIDSWLIWKLTggKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDpdlfgaEIPIAGIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 224 DQQAALYGHGCRTAGDCKITFGTGAFLLSVAGN-GRPSTGELLPTIAWQMQGAPaVFAIEGGVYDAGAAVEWAK-KIGLY 301
Cdd:COG0554 243 DQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDePVRSKNGLLTTIAWGLGGKV-TYALEGSIFVAGAAVQWLRdGLGLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 302 AENAELDWF--EGPSAirRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEAASAVAPI 379
Cdd:COG0554 322 DSAAESEALarSVEDN--GGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 380 G-DTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI---------DVAAMRRETEIFAP--DGSVGAE 447
Cdd:COG0554 400 PlKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLavgfwksleELAALWKVDRRFEPqmDEEERER 479
|
490
....*....|....*
gi 549799427 448 DHARFARAIDNARCW 462
Cdd:COG0554 480 LYAGWKKAVERTLGW 494
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-428 |
1.40e-127 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 379.32 E-value: 1.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRClvVIDGGTAEVVASRR--HTQFYPAANHVEHDPEELLVNIRAVLAAA----------GPVDAIAIAN 70
Cdd:PTZ00294 4 IGSIDQGTTSTRF--IIFDEKGNVVSSHQipHEQITPHPGWLEHDPEEILRNVYKCMNEAikklrekgpsFKIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 71 QGESCLAWDAVSGEALSPVIVWQDART---AQTLAALPPSATHLSKeICGLPLDPYFSASKLAWLVRHNPAVAEAKAAGR 147
Cdd:PTZ00294 82 QRETVVAWDKVTGKPLYNAIVWLDTRTydiVNELTKKYGGSNFFQK-ITGLPISTYFSAFKIRWMLENVPAVKDAVKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 148 LRLGTTDAFFLDRLT--SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI--------EGTP 217
Cdd:PTZ00294 161 LLFGTIDTWLIWNLTggKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTIsgeavpllEGVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 218 IRVSIVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNG-RPSTGELLPTIAWQM-QGAPAVFAIEGGVYDAGAAVEWA 295
Cdd:PTZ00294 241 ITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEiVFSKHGLLTTVCYQLgPNGPTVYALEGSIAVAGAGVEWL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 296 KK-IGLYAENAELDWFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEAAS 374
Cdd:PTZ00294 321 RDnMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESME 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 549799427 375 AVAPIG-DTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGIDV 428
Cdd:PTZ00294 401 KDAGIElNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAV 455
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
3-462 |
2.02e-124 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 370.80 E-value: 2.02e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVNIRAVLAAA------GP--VDAIAIANQGES 74
Cdd:TIGR01311 3 ILAIDQGTTSSRAIVFDKDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEAlakagiKPddIAAIGITNQRET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAVSGEALSPVIVWQDARTAQTLAALPpSATH--LSKEICGLPLDPYFSASKLAWLVRHNPAVAEAKAAGRLRLGT 152
Cdd:TIGR01311 83 TVVWDKATGKPLYNAIVWQDRRTASICEELK-AEGYgeFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERGELLFGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 153 TDAFFLDRLT--SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI------EGTPIRVSIVD 224
Cdd:TIGR01311 162 IDTWLIWNLTggKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTdpgllgAEIPITGVLGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 225 QQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRP-STGELLPTIAWQMQGAPAVFAIEGGVYDAGAAVEWAK-KIGLYA 302
Cdd:TIGR01311 242 QQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPViSKHGLLTTVAYQLGGKKPVYALEGSVFVAGAAVQWLRdNLKLIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 303 ENAELDWFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEAASAVAPI-GD 381
Cdd:TIGR01311 322 HAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVeIT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 382 TISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI---------DVAAMRRETEIFAPDGS--VGAEDHA 450
Cdd:TIGR01311 402 KLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLavgywksleEIEALWRVEKTFEPEMDeeEREARYA 481
|
490
....*....|..
gi 549799427 451 RFARAIDNARCW 462
Cdd:TIGR01311 482 GWKEAVKRSLGW 493
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-440 |
2.02e-122 |
|
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: 365.66 E-value: 2.02e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVN----IRAVLAAAG----PVDAIAIANQGES 74
Cdd:cd07786 2 ILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESqlavAREALAKAGirasDIAAIGITNQRET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAVSGEALSPVIVWQDARTAQTLAALppSATHLSKEIC---GLPLDPYFSASKLAWLVRHNPAVAEAKAAGRLRLG 151
Cdd:cd07786 82 TVVWDRETGKPVYNAIVWQDRRTADICEEL--KAEGHEEMIRektGLVLDPYFSATKIRWILDNVPGARERAERGELAFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 152 TTDAFFLDRLT--SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSIEGT------PIRVSIV 223
Cdd:cd07786 160 TIDSWLIWKLTggKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDllgaeiPIAGIAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 224 DQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRP-STGELLPTIAWQMQGAPaVFAIEGGVYDAGAAVEW-------- 294
Cdd:cd07786 240 DQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVrSKNGLLTTIAWQLGGKV-TYALEGSIFIAGAAVQWlrdglgli 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 295 --AKKIGLYAENAELDwfegpsairRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEA 372
Cdd:cd07786 319 esAAETEALARSVPDN---------GGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799427 373 ASAVAPIG-DTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI---------DVAAMRRETEIFAP 440
Cdd:cd07786 390 MEADSGIPlKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLavglwksldELAKLWQVDRRFEP 467
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
3-428 |
6.60e-121 |
|
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: 362.23 E-value: 6.60e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVidGGTAEVVASRR--HTQFYPAANHVEHDPEELLVNIR-------AVLAAAGP----VDAIAIA 69
Cdd:cd07792 3 VGAIDQGTTSTRFIVF--DSTGELVASHQveHKQIYPKPGWVEHDPMEILESVYecieeavEKLKALGIspsdIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 70 NQGESCLAWDAVSGEALSPVIVWQDARTAQTLAAL----PPSATHLsKEICGLPLDPYFSASKLAWLVRHNPAVAEAKAA 145
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELsaktPGGKDHF-RKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 146 GRLRLGTTDAFFLDRLT-----SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKV-------GPVDGgfGSI 213
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTggkngGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIrsssevyGKIAS--GPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 214 EGTPIRVSIVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGR-PSTGELLPTIAWQM-QGAPAVFAIEGGVYDAGAA 291
Cdd:cd07792 238 AGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPvFSKHGLLTTVAYKLgPDAPPVYALEGSIAIAGAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 292 VEWAK-KIGLYAENAELdwfegpSAIRR------GLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIAL 364
Cdd:cd07792 318 VQWLRdNLGIISSASEV------ETLAAsvpdtgGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549799427 365 LTARLIEAASAVAPIGDT-ISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGIDV 428
Cdd:cd07792 392 QTREILDAMNKDSGIPLTsLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAV 456
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-440 |
9.52e-103 |
|
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: 315.66 E-value: 9.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVNIRAVL--------AAAGPVDAIAIANQGES 74
Cdd:cd07793 2 ILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIkealknagLTPEDIAAIGISTQRNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAVSGEALSPVIVWQDARTAQ---------------TLAALPPSATHLSKEICG--LPLDPYFSASKLAWLVRHNP 137
Cdd:cd07793 82 FLTWDKKTGKPLHNFITWQDLRAAElceswnrslllkalrGGSKFLHFLTRNKRFLAAsvLKFSTAHVSIRLLWILQNNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 138 AVAEAKAAGRLRLGTTDAFFLDRLT--SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSIE- 214
Cdd:cd07793 162 ELKEAAEKGELLFGTIDTWLLWKLTggKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 215 -----GTPIRVSIVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNgRP--STGELLPTIAWQMQGAPaVFAIEGGVYD 287
Cdd:cd07793 242 sifgaEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGS-KPhaSVKGLYPLVGWKIGGEI-TYLAEGNASD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 288 AGAAVEWAKKIGLYAENAELDWFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTA 367
Cdd:cd07793 320 TGTVIDWAKSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 368 RLIEAASAVAPIG-DTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI---------DVAAMRRETEI 437
Cdd:cd07793 400 QLLETMEKETSIKiSSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLasgiwkskeELKKLRKIEKI 479
|
...
gi 549799427 438 FAP 440
Cdd:cd07793 480 FEP 482
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
3-428 |
3.50e-96 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 298.66 E-value: 3.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVNIRAVLAAA--------GPVDAIAIANQGES 74
Cdd:PRK00047 7 ILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEAlakagispDQIAAIGITNQRET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAVSGEALSPVIVWQDARTAQTLAALPPSA-THLSKEICGLPLDPYFSASKLAWLVRHNPAVAEAKAAGRLRLGTT 153
Cdd:PRK00047 87 TVVWDKETGRPIYNAIVWQDRRTADICEELKRDGyEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGELLFGTI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 154 DAFFLDRLT--SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSIEGT-------PIRVSIVD 224
Cdd:PRK00047 167 DTWLVWKLTggKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgffggevPIAGIAGD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 225 QQAALYGHGCRTAGDCKITFGTGAFLLSvagngrpSTGE--------LLPTIAWQMQGAPaVFAIEGGVYDAGAAVEWAK 296
Cdd:PRK00047 247 QQAALFGQLCFEPGMAKNTYGTGCFMLM-------NTGEkavksengLLTTIAWGIDGKV-VYALEGSIFVAGSAIQWLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 297 -KIGLYAENAELDWFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEAASA 375
Cdd:PRK00047 319 dGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 549799427 376 VAPIG-DTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGIDV 428
Cdd:PRK00047 399 DSGIRlKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAV 452
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
3-442 |
6.19e-92 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 288.14 E-value: 6.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRclVVIDGGTAEVVAS--RRHTQFYPAANHVEHDPEELLVNIRAVLAAA------------GPVDAIAI 68
Cdd:PLN02295 2 VGAIDQGTTSTR--FIIYDRDARPVAShqVEFTQIYPQAGWVEHDPMEILESVLTCIAKAlekaaakghnvdSGLKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 69 ANQGESCLAWDAVSGEALSPVIVWQDARTAQTLAAL----PPSATHLsKEICGLPLDPYFSASKLAWLVRHNPAVAEAKA 144
Cdd:PLN02295 80 TNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLekelSGGRKHF-VETCGLPISTYFSATKLLWLLENVDAVKEAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 145 AGRLRLGTTDAFFLDRLTSS-----FRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI------ 213
Cdd:PLN02295 159 SGDALFGTIDSWLIWNLTGGasggvHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIakgwpl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 214 EGTPIRVSIVDQQAALYGHGCRtAGDCKITFGTGAFLLSVAGNGR-PSTGELLPTIAWQM-QGAPAVFAIEGGVYDAGAA 291
Cdd:PLN02295 239 AGVPIAGCLGDQHAAMLGQRCR-PGEAKSTYGTGCFILLNTGEEVvPSKHGLLTTVAYKLgPDAPTNYALEGSVAIAGAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 292 VEWAK-KIGLYAENAELDWFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLI 370
Cdd:PLN02295 318 VQWLRdNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799427 371 EAASAVAPIGDT------ISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGIDVAAMRREtEIFAPDG 442
Cdd:PLN02295 398 DAMRKDAGEEKShkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEE-EIFASEK 474
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-455 |
3.15e-72 |
|
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: 236.27 E-value: 3.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVN----IRAVLAAAG----PVDAIAIANQGES 74
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAvveaIRELLAKAGvdpeEIAAIGVSGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAvSGEALSPVIVWQDARTAQTLAAL----PPSATHlskEICGLPLDPYFSASKLAWLVRHNPAVAEAkaagrlrl 150
Cdd:COG1070 83 LVLLDA-DGEPLRPAILWNDTRAAAEAAELreelGEEALY---EITGNPLHPGFTAPKLLWLKENEPEIFAR-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 151 gtTDAFFL--D----RLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI----------- 213
Cdd:COG1070 151 --IAKVLLpkDylryRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLtaeaaaetglp 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 214 EGTPIRVSIVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRPSTGELLPTIAWqmqGAPAVFAIEGGVYDAGAAVE 293
Cdd:COG1070 229 AGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCH---AVPGRWLPMGATNNGGSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 294 WAKKIGLYAENAELDWFEG------PSAirRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTA 367
Cdd:COG1070 306 WFRDLFADGELDDYEELNAlaaevpPGA--DGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 368 RLIEAASAVAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI----------DVAAMRRETEI 437
Cdd:COG1070 384 DGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVglglyddleeAAAAMVRVGET 463
|
490
....*....|....*...
gi 549799427 438 FAPDgsvgAEDHARFARA 455
Cdd:COG1070 464 IEPD----PENVAAYDEL 477
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-426 |
1.04e-68 |
|
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: 225.54 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVNIRAVL------AAAGPVDAIAIANQGESCL 76
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIreaaaqAGPDPIAAISVSSQGESGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 77 AWDAvSGEALSPVIVWQDARTAQTLAALppsATHLSKE----ICGLPLDPYFSASKLAWLVRHNPavaEAKAAGRLRLGT 152
Cdd:cd07773 82 PVDR-DGEPLGPAIVWFDPRGKEEAEEL---AERIGAEelyrITGLPPSPMYSLAKLLWLREHEP---EIFAKAAKWLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 153 TDaFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPK-------VGPVDGGFGSIEGTPIRVSIV-- 223
Cdd:cd07773 155 AD-YIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPElvpsgtvIGTVTPEAAEELGLPAGTPVVvg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 224 --DQQAALYGHGCRTAGDCKITFGTGAFLLSVagngrpsTGELLPTIAWQMQGAPAVFAIEGGVY------DAGAAVEWA 295
Cdd:cd07773 234 ghDHLCAALGAGVIEPGDVLDSTGTAEALLAV-------VDEPPLDEMLAEGGLSYGHHVPGGYYylagslPGGALLEWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 296 KK---IGLYAENAELDWFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEA 372
Cdd:cd07773 307 RDlfgGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 549799427 373 ASAVAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI 426
Cdd:cd07773 387 LEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGV 440
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-441 |
1.37e-64 |
|
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: 214.30 E-value: 1.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEEL---LVN-IRAVLAAAGP----VDAIAIANQGES 74
Cdd:cd07779 2 ILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWwdaLCEaLKEAVAKAGVdpedIAAIGLTSQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAvSGEALSPVIVWQDARTAqtlaalppsathlskeicglpldpyfsasklawlvrhnpavaeakaagrlRLGTTD 154
Cdd:cd07779 82 FVPVDE-DGRPLRPAISWQDKRTA--------------------------------------------------KFLTVQ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 155 AFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKV---GPVDGG--------FGSIEGTPIRVSIV 223
Cdd:cd07779 111 DYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELvppGTVIGTltkeaaeeTGLPEGTPVVAGGG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 224 DQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRPSTGELLPTIAWQMQGApavFAIEGGVYDAGAAVEWAKKIglYAE 303
Cdd:cd07779 191 DQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGK---WVLEGSINTGGSAVRWFRDE--FGQ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 304 NAELDWFEGPSAIR-------------RGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLI 370
Cdd:cd07779 266 DEVAEKELGVSPYEllneeaaksppgsDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 371 EA-ASAVAPIgDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI------D----VAAMRRETEIFA 439
Cdd:cd07779 346 EAmEKAGVPI-EEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVgagiypDfeeaVKAMVRVTDTFE 424
|
..
gi 549799427 440 PD 441
Cdd:cd07779 425 PD 426
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-455 |
1.80e-55 |
|
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: 191.62 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVNIRAVLAAA------GPVDAIAIANQGESCL 76
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVlaklggGEVDAIGFSSAMHSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 77 AWDAvSGEALSPVIVWQDARTAQTLAALppSATHLSKEI---CGLPLDPYFSASKLAWLVRHNPAVAEAKAagrlRLGTT 153
Cdd:cd07770 82 GVDE-DGEPLTPVITWADTRAAEEAERL--RKEGDGSELyrrTGCPIHPMYPLAKLLWLKEERPELFAKAA----KFVSI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 154 DAFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI-----------EGTPIRVSI 222
Cdd:cd07770 155 KEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLkpefaerlgllAGTPVVLGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 223 VDQQAALYGHGCRTAGDCKITFGT-GAFLLSVAgngRPSTGEllPTIAWQMQGAPAVFAIEGGVYDAGAAVEWAKKI--G 299
Cdd:cd07770 235 SDGALANLGSGALDPGRAALTVGTsGAIRVVSD---RPVLDP--PGRLWCYRLDENRWLVGGAINNGGNVLDWLRDTllL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 300 LYAENAELD-WFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEAASAVAP 378
Cdd:cd07770 310 SGDDYEELDkLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 379 IGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLA--------ELCGIDVAAMRRETEIFAPDgsvgAEDHA 450
Cdd:cd07770 390 PVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAAllalealgLISSLEADELVKIGKVVEPD----PENHA 465
|
....*
gi 549799427 451 RFARA 455
Cdd:cd07770 466 IYAEL 470
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-421 |
7.78e-55 |
|
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: 187.77 E-value: 7.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEE----LLVNIRAVLAAAG----PVDAIAIANQGES 74
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDwwqaVVEAIREVLAKAGidpsDIAAIGISGQMPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAvSGEALSPVIVWQDARTaqtlaalppsathlskeicglpldpyfsasklawlvrhnpavaeakaagrlRLGTTD 154
Cdd:cd00366 82 VVLVDA-DGNPLRPAIIWLDRRA---------------------------------------------------KFLQPN 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 155 AFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI-----------EGTPIRVSIV 223
Cdd:cd00366 110 DYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVtpeaaeetglpAGTPVVAGGG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 224 DQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRPSTGELLPTIAwqmqGAPAVFAIEGGVYDAGAAVEWAKKI----- 298
Cdd:cd00366 190 DTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCH----VVPGLWLLEGAINTGGASLRWFRDEfgeee 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 299 GLYAENAELD-WFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEAASAVA 377
Cdd:cd00366 266 DSDAEYEGLDeLAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELG 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 549799427 378 PIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLA 421
Cdd:cd00366 346 VKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAA 389
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
6-454 |
5.94e-53 |
|
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: 185.05 E-value: 5.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 6 IDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEE----LLVNIRAVLAAAGP----VDAIAIANQGESCLA 77
Cdd:cd07808 5 IDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDwwqaTKEALRELLAKAGIspsdIAAIGLTGQMHGLVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 78 WDAvSGEALSPVIVWQDARTAQTLAALPPSATHLSKEICGLPLDPYFSASKLAWLVRHNPAVAEAkaagrlrlgtTDAFF 157
Cdd:cd07808 85 LDK-NGRPLRPAILWNDQRSAAECEELEARLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFAR----------IRKIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 158 L--D----RLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI-----------EGTPIRV 220
Cdd:cd07808 154 LpkDylryRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLtpeaaeelglpEGTPVVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 221 SIVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRPSTGELLPTIA------WQMQGApaVFAieggvydAGAAVEW 294
Cdd:cd07808 234 GAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPhavpgkWYAMGV--TLS-------AGLSLRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 295 AKKIgLYAENAELDWF----EGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLI 370
Cdd:cd07808 305 LRDL-FGPDRESFDELdaeaAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 371 EAASAVAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI----------DVAAMRRETEIFAP 440
Cdd:cd07808 384 EVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVgagvfddleeAAAACIKIEKTIEP 463
|
490
....*....|....
gi 549799427 441 DgsvgAEDHARFAR 454
Cdd:cd07808 464 D----PERHEAYDE 473
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-454 |
4.67e-51 |
|
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: 180.02 E-value: 4.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTR-CLVVIDGgtaEVVAS--RRHTQFYPAANHVEHDPEE----LLVNIRAVLAAAGP----VDAIAIANQ 71
Cdd:cd07805 2 ILAIDLGTSGVKaALVDLDG---ELVASafAPYPTYYPKPGWAEQDPEDwwdaVCRATRALLEKSGIdpsdIAAIAFSGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 72 GESCLAWDAvSGEALSPVIVWQDART---AQTLAALPPSATHLSKeICGLPLDPYFSASKLAWLVRHNPAVAEAKAAgrl 148
Cdd:cd07805 79 MQGVVPVDK-DGNPLRNAIIWSDTRAaeeAEEIAGGLGGIEGYRL-GGGNPPSGKDPLAKILWLKENEPEIYAKTHK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 149 RLGTTDaFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPK-------VGPVDGG----FGSIEGTP 217
Cdd:cd07805 154 FLDAKD-YLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPElvpstevVGELTPEaaaeLGLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 218 IRVSIVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAgnGRPSTGEllptiawqmqgAPAVFAIEGGVYD---------- 287
Cdd:cd07805 233 VVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHV--PKPKTDP-----------DHGIFTLASADPGryllaaeqet 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 288 AGAAVEWAKKIGLYAENAELDWFE---------GPSAirRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAV 358
Cdd:cd07805 300 AGGALEWARDNLGGDEDLGADDYElldelaaeaPPGS--NGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 359 LEGIALLTARLIEAASAVAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPA-MRELTALGLAELCGI---------DV 428
Cdd:cd07805 378 LEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPEnPQEAGALGAALLAAVglgllksfdEA 457
|
490 500
....*....|....*....|....*.
gi 549799427 429 AAMRRETEIFAPDgsvgAEDHARFAR 454
Cdd:cd07805 458 KALVKVEKVFEPD----PENRARYDR 479
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-231 |
4.80e-45 |
|
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: 157.50 E-value: 4.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVNIRAVLAAAGP--------VDAIAIANQGES 74
Cdd:pfam00370 2 YLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlgislkqIKGIGISNQGHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAvSGEALSPVIVWQDARTAQTLAALP-PSATHLSKEICGLPLDPYFSASKLAWLVRHNPAVAEAKAAgrlrLGTT 153
Cdd:pfam00370 82 TVLLDK-NDKPLYNAILWKDRRTAEIVENLKeEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHK----FLTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 154 DAFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGP-----------VDGGFGSIEGTPIRVSI 222
Cdd:pfam00370 157 HDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVEsseiygelnpeLAAMWGLDEGVPVVGGG 236
|
....*....
gi 549799427 223 VDQQAALYG 231
Cdd:pfam00370 237 GDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-426 |
5.19e-39 |
|
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: 146.52 E-value: 5.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 6 IDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVN----IRAVLAAAGP----VDAIAIANQGESCLA 77
Cdd:cd07804 5 IDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAvceiIRELLAKAGIspkeIAAIGVSGLVPALVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 78 WDAvSGEALSPVIVWQDARTAQTLAALppsATHLSK----EICGLPLDPYFSASKLAWLVRHNPAVAeAKAAgrlRLGTT 153
Cdd:cd07804 85 VDE-NGKPLRPAILYGDRRATEEIEWL---NENIGEdrifEITGNPLDSQSVGPKLLWIKRNEPEVF-KKTR---KFLGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 154 DAFFLDRLTSSFRTDLATASRT-GLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI-----------EGTPIRVS 221
Cdd:cd07804 157 YDYIVYKLTGEYVIDYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVtkeaaeetglaEGTPVVAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 222 IVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRPstgelLPTIAWQMQGAPAVFAIEGGVYDAGAAVEWAKKiGLY 301
Cdd:cd07804 237 TVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPT-----DPRLWLDYHDIPGTYVLNGGMATSGSLLRWFRD-EFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 302 AENAELDWFEGPSAIRR-------------GLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTAR 368
Cdd:cd07804 311 GEEVEAEKSGGDSAYDLldeeaekippgsdGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRH 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799427 369 LIEAASAVAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI 426
Cdd:cd07804 391 HLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGV 448
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-421 |
1.60e-36 |
|
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: 139.28 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVNIRAVLAA------AGPVDAIAIANQGESCL 76
Cdd:cd07783 2 FLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRElpaelrPRRVVAIAVDGTSGTLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 77 AWDAvSGEALSPVIVWQDARtAQTLAALPPSATHLSKEICGLPLDPYFSASKLAWLVRHNPAVAEAKAAGrlrLGTTDaF 156
Cdd:cd07783 82 LVDR-EGEPLRPAIMYNDAR-AVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKF---LHQAD-W 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 157 FLDRLTSSF-RTDLATASRTGlLDLSTGDWSPELCALHGVTMDCLPKV-------GPVDGGFGSI----EGTPIRVSIVD 224
Cdd:cd07783 156 LAGRLTGDRgVTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVvapgtviGTLTAEAAEElglpAGTPVVAGTTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 225 QQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRPSTGEL-----LPTIAWqmqgapavfaIEGGVYDAGAAV-EWAKKI 298
Cdd:cd07783 235 SIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGvyshrHGDGYW----------LVGGASNTGGAVlRWFFSD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 299 GLYAE-NAELDwFEGPSairrGLAFVP-AFSGLAAPYWDRHAVPLFIGMNHatERSDMVRAVLEGIALLTARLIEAA-SA 375
Cdd:cd07783 305 DELAElSAQAD-PPGPS----GLIYYPlPLRGERFPFWDPDARGFLLPRPH--DRAEFLRALLEGIAFIERLGYERLeEL 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 549799427 376 VAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRElTALGLA 421
Cdd:cd07783 378 GAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE-AALGAA 422
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
5-426 |
1.47e-34 |
|
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: 134.27 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 5 AIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANH--VEHDPEELLVNI----RAVLAAAGP----VDAIAIANQGES 74
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPdaKEFDPEELWEKIceaiREALKKAGIspedISAVSSTSQREG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAvSGEALS--PVIvwqDARTAQTLAALPPSATHLSKEICGLPLDPYFSASKLAWLVRHNPAVAEaKAAgrlRLGT 152
Cdd:cd07798 84 IVFLDK-DGRELYagPNI---DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFE-RIA---TVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 153 TDAFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPK-------VGPVDG----GFGSIEGTPIRVS 221
Cdd:cd07798 156 ISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEivpsgtvLGTVSEeaarELGLPEGTPVVVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 222 IVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAGN-----------GRPSTGELlptiaWQMQGAPAVfaieggvydAGA 290
Cdd:cd07798 236 GADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEpiidperrlwtGCHLVPGK-----WVLESNAGV---------TGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 291 AVEWAKKIGLYAENAELDWFEGPSAIRRGLAF-VPAFSGLAAPYWDRHAVPL------FIGMNHATERSDMVRAVLEGIA 363
Cdd:cd07798 302 NYQWLKELLYGDPEDSYEVLEEEASEIPPGANgVLAFLGPQIFDARLSGLKNggflfpTPLSASELTRGDFARAILENIA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799427 364 LLTARLIEAASAVAPIG-DTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI 426
Cdd:cd07798 382 FAIRANLEQLEEVSGREiPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAV 445
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
6-426 |
1.10e-32 |
|
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: 128.82 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 6 IDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEELLVN----IRAVLAAAGP----VDAIAIANQGESCLA 77
Cdd:cd07802 5 IDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQAtaeaIRELLEKSGVdpsdIAGVGVTGHGNGLYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 78 WDAVsGEALSPVIVWQDARTAQTLAALPPSATHLS-KEICGLPLDPYFSASKLAWLVRHNPAVAEAkaagrlrlgtTDAF 156
Cdd:cd07802 85 VDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEKvYPLTGQPLWPGQPVALLRWLKENEPERYDR----------IRTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 157 FL--D----RLTSSFRTDLATASrTGLLDLSTGDWSPELCALHGVT--MDCLPKVGPVDGGFGSI-----------EGTP 217
Cdd:cd07802 154 LFckDwiryRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVtaeaaaltglpEGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 218 IRVSIVDQQAALYGHGCRTAGDCKITFGTgafllsVAGNGRPSTGELLPTIAWQMQ--GAPAVFAIEGGVYDAGAAVEWA 295
Cdd:cd07802 233 VAAGAFDVVASALGAGAVDEGQLCVILGT------WSINEVVTDEPVVPDSVGSNSlhADPGLYLIVEASPTSASNLDWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 296 kkIGLYAENAELDWFEGPSAIRRGLAFVPAFSG-------LAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTAR 368
Cdd:cd07802 307 --LDTLLGEEKEAGGSDYDELDELIAAVPPGSSgviflpyLYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRD 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799427 369 LIEAASAVAPIgDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI 426
Cdd:cd07802 385 HLERLLVARKP-ETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAV 441
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-421 |
5.63e-32 |
|
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: 126.57 E-value: 5.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 5 AIDQGTTSTrCLVVIDGGTAEVVASRRHTQFYPAA----NHVEHDPEELLVNIRAVLA-----AAGPVDAIAIANQGESC 75
Cdd:cd07777 4 GIDIGTTSI-KAALLDLESGRILESVSRPTPAPISsddpGRSEQDPEKILEAVRNLIDelpreYLSDVTGIGITGQMHGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 76 LAWDAvSGEALSPVIVWQDARTAQTLAALPPSATHLSKEICGLPLDPYFSASKLAWLVRHNPAVAEAKAAGRLrlgtTDa 155
Cdd:cd07777 83 VLWDE-DGNPVSPLITWQDQRCSEEFLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGPLPSKADRAGTI----GD- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 156 FFLDRLT--SSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVD--GGFGSIE---GTPIRVSIVDQQAA 228
Cdd:cd07777 157 YIVARLTglPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGeiVGTLSSAlpkGIPVYVALGDNQAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 229 LYGHGCRTAGDCKITFGTGAfLLSVAGNG---------RP-STGELLPTIAwqmqgapavfAIEGG-VYD--AGAAVEWA 295
Cdd:cd07777 237 VLGSGLNEENDAVLNIGTGA-QLSFLTPKfelsgsveiRPfFDGRYLLVAA----------SLPGGrALAvlVDFLREWL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 296 KKIGLYAENAEL-DWFE--GPSAIRRGLAFVPAFSGLAAPYwDRHAVPLFIGMNHATErSDMVRAVLEGIALLTARLIEA 372
Cdd:cd07777 306 RELGGSLSDDEIwEKLDelAESEESSDLSVDPTFFGERHDP-EGRGSITNIGESNFTL-GNLFRALCRGIAENLHEMLPR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 549799427 373 ASAVAPIGDTISIDGG-LSNSRYFVRFLAAASGRTICVPAMRELTALGLA 421
Cdd:cd07777 384 LDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-421 |
1.87e-30 |
|
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: 122.66 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 4 AAIDQGTTSTRcLVVIDGGTAEVVAS--RRHTQFYPAANHVEHDPEELLVNIRAVLAAAGP--------VDAIAIANQGE 73
Cdd:cd07809 3 LGIDLGTQSIK-AVLIDAETGRVVASgsAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKdagaelrdVAAIGISGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 74 SCLAWDAvSGEALSPVIVWQDARTAQTLAALPPSATHLSKEICGLPLDPYFSASKLAWLVRHNPavaeaKAAGRLRLGTT 153
Cdd:cd07809 82 GLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARFTASKLLWLKENEP-----EHYARIAKILL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 154 DAFFLD-RLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVT---MDCLPKVGPVDGGFGSI-----------EGTPI 218
Cdd:cd07809 156 PHDYLNwKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSrdlRDLLPEVLPAGEVAGRLtpegaeelglpAGIPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 219 RVSIVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAgnGRPSTGEllptiawqmQGAPAVFAIEGGVY--------DAGA 290
Cdd:cd07809 236 APGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVS--DKPVSDP---------HGRVATFCDSTGGMlplinttnCLTA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 291 AVEWAKKI--GLYAENAELdwFEGPSAIRRGLAFVPAFSGLAAPYWdRHAVPLFIGMNHA-TERSDMVRAVLEGIALLTA 367
Cdd:cd07809 305 WTELFRELlgVSYEELDEL--AAQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLR 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 549799427 368 RLIEAASAVAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLA 421
Cdd:cd07809 382 YGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAA 435
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-421 |
1.49e-26 |
|
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: 111.56 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEEL----LVNIRAVLAAAGP----VDAIAIANQGES 74
Cdd:cd24121 2 LIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETwqavVATIREVVAKLDVlpdrVAAIGVTGQGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 75 CLAWDAvSGEALSPVIVWQDARTAQTLAALPPSAT-HLSKEICGLPLDPYFSASKLAWLVRHNP-AVAEAKAAGRLRlgt 152
Cdd:cd24121 82 TWLVDE-DGRPVRDAILWLDGRAADIVERWQADGIaEAVFEITGTGLFPGSQAAQLAWLKENEPeRLERARTALHCK--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 153 tDAFFLdRLTSSFRTDLATASRTgLLDLSTGDWSPELCALHGVTmDCLPKVGPVDGGFGSI--------------EGTPI 218
Cdd:cd24121 158 -DWLFY-KLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLE-ELRHLLPPIRPGTEVIgpltpeaaaatglpAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 219 RVSIVDQQAALYGHGCRTAGDCKITFGTGAF---LLSVAGNGRPSTGELLPtIAWQ---------MQGAPAVFAIEGGVY 286
Cdd:cd24121 234 VLGPFDVVATALGSGAIEPGDACSILGTTGVhevVVDEPDLEPEGVGYTIC-LGVPgrwlramanMAGTPNLDWFLRELG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 287 DAGAAVEWAKKIGLYAEnaeLD-WFEGPSAIRRGLAFVPAFS--GLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIA 363
Cdd:cd24121 313 EVLKEGAEPAGSDLFQD---LEeLAASSPPGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 549799427 364 LLTARLIEAASAVApigDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLA 421
Cdd:cd24121 390 LAMRDCYEHMGEDP---GELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAA 444
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
240-426 |
5.74e-25 |
|
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: 101.63 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 240 CKITFGTGAFLLSVAGNGRPSTGELLPTIAWQMqgAPAVFAIEGGVYDAGAAVEW-------------AKKIGLYAENAE 306
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEM--LPGYWGLEGGQSAAGSLLAWllqfhglreelrdAGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 307 LDWfegpSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEAASAVAPI-GDTISI 385
Cdd:pfam02782 79 LAA----VAPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHpIDTIHV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 549799427 386 DGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGI 426
Cdd:pfam02782 155 SGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAV 195
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
6-404 |
5.20e-23 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 101.58 E-value: 5.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 6 IDQGTTSTRCLVVIDGGtaEVVASR--RHTQFYPAANHVEHDPEEL-LVNIRAVLA-----AAGPVDAIAIANQGESCLA 77
Cdd:PRK15027 5 IDLGTSGVKVILLNEQG--EVVASQteKLTVSRPHPLWSEQDPEQWwQATDRAMKAlgdqhSLQDVKALGIAGQMHGATL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 78 WDAvSGEALSPVIVWQDARTAQTLAALPPSAThLSKEICGLPLDPYFSASKLAWLVRHNPAVAEAKAAGRLrlgtTDAFF 157
Cdd:PRK15027 83 LDA-QQRVLRPAILWNDGRCAQECALLEARVP-QSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLL----PKDYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 158 LDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKV-------GPVDGGFGSIEGTPiRVSIV----DQQ 226
Cdd:PRK15027 157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALyegseitGALLPEVAKAWGMA-TVPVVagggDNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 227 AALYGHGCRTAGDCKITFGTGAFLLSVAgNGRPSTGEllPTIAWQMQGAPAVFAIEGGVYDAGAAVEWAKKI-------G 299
Cdd:PRK15027 236 AGAVGVGMVDANQAMLSLGTSGVYFAVS-EGFLSKPE--SAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLtglsnvpA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 300 LYAENAELDWFEGPsairrgLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVRAVLEGIALLTARLIEAASAVAPI 379
Cdd:PRK15027 313 LIAAAQQADESAEP------VWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIK 386
|
410 420
....*....|....*....|....*
gi 549799427 380 GDTISIDGGLSNSRYFVRFLAAASG 404
Cdd:PRK15027 387 PQSVTLIGGGARSEYWRQMLADISG 411
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-428 |
9.50e-22 |
|
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: 97.79 E-value: 9.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 3 IAAIDQGTTSTRCLVVIDGGTAEVVASR--RHTQF--YPAANH--VEHDPEELLVNIRAVLAAAG--PVDAIAIANQG-- 72
Cdd:cd07775 2 LLALDAGTGSGRAVIFDLEGNQIAVAQRewRHKEVpdVPGSMDfdTEKNWKLICECIREALKKAGiaPKSIAAISTTSmr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 73 ESCLAWDAVSGE--ALSPVivwqDARTAQTLAALPPSATHLSKEIcglpldpyFSAS----------KLAWLVRHNPAVA 140
Cdd:cd07775 82 EGIVLYDNEGEEiwACANV----DARAAEEVSELKELYNTLEEEV--------YRISgqtfalgaipRLLWLKNNRPEIY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 141 eAKAAgrlRLGTTDAFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVGPVDGGFGSI------- 213
Cdd:cd07775 150 -RKAA---KITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVtkeaaee 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 214 ----EGTPIRVSIVDQQAALYGHGCRTAGDCKITFGTgaFLLSVAGNGRPSTGELLpTIAWQMQGAPAVFAIEGGVYDAG 289
Cdd:cd07775 226 tglkEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGS--FWQQEVNTAAPVTDPAM-NIRVNCHVIPDMWQAEGISFFPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 290 AAVEWAKKiGLYAENAELDWFEGPSA---IRRGLAFVPAFS-GLAAPYWD-------RHAVPLFIGMN---HATERSDMV 355
Cdd:cd07775 303 LVMRWFRD-AFCAEEKEIAERLGIDAydlLEEMAKDVPPGSyGIMPIFSDvmnyknwRHAAPSFLNLDidpEKCNKATFF 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549799427 356 RAVLEGIALLTA---RLIEAASAVAPigDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAELCGIDV 428
Cdd:cd07775 382 RAIMENAAIVSAgnlERIAEFSGIFP--DSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGA 455
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
6-454 |
1.24e-20 |
|
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: 94.53 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 6 IDQGTTSTRCLVViDGGTAEVVASrrHTQFY------PAANHVEHDPEE----LLVNIRAVLAAAGP----VDAIAIANQ 71
Cdd:cd07781 5 IDFGTQSVRAGLV-DLADGEELAS--AVVPYptgyipPRPGWAEQNPADyweaLEEAVRGALAEAGVdpedVVGIGVDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 72 GESCLAWDAvSGEALSPVIVWQDART---AQTLAALPPSATHLSKEICGLPldpyFSA----SKLAWLVRHNPAVAEAka 144
Cdd:cd07781 82 SSTVVPVDE-DGNPLAPAILWMDHRAqeeAAEINETAHPALEYYLAYYGGV----YSSewmwPKALWLKRNAPEVYDA-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 145 agrlrlgtTDAF--FLD----RLTSSFRTDLATASRTGLLDLSTGDWSPE-LCALH---GVTMDCLP-KVGPVDGGFGSI 213
Cdd:cd07781 155 --------AYTIveACDwinaRLTGRWVRSRCAAGHKWMYNEWGGGPPREfLAALDpglLKLREKLPgEVVPVGEPAGTL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 214 -----------EGTPIRVSIVDQQAALYGHGCRTAGDCKITFGTGAFLLSVAGNGRPstgelLPTIAWQMQGA--PAVFA 280
Cdd:cd07781 227 taeaaerlglpAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVD-----IPGICGPVPDAvvPGLYG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 281 IEGGVYDAGAAVEWAKKIGLYAEN-------AELDwfEGPSAIR---RGLAFVPAFSGLAAPYWDRHAVPLFIGMNHATE 350
Cdd:cd07781 302 LEAGQSAVGDIFAWFVRLFVPPAEergdsiyALLS--EEAAKLPpgeSGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 351 RSDMVRAVLEGIALLTARLIEA-ASAVAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLAEL----CG 425
Cdd:cd07781 380 PAHIYRALLEATAFGTRAIIERfEEAGVPVNRVVACGGIAEKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILaavaAG 459
|
490 500 510
....*....|....*....|....*....|....*
gi 549799427 426 ID------VAAMRRETEIFAPDgsvgAEDHARFAR 454
Cdd:cd07781 460 VYadieeaADAMVRVDRVYEPD----PENHAVYEE 490
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
5-421 |
5.69e-11 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 64.64 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 5 AIDQGTTSTRClVVIDGGTAEVVASRR---HTQFYPAANHVEHDPEE---LLVN-IRAVLAAAG--PVDAIAIA--NQGE 73
Cdd:PRK10939 7 ALDAGTGSIRA-VIFDLNGNQIAVGQAewrHLAVPDVPGSMEFDLEKnwqLACQcIRQALQKAGipASDIAAVSatSMRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 74 SCLAWDAvSGEALspvivWQ----DARTAQTLAALPPSATHLSKEIcglpldpyFSAS----------KLAWLVRHNPAV 139
Cdd:PRK10939 86 GIVLYDR-NGTEI-----WAcanvDARASREVSELKELHNNFEEEV--------YRCSgqtlalgalpRLLWLAHHRPDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 140 AEAKAAgrlrLGTTDAFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKV---GPVDGGF------ 210
Cdd:PRK10939 152 YRQAHT----ITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVketGTVLGHVtakaaa 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 211 --GSIEGTPIRVSIVDQQAALYGHGCRTAGDCKITFGTgaFLLSVAGNGRPSTGellPTIAWQMQgaPAVFA----IEGG 284
Cdd:PRK10939 228 etGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGT--FWQQVVNLPAPVTD---PNMNIRIN--PHVIPgmvqAESI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 285 VYDAGAAVEW------------AKKIG-----LYAENAElDWFEGPSAIrrglafVPAFSGlAAPY--WdRHAVPLFIGM 345
Cdd:PRK10939 301 SFFTGLTMRWfrdafcaeekllAERLGidaysLLEEMAS-RVPVGSHGI------IPIFSD-VMRFksW-YHAAPSFINL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 346 NHATERSD---MVRAVLEGIALLTAR---LIEAASAVAPigDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALG 419
Cdd:PRK10939 372 SIDPEKCNkatLFRALEENAAIVSACnlqQIAAFSGVFP--SSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALG 449
|
..
gi 549799427 420 LA 421
Cdd:PRK10939 450 CA 451
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
2-419 |
3.15e-09 |
|
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: 58.69 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 2 RIAAIDQGTTSTR-CLVVIDGGTAEV-VASRRHTQFYPAANHVEHDPEELLVNIRAVLAAA----GPVDAIAIAnqgesc 75
Cdd:cd07771 1 NYLAVDLGASSGRvILGSLDGGKLELeEIHRFPNRPVEINGHLYWDIDRLFDEIKEGLKKAaeqgGDIDSIGID------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 76 lAW-------DAvSGEALSPVIVWQDARTAQTLAALppsATHLSKE----ICGLPLDPYFSASKLAWLVRHNPAVAEaKA 144
Cdd:cd07771 75 -TWgvdfgllDK-NGELLGNPVHYRDPRTEGMMEEL---FEKISKEelyeRTGIQFQPINTLYQLYALKKEGPELLE-RA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 145 AGRLRLGttDaFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKV-------GPV------DGGFG 211
Cdd:cd07771 149 DKLLMLP--D-LLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIvppgtvlGTLkpevaeELGLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 212 SIE----------------------------------GTPIRVSIVDQQAALYGHGCRTAGDCKITfgtgaFLLSVAGng 257
Cdd:cd07771 226 GIPviavashdtasavaavpaededaafissgtwsliGVELDEPVITEEAFEAGFTNEGGADGTIR-----LLKNITG-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 258 rpstgeLlptiaWQMQGAPAVFAIEGGVYDAGAAVEwakkiglYAENAE-LDWF------------EGPSAIRRglafvp 324
Cdd:cd07771 299 ------L-----WLLQECRREWEEEGKDYSYDELVA-------LAEEAPpFGAFidpddprflnpgDMPEAIRA------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 325 afsglaapYWDRHAVPLfigmnhATERSDMVRAVLEGIALLTARLIEAASAVAPIG-DTISIDGGLSNSRYFVRFLAAAS 403
Cdd:cd07771 355 --------YCRETGQPV------PESPGEIARCIYESLALKYAKTIEELEELTGKRiDRIHIVGGGSRNALLCQLTADAT 420
|
490
....*....|....*..
gi 549799427 404 GRTICV-PAmrELTALG 419
Cdd:cd07771 421 GLPVIAgPV--EATAIG 435
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
83-421 |
1.80e-08 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 56.58 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 83 GEALSPVIVWQDARTAQTLAALppsATHLSKE----ICGLPLDPYFSASKLAWLVRHNPAVAEaKAAGRLRLGTTDAFfl 158
Cdd:PRK10331 91 GNLLYPIISWKCPRTAAVMENI---ERYISAQqlqqISGVGAFSFNTLYKLVWLKENHPQLLE-QAHAWLFISSLINH-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 159 dRLTSSFRTDLATASRTGLLDLSTGDWSPELCALHGVTMDCLPKVgpVDGG--FGSIE-------GTPIRVSIV----DQ 225
Cdd:PRK10331 165 -RLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRL--VEAGeqIGTLQpsaaallGLPVGIPVIsaghDT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 226 QAALYGHGcrtAGDCKITFGTGAFLLSVAGNGRPSTgELLPtiawQMQGAPAVFAIEGGVYDAG------AAVEWAKKIG 299
Cdd:PRK10331 242 QFALFGSG---AGQNQPVLSSGTWEILMVRSAQVDT-SLLS----QYAGSTCELDSQSGLYNPGmqwlasGVLEWVRKLF 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 300 LYAENAELDWFEGPSAI---RRGLAFVPAFSGLAAPYWDrhavplfiGMNHATERSDMVRAVLEGialLTARLIEAASAV 376
Cdd:PRK10331 314 WTAETPYQTMIEEARAIppgADGVKMQCDLLACQNAGWQ--------GVTLNTTRGHFYRAALEG---LTAQLKRNLQVL 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 549799427 377 APIG----DTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLA 421
Cdd:PRK10331 383 EKIGhfkaSELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAA 431
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
6-440 |
2.33e-06 |
|
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: 49.93 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 6 IDQGTTSTRcLVVIDGGTAEVVA--SRRHTQF-YPAANHVEHDPEE----LLVNIRAVLAAAGpVDAIAIANQGESCLAW 78
Cdd:cd07768 5 VDVGTSSAR-AGVYDLYAGLEMAqePVPYYQDsSKKSWKFWQKSTEiikaLQKCVQKLNIREG-VDAYEVKGCGVDATCS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 79 DAVSGEALSP------------VIVWQDARTAQTLAALPPSATHLSKEICGLPLDPYFSASKLAWLVRHNPAVAEakAAG 146
Cdd:cd07768 83 LAIFDREGTPlmalipypnednVIFWMDHSAVNEAQWINMQCPQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRD--KHF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 147 RLrLGTTDaFFLDRLTSSFRTDLATASRTGLLDLSTGDWSPE------LCALHGVTMDCLPKVGPV-----------DGG 209
Cdd:cd07768 161 HI-FDLHD-YIAYELTRLYEWNICGLLGKENLDGEESGWSSSffknidPRLEHLTTTKNLPSNVPIgttsgvalpemAEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 210 FGSIEGTPIRVSIVDQQAALYGHGcrtagdcKITFGTGAFLLSvagnGRPSTGELLPTIAWQMQGAPAVF--AIEGG--V 285
Cdd:cd07768 239 MGLHPGTAVVVSCIDAHASWFAVA-------SPHLETSLFMIA----GTSSCHMYGTTISDRIPGVWGPFdtIIDPDysV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 286 YDAG------------------AAVEWAKKIG--LYAE-NAELDWFEGPSAIRRGLAFVPAFSGLAAPYWDRHAVPLFIG 344
Cdd:cd07768 308 YEAGqsatgkliehlfeshpcaRKFDEALKKGadIYQVlEQTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 345 MNHATERSDMV---RAVLEGIALLTARLIEAASAVAPIGDTISIDGGLSNSRYFVRFLAAASGRTICVPAMRELTALGLA 421
Cdd:cd07768 388 ESLDTSMLNLTykyIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAA 467
|
490 500 510
....*....|....*....|....*....|..
gi 549799427 422 EL--------CGIDV-----AAMRRETEIFAP 440
Cdd:cd07768 468 VLakvaagkkQLADSiteadISNDRKSETFEP 499
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
5-423 |
2.99e-04 |
|
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: 43.29 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 5 AIDQGTTSTRCLVVIDGGTAEVVASRRHTQFYPAANHVEHDPEEL---LVN-IRAVLAAAGpVDAIAIANQGE----SCL 76
Cdd:cd07782 4 GVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIwqaVCEaVKEVLEGAG-VDPEQVKGIGFdatcSLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 77 AWDA--------VSGEALSPVIVWQDARtAQTLAALPPSATHLSKEICGLPLDPYFSASKLAWLVRHNPAVaEAKAAGRL 148
Cdd:cd07782 83 VLDAegkpvsvsPSGDDERNVILWMDHR-AVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPET-WAKAGHFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 149 RLgtTDafFLdrltsSFRtdlATASRT------------GLLDLSTGDWSPELCALHGvtMDCL-------------PKV 203
Cdd:cd07782 161 DL--PD--FL-----TWK---ATGSLTrslcslvckwtyLAHEGSEGGWDDDFFKEIG--LEDLvednfakigsvvlPPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 204 GPVDGGF--------GSIEGTPIRVSIVDQQA-ALYGHGCRTAGDCK----------ITFGTGA--FLLS-----VAG-- 255
Cdd:cd07782 227 EPVGGGLtaeaakelGLPEGTPVGVSLIDAHAgGLGTLGADVGGLPCeadpltrrlaLICGTSSchMAVSpepvfVPGvw 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 256 ---------------NGRPSTGELLPTIawqMQGAPAVFAIEGGVYDAGAAV--EWAKKIGLYAENAELDwfegPSAIRR 318
Cdd:cd07782 307 gpyysamlpglwlneGGQSATGALLDHI---IETHPAYPELKEEAKAAGKSIyeYLNERLEQLAEEKGLP----LAYLTR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799427 319 GLAFVPAFSGLAAPYWDRHAVPLFIGMNHATERSDMVR---AVLEGIALLTARLIEA-ASAVAPIgDTISIDGGLSNSRY 394
Cdd:cd07782 380 DLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAmNAAGHKI-DTIFMCGGLSKNPL 458
|
490 500
....*....|....*....|....*....
gi 549799427 395 FVRFLAAASGRTICVPAMRELTALGLAEL 423
Cdd:cd07782 459 FVQLHADVTGCPVVLPKEPEAVLLGAAIL 487
|
|
| |
