|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
20-520 |
0e+00 |
|
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: 881.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKTGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHSSCRVLHFFTRSKRLFTASLFTFTTQQTSLRLVWILQNL 179
Cdd:cd07793 81 TFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLLLKALRGGSKFLHFLTRNKRFLAASVLKFSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 180 TEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVD 259
Cdd:cd07793 161 PELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGSTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 260 EEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAESNAGDT 339
Cdd:cd07793 241 PSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGEITYLAEGNASDT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 340 GTAIKWAQQLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQ 419
Cdd:cd07793 321 GTVIDWAKSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 420 LYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKKLRQSEVVF 499
Cdd:cd07793 401 LLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEELKKLRKIEKIF 480
|
490 500
....*....|....*....|.
gi 88196792 500 KPQKKCQEYEMSLENWAKAVK 520
Cdd:cd07793 481 EPKMDNEKREELYKNWKKAVK 501
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
20-520 |
0e+00 |
|
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: 644.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKTGNHFHNFISWQDLRAVELVKSWNNSLL-MKIFHSSCRVLHFFtrskrlFTASlftfttqqtslRLVWILQN 178
Cdd:cd07769 81 TTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLeERIREKTGLPLDPY------FSAT-----------KIKWILDN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 179 LTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSV 258
Cdd:cd07769 144 VPGARERAERGELLFGTIDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 259 DEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAESNAGD 338
Cdd:cd07769 224 DPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVTYALEGSIFI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 339 TGTAIKWA-QQLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRN 417
Cdd:cd07769 304 AGAAIQWLrDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 418 KQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKKLRQSEV 497
Cdd:cd07769 384 RDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVDK 463
|
490 500
....*....|....*....|...
gi 88196792 498 VFKPQKKCQEYEMSLENWAKAVK 520
Cdd:cd07769 464 RFEPSMDEEERERLYRGWKKAVE 486
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
20-525 |
4.32e-180 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 515.38 E-value: 4.32e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:COG0554 4 YILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKTGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHsscrvlhfftrsKR--LFTASLFTFTtqqtslRLVWILQ 177
Cdd:COG0554 84 TTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLEDLIR------------EKtgLVLDPYFSAT------KIKWILD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 178 NLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGS 257
Cdd:COG0554 146 NVPGARERAEAGELLFGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 258 VDEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAESNAG 337
Cdd:COG0554 226 TDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVTYALEGSIF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 338 DTGTAIKW-AQQLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFR 416
Cdd:COG0554 306 VAGAAVQWlRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 417 NKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKKLRQSE 496
Cdd:COG0554 386 TRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVD 465
|
490 500
....*....|....*....|....*....
gi 88196792 497 VVFKPQKKCQEYEMSLENWAKAVKRSMNW 525
Cdd:COG0554 466 RRFEPQMDEEERERLYAGWKKAVERTLGW 494
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
20-520 |
6.82e-160 |
|
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: 463.50 E-value: 6.82e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKTGNHFHNFISWQDLRAVELVKSWNNSLLMKIFhsscrvlhfftRSK---RL---FTASlftfttqqtslRLV 173
Cdd:cd07786 81 TTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEMI-----------REKtglVLdpyFSAT-----------KIR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 174 WILQNLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSH 253
Cdd:cd07786 139 WILDNVPGARERAERGELAFGTIDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 254 NFGSVDEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVV-CLa 332
Cdd:cd07786 219 VFGYTDPDLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVTyAL- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 333 ESNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILE 411
Cdd:cd07786 298 EGSIFIAGAAVQWLRdGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 412 SIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKK 491
Cdd:cd07786 378 SIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAK 457
|
490 500
....*....|....*....|....*....
gi 88196792 492 LRQSEVVFKPQKKCQEYEMSLENWAKAVK 520
Cdd:cd07786 458 LWQVDRRFEPSMSEEEREALYAGWKKAVK 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
20-525 |
2.23e-146 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 429.63 E-value: 2.23e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:PRK00047 6 YILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKTGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHsscrvlhfftRSKRLFTASLFTFTtqqtslRLVWILQNL 179
Cdd:PRK00047 86 TTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYEDYIR----------EKTGLVIDPYFSGT------KIKWILDNV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 180 TEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSV- 258
Cdd:PRK00047 150 EGARERAEKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTn 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 259 DEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAESNAGD 338
Cdd:PRK00047 230 PYGFFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVVYALEGSIFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 339 TGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRN 417
Cdd:PRK00047 310 AGSAIQWLRdGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 418 KQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKKLRQSEV 497
Cdd:PRK00047 390 RDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKIDR 469
|
490 500
....*....|....*....|....*...
gi 88196792 498 VFKPQKKCQEYEMSLENWAKAVKRSMNW 525
Cdd:PRK00047 470 RFEPQMDEEEREKLYAGWKKAVKRTLAW 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
21-525 |
1.72e-144 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 425.16 E-value: 1.72e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 21 VLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGI--QMNQIVGLGISTQR 98
Cdd:PTZ00294 4 IGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREkgPSFKIKAIGITNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 99 ATFITWNKKTGNHFHNFISWQDLRAVELVKSWNNSLLMK-IFHSSCRVLhfftrskrlftaslftFTTQQTSLRLVWILQ 177
Cdd:PTZ00294 84 ETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSnFFQKITGLP----------------ISTYFSAFKIRWMLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 178 NLTEVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGS 257
Cdd:PTZ00294 148 NVPAVKDAVKEGTLLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 258 VDEEIFG--VPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQE--VVCLAE 333
Cdd:PTZ00294 228 ISGEAVPllEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNgpTVYALE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 334 SNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILES 412
Cdd:PTZ00294 308 GSIAVAGAGVEWLRdNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 413 IAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEELKKL 492
Cdd:PTZ00294 388 IALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKL 467
|
490 500 510
....*....|....*....|....*....|....
gi 88196792 493 -RQSEVVFKPQKKCQEYEMSLENWAKAVKRSMNW 525
Cdd:PTZ00294 468 iRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKW 501
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
20-522 |
2.90e-136 |
|
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: 403.83 E-value: 2.90e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAV---KAAGIQMNQIVGLGIST 96
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVeklKALGISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 97 QRATFITWNKKTGNHFHNFISWQDLRAVELVKSwnnsLLMKIFHSScrvLHFftRSKrlftASLfTFTTQQTSLRLVWIL 176
Cdd:cd07792 82 QRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEE----LSAKTPGGK---DHF--RKK----TGL-PISTYFSAVKLRWLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 177 QNLTEVQKAVEEENCCFGTIDTWLLYKLTKG---SVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSH 253
Cdd:cd07792 148 DNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGkngGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 254 NFGSVDEEIF-GVPIpiVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIG-QEVVCL 331
Cdd:cd07792 228 VYGKIASGPLaGVPI--SGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGpDAPPVY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 332 A-ESNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAI 409
Cdd:cd07792 306 AlEGSIAIAGAAVQWLRdNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 410 LESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTDKEEL 489
Cdd:cd07792 386 LEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDEL 465
|
490 500 510
....*....|....*....|....*....|....
gi 88196792 490 KKLRQSEV-VFKPQKKCQEYEMSLENWAKAVKRS 522
Cdd:cd07792 466 KSLNEGGRtVFEPQISEEERERRYKRWKKAVERS 499
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
20-525 |
6.09e-113 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 344.38 E-value: 6.09e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVG----LGIS 95
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDSglkaIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 96 TQRATFITWNKKTGNHFHNFISWQDLRAVELVKSwnnslLMKIFHSSCRvlhFFTRSKRLFTASLFTfttqqtSLRLVWI 175
Cdd:PLN02295 81 NQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRR-----LEKELSGGRK---HFVETCGLPISTYFS------ATKLLWL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 176 LQNLTEVQKAVEEENCCFGTIDTWLLYKLT---KGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTS 252
Cdd:PLN02295 147 LENVDAVKEAVKSGDALFGTIDSWLIWNLTggaSGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 253 HNFGSVDEEIFGVPIPIVALVADQQSAMFGECCfQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCL- 331
Cdd:PLN02295 227 EVIGTIAKGWPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNy 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 332 -AESNAGDTGTAIKWAQ-QLDLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAI 409
Cdd:PLN02295 306 aLEGSVAIAGAAVQWLRdNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 410 LESIAFRNKQLYEMMKKEI-----HIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWT 484
Cdd:PLN02295 386 LESMCFQVKDVLDAMRKDAgeeksHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWT 465
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 88196792 485 DKEELKKLRQ-SEVVFKPQKKCQEYEMSLENWAKAVKRSMNW 525
Cdd:PLN02295 466 EEEIFASEKWkNTTTFRPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
21-521 |
1.89e-85 |
|
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: 272.86 E-value: 1.89e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 21 VLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRAT 100
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 101 FITWNKKtGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHSSCRVlhfftrskrlftaslfTFTTQQTSLRLVWILQNLT 180
Cdd:COG1070 83 LVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEALYEITGN----------------PLHPGFTAPKLLWLKENEP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 181 EVQKAVEeencCFGTIDTWLLYKLTkGsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDE 260
Cdd:COG1070 146 EIFARIA----KVLLPKDYLRYRLT-G-EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 261 EI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTgNSLQQTTGGFYPLIGWKIGQEVVCLAESN 335
Cdd:COG1070 220 EAaaeTGLPagTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGRWLPMGATN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 336 AGdtGTAIKWAQQL---DLFTDAAE-TEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILE 411
Cdd:COG1070 299 NG--GSALRWFRDLfadGELDDYEElNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 412 SIAFRNKQLYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTD-KEELK 490
Cdd:COG1070 377 GVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDlEEAAA 455
|
490 500 510
....*....|....*....|....*....|..
gi 88196792 491 KLRQSEVVFKPQKKCQE-YEMSLENWAKAVKR 521
Cdd:COG1070 456 AMVRVGETIEPDPENVAaYDELYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
20-504 |
1.14e-78 |
|
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: 253.21 E-value: 1.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKtGNHFHNFISWQDLRAVelvkswnnsllmkifhsscrvlhfftrskrlftaslftfttqqtslrlvwilqnl 179
Cdd:cd07779 81 TFVPVDED-GRPLRPAISWQDKRTA------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 180 tevqkaveeencCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVD 259
Cdd:cd07779 105 ------------KFLTVQDYLLYRLT--GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 260 EEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFYPLIGWKIGQEVVclaES 334
Cdd:cd07779 171 KEAaeeTGLPegTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVL---EG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 335 NAGDTGTAIKWAQQLdLFTDAAETEKMAKSLED------------SEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSK 402
Cdd:cd07779 248 SINTGGSAVRWFRDE-FGQDEVAEKELGVSPYEllneeaaksppgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 403 YHLVRAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVGF 482
Cdd:cd07779 327 AHLARAILEGIAFELRDNLEAMEKA-GVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGI 405
|
490 500
....*....|....*....|...
gi 88196792 483 WTDKEE-LKKLRQSEVVFKPQKK 504
Cdd:cd07779 406 YPDFEEaVKAMVRVTDTFEPDPE 428
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
21-481 |
1.35e-77 |
|
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: 250.58 E-value: 1.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 21 VLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIqmNQIVGLGISTQRAT 100
Cdd:cd07773 2 LLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP--DPIAAISVSSQGES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 101 FITWNKKtGNHFHNFISWQDLRAVELVKSWNNSLLMK-IFHSSCRVLHFftrskrlfTASLFtfttqqtslRLVWILQNL 179
Cdd:cd07773 80 GVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEeLYRITGLPPSP--------MYSLA---------KLLWLREHE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 180 TEVQKAVeeenCCFGTIDTWLLYKLTKgsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVD 259
Cdd:cd07773 142 PEIFAKA----AKWLSVADYIAYRLTG--EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 260 EEI---FGVPIPIVALVA--DQQSAMFGECCFQTGDVKLTMGTG-TFLDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAE 333
Cdd:cd07773 216 PEAaeeLGLPAGTPVVVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVVDEPPLDEMLAEGGLSYGHHVPGGYYYLAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 334 SNAGdtGTAIKWAQQL---DLFTDAAETEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAIL 410
Cdd:cd07773 296 SLPG--GALLEWFRDLfggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAIL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196792 411 ESIAFRNKQLYEMMKKeIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAVG 481
Cdd:cd07773 374 EGLAFELRLNLEALEK-AGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
21-476 |
1.37e-76 |
|
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: 246.32 E-value: 1.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 21 VLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRAT 100
Cdd:cd00366 2 LLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 101 FITWNKKtGNHFHNFISWQDLRAvelvkswnnsllmkifhsscrvlhfftrskrlftaslftfttqqtslrlvwilqnlt 180
Cdd:cd00366 82 VVLVDAD-GNPLRPAIIWLDRRA--------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 181 evqkaveeencCFGTIDTWLLYKLTKgsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDE 260
Cdd:cd00366 104 -----------KFLQPNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 261 EI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGgfypLIGWKIGQEVVCLAESN 335
Cdd:cd00366 171 EAaeeTGLPagTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPR----LLNRCHVVPGLWLLEGA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 336 AGDTGTAIKWAqqLDLF----TDAAETEKM----AKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVR 407
Cdd:cd00366 247 INTGGASLRWF--RDEFgeeeDSDAEYEGLdelaAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIR 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196792 408 AILESIAFRNKQLYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLA 476
Cdd:cd00366 325 AVLEGVAYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
20-509 |
1.45e-71 |
|
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: 236.28 E-value: 1.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKtGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHSSC-RVLHFFTRSKrlftaslftfttqqtslrLVWILQN 178
Cdd:cd07808 81 GLVLLDKN-GRPLRPAILWNDQRSAAECEELEARLGDEILIITGnPPLPGFTLPK------------------LLWLKEN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 179 ltevqkavEEENccFGTIDTWLL------YKLTKgsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTS 252
Cdd:cd07808 142 --------EPEI--FARIRKILLpkdylrYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVEST 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 253 HNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGT-GTFL------DINTGNSLQqttggFYPLI 320
Cdd:cd07808 210 EIVGTLTPEAaeeLGLPegTPVVAGAGDNAAAALGAGVVEPGDALISLGTsGVVFaptdkpVPDPKGRLH-----TFPHA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 321 ---GWKIgqevvcLAESNAGdtGTAIKWAQQLdLFTDAAETEKM----AKSLEDSEGVCFVPSFSGLQAPLNDPWACASF 393
Cdd:cd07808 285 vpgKWYA------MGVTLSA--GLSLRWLRDL-FGPDRESFDELdaeaAKVPPGSEGLLFLPYLSGERTPYWDPNARGSF 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 394 MGLKPSTSKYHLVRAILESIAFRNKQLYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAA 473
Cdd:cd07808 356 FGLSLSHTRAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAA 434
|
490 500 510
....*....|....*....|....*....|....*...
gi 88196792 474 SLAGLAVGFWTDKEE-LKKLRQSEVVFKP-QKKCQEYE 509
Cdd:cd07808 435 LLAAVGAGVFDDLEEaAAACIKIEKTIEPdPERHEAYD 472
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
20-508 |
4.08e-70 |
|
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: 232.06 E-value: 4.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIqmNQIVGLGISTQRA 99
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGG--GEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKtGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHSS--CRVLHfftrskrlftASLFTfttqqtslRLVWILQ 177
Cdd:cd07770 79 SLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSELYRRtgCPIHP----------MYPLA--------KLLWLKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 178 NLTEVQKAVeeenCCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGS 257
Cdd:cd07770 140 ERPELFAKA----AKFVSIKEYLLYRLT--GELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 258 VDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGT---------GTFLDINTGNSLQQTTGGFYpLIGwk 323
Cdd:cd07770 214 LKPEFaerLGLLagTPVVLGASDGALANLGSGALDPGRAALTVGTsgairvvsdRPVLDPPGRLWCYRLDENRW-LVG-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 324 igqevvcLAESNAGDtgtAIKWAQQ--LDLFTDAAETEKMAKSLE-DSEGVCFVPSFSGLQAPLNDPWACASFMGLKPST 400
Cdd:cd07770 291 -------GAINNGGN---VLDWLRDtlLLSGDDYEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNH 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 401 SKYHLVRAILESIAFRNKQLYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAV 480
Cdd:cd07770 361 TRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEAL 439
|
490 500
....*....|....*....|....*...
gi 88196792 481 GFWTDKEELKKLRQSEvVFKPQKKCQEY 508
Cdd:cd07770 440 GLISSLEADELVKIGK-VVEPDPENHAI 466
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
20-509 |
3.29e-64 |
|
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: 216.62 E-value: 3.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKtGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHsscrvlhfftrskRLFTASLFTfttQQTSL-RLVWILQN 178
Cdd:cd07805 81 GVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGY-------------RLGGGNPPS---GKDPLaKILWLKEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 179 LTEV-QKAVeeenCCFGTIDtWLLYKLTkGsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGS 257
Cdd:cd07805 144 EPEIyAKTH----KFLDAKD-YLNFRLT-G-RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 258 VDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGT----GTF-----LDINTG-NSLQQTTGGFYPLIGw 322
Cdd:cd07805 217 LTPEAaaeLGLPagTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTsgwvAAHvpkpkTDPDHGiFTLASADPGRYLLAA- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 323 kigqevvclAESNAGdtgTAIKWA-----QQLDLFTDAAE--TEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMG 395
Cdd:cd07805 296 ---------EQETAG---GALEWArdnlgGDEDLGADDYEllDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 396 LKPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHiPVRKIRADGGVCKNGFVMQMTSDLINENIDRPAD-IDMSCLGAAS 474
Cdd:cd07805 364 LSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAAL 442
|
490 500 510
....*....|....*....|....*....|....*.
gi 88196792 475 LAGLAVGFWTDKEELKKLRQSEVVFKPQKKCQE-YE 509
Cdd:cd07805 443 LAAVGLGLLKSFDEAKALVKVEKVFEPDPENRArYD 478
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
20-481 |
5.01e-58 |
|
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: 199.29 E-value: 5.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKtGNHFHNFISWQDLRAVELVKsWNNSLLmkifhsscrvlhfftRSKRLFTASLFTFTTQQTSLRLVWILQNL 179
Cdd:cd07804 81 ALVPVDEN-GKPLRPAILYGDRRATEEIE-WLNENI---------------GEDRIFEITGNPLDSQSVGPKLLWIKRNE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 180 TEV-QKAVEeenccFGTIDTWLLYKLTkgSVYATDFSNAS-TTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGS 257
Cdd:cd07804 144 PEVfKKTRK-----FLGAYDYIVYKLT--GEYVIDYSSAGnEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 258 VDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGN--SLQQ------------------T 312
Cdd:cd07804 217 VTKEAaeeTGLAegTPVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKlpTDPRlwldyhdipgtyvlnggmA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 313 TGGfyPLIGWKIGQevVCLAESNAGDTGTAIKWaQQLDlftdaaetEKMAKSLEDSEGVCFVPSFSGLQAPLNDPWACAS 392
Cdd:cd07804 297 TSG--SLLRWFRDE--FAGEEVEAEKSGGDSAY-DLLD--------EEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 393 FMGLKPSTSKYHLVRAILESIAFRNKQLYEMMkKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGA 472
Cdd:cd07804 364 IFGLTLSHTRAHLYRALLEGVAYGLRHHLEVI-REAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGD 442
|
....*....
gi 88196792 473 ASLAGLAVG 481
Cdd:cd07804 443 AFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
20-481 |
3.92e-54 |
|
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: 188.91 E-value: 3.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKtGNHFHNFISWQDLRAVELVKSWNNS-LLMKIFHSSCRVLhfftrskrlftaslftFTTQQTSLrLVWILQN 178
Cdd:cd07802 81 GLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDgTLEKVYPLTGQPL----------------WPGQPVAL-LRWLKEN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 179 ltevqkavEEENccFGTIDT------WLLYKLTkGsVYATDFSNASTtGLFDPYKMCWSGMITSLISIP--LSLLPPVRD 250
Cdd:cd07802 143 --------EPER--YDRIRTvlfckdWIRYRLT-G-EISTDYTDAGS-SLLDLDTGEYDDELLDLLGIEelKDKLPPLVP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 251 TSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGT----GTFLD-INTGNSLQQTtgGFYPLI 320
Cdd:cd07802 210 STEIAGRVTAEAaalTGLPegTPVAAGAFDVVASALGAGAVDEGQLCVILGTwsinEVVTDePVVPDSVGSN--SLHADP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 321 GWKigqevvcLAESNAGDTGTAIKWAqqLDLFTDAAET----------EKMAKSLEDSEGVCFVPSFSGlqAPLNdPWAC 390
Cdd:cd07802 288 GLY-------LIVEASPTSASNLDWF--LDTLLGEEKEaggsdydeldELIAAVPPGSSGVIFLPYLYG--SGAN-PNAR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 391 ASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKeiHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCL 470
Cdd:cd07802 356 GGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLV--ARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGAL 433
|
490
....*....|.
gi 88196792 471 GAASLAGLAVG 481
Cdd:cd07802 434 GAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
20-480 |
2.90e-53 |
|
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: 186.27 E-value: 2.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIqmNQIVGLGISTQRA 99
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRP--RRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKtGNHFHNFISWQDLRAVELVKswnnsLLMKIFHSSCRVLHFftrskrLFTASlFTFTtqqtslRLVWILQNL 179
Cdd:cd07783 79 TLVLVDRE-GEPLRPAIMYNDARAVAEAE-----ELAEAAGAVAPRTGL------AVSPS-SSLA------KLLWLKRHE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 180 TEVQKAVeeenCCFGTIDTWLLYKLTkGSVYATDFSNASTTGlFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVD 259
Cdd:cd07783 140 PEVLAKT----AKFLHQADWLAGRLT-GDRGVTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 260 EEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQTTGGFY----PLIGWKIGqevvc 330
Cdd:cd07783 214 AEAaeeLGLPagTPVVAGTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYshrhGDGYWLVG----- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 331 lAESNAGdtGTAIKWAQQLDlftDAAETEKMAKSlEDSEGVCFVP-SFSGLQAPLNDPWACASFmgLKPSTSKYHLVRAI 409
Cdd:cd07783 289 -GASNTG--GAVLRWFFSDD---ELAELSAQADP-PGPSGLIYYPlPLRGERFPFWDPDARGFL--LPRPHDRAEFLRAL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196792 410 LESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINenidRP---ADIDMSCLGAASLAGLAV 480
Cdd:cd07783 360 LEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLG----VPvviAEEEEAALGAALLAAAGL 429
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
20-282 |
3.38e-48 |
|
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: 167.13 E-value: 3.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKTgNHFHNFISWQDLRAVELVKSWNNSLLMKIFHSSCRVLhfftrskrlftasLFTFTtqqTSLRLVWILQNL 179
Cdd:pfam00370 81 GTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLP-------------IWPGF---TLSKLRWIKENE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 180 TEVQKAVEeencCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVD 259
Cdd:pfam00370 144 PEVFEKIH----KFLTIHDYLRWRLT--GVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELN 217
|
250 260
....*....|....*....|....*...
gi 88196792 260 EEIFG-----VPIPIVALVADQQSAMFG 282
Cdd:pfam00370 218 PELAAmwgldEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
20-481 |
2.37e-44 |
|
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: 162.39 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYP--QIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQ 97
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 98 RATFITWNKKtGNHFH---NFiswqDLRAVELVKSWNNSLLMKIFHSSCRVLHFftrskrLFTASlftfttqqtslRLVW 174
Cdd:cd07798 81 REGIVFLDKD-GRELYagpNI----DARGVEEAAEIDDEFGEEIYTTTGHWPTE------LFPAA-----------RLLW 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 175 ILQNltevQKAVEEENCCFGTIDTWLLYKLTKgsVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHN 254
Cdd:cd07798 139 FKEN----RPEIFERIATVLSISDWIGYRLTG--ELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 255 FGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTfldintgnSLQQTTGGfyPLIG-----WkI 324
Cdd:cd07798 213 LGTVSEEAareLGLPegTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTT--------PVQMVTDE--PIIDperrlW-T 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 325 GQEVVC---LAESNAGDTGTAIKWAQQLdLFTDAAET-EKMAKSLEDSEGVCF-VPSFSGLQAPlnDPWACA-------- 391
Cdd:cd07798 282 GCHLVPgkwVLESNAGVTGLNYQWLKEL-LYGDPEDSyEVLEEEASEIPPGANgVLAFLGPQIF--DARLSGlknggflf 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 392 SFMGLKPSTSKYHLVRAILESIAF---RN-KQLYEMMKKEIhipvRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDM 467
Cdd:cd07798 359 PTPLSASELTRGDFARAILENIAFairANlEQLEEVSGREI----PYIILCGGGSRSALLCQILADVLGKPVLVPEGREA 434
|
490
....*....|....
gi 88196792 468 SCLGAASLAGLAVG 481
Cdd:cd07798 435 SALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
20-481 |
1.02e-39 |
|
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: 149.70 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TfiTW-NKKTGNHFHNFISWQDLRAVELVKSWNNSllmkifhsscrvlhffTRSKRLF--TASLfTFTTQQTSLrLVWIL 176
Cdd:cd24121 81 G--TWlVDEDGRPVRDAILWLDGRAADIVERWQAD----------------GIAEAVFeiTGTG-LFPGSQAAQ-LAWLK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 177 QNLTEVQKAVEEENCCFGtidtWLLYKLTkgSVYATDFSNASTTgLFDPYKMCWSGMITSLISIP--LSLLPPVRDTSHN 254
Cdd:cd24121 141 ENEPERLERARTALHCKD----WLFYKLT--GEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 255 FGSVDEEI---FGVP--IPIValvadqqSAMFgeccfqtgDVKLT-MGTGTFLDiNTGNSLQQTTG-----GFYPLIGWK 323
Cdd:cd24121 214 IGPLTPEAaaaTGLPagTPVV-------LGPF--------DVVATaLGSGAIEP-GDACSILGTTGvhevvVDEPDLEPE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 324 IGQEVVCLAESN------AGDTGTA-IKWAqqLDLFTDAAETEKMAKSLED--------------SEGVCFVPSFS--GL 380
Cdd:cd24121 278 GVGYTICLGVPGrwlramANMAGTPnLDWF--LRELGEVLKEGAEPAGSDLfqdleelaassppgAEGVLYHPYLSpaGE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 381 QAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKkeihIPVRKIRADGGVCKNGFVMQMTSDLINENID 460
Cdd:cd24121 356 RAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYEHMG----EDPGELRLSGGGARSDTWCQILADALGVPVR 431
|
490 500
....*....|....*....|.
gi 88196792 461 RPADIDMSCLGAASLAGLAVG 481
Cdd:cd24121 432 VPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
20-481 |
2.66e-33 |
|
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: 131.52 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYD-RAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQR 98
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 99 ATFITWNKKtGNHFHNFISWQDLRAVELvkswnNSLLMKIFHSSCRVLHFFTRSKRlFTASlftfttqqtslRLVWILQN 178
Cdd:cd07809 81 HGLVALDAD-GKVLRPAKLWCDTRTAPE-----AEELTEALGGKKCLLVGLNIPAR-FTAS-----------KLLWLKEN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 179 ltevqkavEEENccFGTIDT------WLLYKLTKGSVyaTDFSNASTTGLFDPYKMCWSGMITSLIS---IPLSLLPPVR 249
Cdd:cd07809 143 --------EPEH--YARIAKillphdYLNWKLTGEKV--TGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDLLPEVL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 250 DTSHNFGSVDEEI---FGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTFLDINTGNSLQQ----------TTG 314
Cdd:cd07809 211 PAGEVAGRLTPEGaeeLGLPagIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDphgrvatfcdSTG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 315 GFYPLIgwkigqevvclaeSNAGDTGTAIKWAQQLdLFTDAAETEKMA-KSLEDSEGVCFVPSFSGLQAPlNDPWACASF 393
Cdd:cd07809 291 GMLPLI-------------NTTNCLTAWTELFREL-LGVSYEELDELAaQAPPGAGGLLLLPFLNGERTP-NLPHGRASL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 394 MGLKPS-TSKYHLVRAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGA 472
Cdd:cd07809 356 VGLTLSnFTRANLARAALEGATFGLRYGLDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGA 434
|
....*....
gi 88196792 473 ASLAGLAVG 481
Cdd:cd07809 435 ALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
20-509 |
1.03e-30 |
|
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: 124.96 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAA-RVCGSSVQKVENLY--PQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGIST 96
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLADgEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 97 QRATFITWNKKtGNHFHNFISWQDLRAV-------ELVKSWNNSLLMKIFHSscrvlhffTRSKRLFTASLftfttqqts 169
Cdd:cd07781 81 TSSTVVPVDED-GNPLAPAILWMDHRAQeeaaeinETAHPALEYYLAYYGGV--------YSSEWMWPKAL--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 170 lrlvWILQNLTEVQKA----VEeenCCfgtiDtWLLYKLT---KGSVyatdfSNASTTGLFDPYKMCWSGMITSLISIPL 242
Cdd:cd07781 143 ----WLKRNAPEVYDAaytiVE---AC----D-WINARLTgrwVRSR-----CAAGHKWMYNEWGGGPPREFLAALDPGL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 243 SLL-----PPVRDTSHNFGSVDEE---IFGVP--IPIVALVADQQSAMFGECCFQTGDVKLTMGTGTfLDINTGNSLQQT 312
Cdd:cd07781 206 LKLreklpGEVVPVGEPAGTLTAEaaeRLGLPagIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTST-CHLMVSPKPVDI 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 313 TG--GFYP------LIGWKIGQevvclaeSNAGDTgtaIKWAQQLdLFTDAAET--------EKMAKSLE-DSEGVCFVP 375
Cdd:cd07781 285 PGicGPVPdavvpgLYGLEAGQ-------SAVGDI---FAWFVRL-FVPPAEERgdsiyallSEEAAKLPpGESGLVALD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 376 SFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGV-CKNGFVMQMTSDL 454
Cdd:cd07781 354 WFNGNRTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEA-GVPVNRVVACGGIaEKNPLWMQIYADV 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 88196792 455 INENIDRPADIDMSCLGAASLAGLAVGFWTDKEEL-KKLRQSEVVFKPQKKCQE-YE 509
Cdd:cd07781 433 LGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAaDAMVRVDRVYEPDPENHAvYE 489
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
291-479 |
1.53e-30 |
|
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: 117.81 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 291 VKLTMGTGTFLDINTGNSLQQTTGgFYPLIGWKIGQEVVCLAESNAgDTGTAIKWAQQLDLFTDAAETEKMAKSLE---- 366
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHG-VWGPYTNEMLPGYWGLEGGQS-AAGSLLAWLLQFHGLREELRDAGNVESLAelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 367 -----DSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGV 441
Cdd:pfam02782 79 laavaPAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 88196792 442 CKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLA 479
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
20-476 |
1.94e-30 |
|
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: 123.49 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAA-RVcgSSVQKVENLYPQ----IGWVEIDPDVLWIQFVAVIKEAVKAAGIQmnqIVGLGI 94
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESgRI--LESVSRPTPAPIssddPGRSEQDPEKILEAVRNLIDELPREYLSD---VTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 95 STQRATFITWNKKtGNHFHNFISWQDLRAVELVKSWNNSLLMKIFHSSCRVLHfftrskrlftaSLFTFTTqqtslrLVW 174
Cdd:cd07777 76 TGQMHGIVLWDED-GNPVSPLITWQDQRCSEEFLGGLSTYGEELLPKSGMRLK-----------PGYGLAT------LFW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 175 ILQNltevqKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHN 254
Cdd:cd07777 138 LLRN-----GPLPSKADRAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 255 FGSVDEEIfGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTG---TFLDintgnSLQQTTGGF--YPLIGwkiGQEVV 329
Cdd:cd07777 213 VGTLSSAL-PKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGaqlSFLT-----PKFELSGSVeiRPFFD---GRYLL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 330 CLAESNAGDTGTAIK-----WAQQLDLFTDAAE-TEKMAKSL--EDSEGVCFVPSFSGLQaplNDPWACASFMGLKPSTS 401
Cdd:cd07777 284 VAASLPGGRALAVLVdflreWLRELGGSLSDDEiWEKLDELAesEESSDLSVDPTFFGER---HDPEGRGSITNIGESNF 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196792 402 KY-HLVRAILESIAfrnKQLYEMMKKEI--HIPVRKIRADGGVC-KNGFVMQMTSDLINENIDRPADIDMSCLGAASLA 476
Cdd:cd07777 361 TLgNLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
20-515 |
8.13e-26 |
|
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: 110.50 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSS----VQKVENLYPqiGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGIS 95
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAqrewRHKEVPDVP--GSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 96 TQRATFITWNKKTGNHF--HNFiswqDLRAVELVKswnnsLLMKIFHsscrvlhffTRSKRLFTASLFTFTTqqTSL-RL 172
Cdd:cd07775 79 SMREGIVLYDNEGEEIWacANV----DARAAEEVS-----ELKELYN---------TLEEEVYRISGQTFAL--GAIpRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 173 VWILQNLTEVQKAVeeenCCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTS 252
Cdd:cd07775 139 LWLKNNRPEIYRKA----AKITMLSDWIAYKLS--GELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 253 HNFGSVDEEI---FGVP--IPIVALVADQQSAMFGeccfqTGDVKLTMGT---GTFldintgnsLQQTTGGFYPLIGWKI 324
Cdd:cd07775 213 TVIGKVTKEAaeeTGLKegTPVVVGGGDVQLGCLG-----LGVVRPGQTAvlgGSF--------WQQEVNTAAPVTDPAM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 325 GQEVVC-------LAESNAGDTGTAIKWaqqldlFTDA-----------------AETEKMAKSLE-DSEGVcfVPSFSG 379
Cdd:cd07775 280 NIRVNChvipdmwQAEGISFFPGLVMRW------FRDAfcaeekeiaerlgidayDLLEEMAKDVPpGSYGI--MPIFSD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 380 LQAPLNDPWACASFMGL---KPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLIN 456
Cdd:cd07775 352 VMNYKNWRHAAPSFLNLdidPEKCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLG 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196792 457 ENIDRPADIDMSCLGAASLAGLAVGFWTDKEE-LKKLRQSEVVFKPQKKCQE-YEMSLENW 515
Cdd:cd07775 432 LPVKVPVVKEATALGAAIAAGVGAGIYSSLEEaVESLVKWEREYLPNPENHEvYQDLYEKW 492
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
22-481 |
3.22e-19 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 90.41 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 22 LGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIqfvaVIKEAVKAAGIQ--MNQIVGLGISTQR- 98
Cdd:PRK15027 3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQ----ATDRAMKALGDQhsLQDVKALGIAGQMh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 99 -ATFITWNKKTgnhFHNFISWQDLRAVElvkswnnsllmkifhsSCRVLHFFTRSKRLFTASLFT--FTTQqtslRLVWI 175
Cdd:PRK15027 79 gATLLDAQQRV---LRPAILWNDGRCAQ----------------ECALLEARVPQSRVITGNLMMpgFTAP----KLLWV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 176 LQNLTEVqkaveeenccFGTIDTWLLYK----LTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDT 251
Cdd:PRK15027 136 QRHEPEI----------FRQIDKVLLPKdylrLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 252 SHNFGSVDEEI---FGVP-IPIVALVADQQSAMFGECCFQTGDVKLTMGT-GTFLDINTG--NSLQQTTGGF-YPLIG-W 322
Cdd:PRK15027 206 SEITGALLPEVakaWGMAtVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflSKPESAVHSFcHALPQrW 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 323 KIgQEVVCLAESnagdtgtAIKWAQQLDLFTDAAETEKMAKSLEDSEG-VCFVPSFSGLQAPLNDPWACASFMGLKPSTS 401
Cdd:PRK15027 286 HL-MSVMLSAAS-------CLDWAAKLTGLSNVPALIAAAQQADESAEpVWFLPYLSGERTPHNNPQAKGVFFGLTHQHG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 402 KYHLVRAILESIAFrnkQLYEMMKKeIH---IPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMS-CLGAASLAG 477
Cdd:PRK15027 358 PNELARAVLEGVGY---ALADGMDV-VHacgIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGpALGAARLAQ 433
|
....
gi 88196792 478 LAVG 481
Cdd:PRK15027 434 IAAN 437
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
192-456 |
5.61e-18 |
|
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: 86.43 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 192 CFGTIDTWLL------YKLTkGSVyATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPVRDTSHNFGSVDEEIF-- 263
Cdd:cd07771 144 LLERADKLLMlpdllnYLLT-GEK-VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAee 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 264 --GVPIPIVAlVA--DQQSAMFGECCFQTGDVKLTMGT----GTFLD--INTGNSLQ------QTTGGFYPLI----GWK 323
Cdd:cd07771 222 lgLKGIPVIA-VAshDTASAVAAVPAEDEDAAFISSGTwsliGVELDepVITEEAFEagftneGGADGTIRLLknitGLW 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 324 IGQEvvCLAEsnagdtgtaikWAQQlDLFTDAAETEKMAKSLEDSEgvCFV----PSFsglQAPLNDPWACASFM---GL 396
Cdd:cd07771 301 LLQE--CRRE-----------WEEE-GKDYSYDELVALAEEAPPFG--AFIdpddPRF---LNPGDMPEAIRAYCretGQ 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 397 KPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLIN 456
Cdd:cd07771 362 PVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATG 421
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
21-509 |
1.70e-14 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 75.84 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 21 VLGLDVGSSVIRCHVYDRAARVCGS------SVQKVENlyPQigWVEIDPDVLWIQFVAVIKEAvkAAGIQMNQIVGLGI 94
Cdd:PRK10331 4 ILVLDCGATNVRAIAVDRQGKIVARastpnaSDIAAEN--SD--WHQWSLDAILQRFADCCRQI--NSELTECHIRGITV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 95 ST---QRATFitwnKKTGNHFHNFISWQDLRAVELVKSwnnsllmkifhsscrvLHFFTRSKRLFTAS---LFTFTTQqt 168
Cdd:PRK10331 78 TTfgvDGALV----DKQGNLLYPIISWKCPRTAAVMEN----------------IERYISAQQLQQISgvgAFSFNTL-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 169 sLRLVWILQNLTEVQkaveEENCCFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLPPV 248
Cdd:PRK10331 136 -YKLVWLKENHPQLL----EQAHAWLFISSLINHRLT--GEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 249 RDTSHNFGSVDEEI-----FGVPIPIVALVADQQSAMFGECCFQTGDVkLTMGTGTFLDINTGN--------------SL 309
Cdd:PRK10331 209 VEAGEQIGTLQPSAaallgLPVGIPVISAGHDTQFALFGSGAGQNQPV-LSSGTWEILMVRSAQvdtsllsqyagstcEL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 310 QQTTGGFYPLIGWkigqevvcLAesnagdTGTaIKWAQQLdLFTDAAETEKM---AKSL-EDSEGVCFVPSFSGLQApln 385
Cdd:PRK10331 288 DSQSGLYNPGMQW--------LA------SGV-LEWVRKL-FWTAETPYQTMieeARAIpPGADGVKMQCDLLACQN--- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 386 dpwacASFMGLKPSTSKYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADI 465
Cdd:PRK10331 349 -----AGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDA 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 88196792 466 DMSCLGAASLAGLAVGFWTDKEELK-KLRQSEVVFKPQKKCQEYE 509
Cdd:PRK10331 424 ETTVAGAAMFGWYGVGEFSSPEQARaQMKYQYRYFYPQTEPEFIE 468
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
20-518 |
8.80e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 67.34 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQK-----VENlYPqiGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGI 94
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQAEwrhlaVPD-VP--GSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 95 STQRATFITWNKkTGNHFhnfisWQ----DLRAVELVKSwnnsllMKIFHSScrvlhfftrskrlFTASLFTFTTQQTSL 170
Cdd:PRK10939 81 TSMREGIVLYDR-NGTEI-----WAcanvDARASREVSE------LKELHNN-------------FEEEVYRCSGQTLAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 171 ----RLVWILQNLTEVQKAVEEenccFGTIDTWLLYKLTkgSVYATDFSNASTTGLFDPYKMCWSGMITSLISIPLSLLP 246
Cdd:PRK10939 136 galpRLLWLAHHRPDIYRQAHT----ITMISDWIAYMLS--GELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 247 PVRDTSHNFGSVDEEI-----FGVPIPIVALVADQQSAmfgecCFQTGDVKL----TMGtGTFLD--INTGNSLQQttgg 315
Cdd:PRK10939 210 PVKETGTVLGHVTAKAaaetgLRAGTPVVMGGGDVQLG-----CLGLGVVRPgqtaVLG-GTFWQqvVNLPAPVTD---- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 316 fyPLIGWKIGQEVV---CLAESNAGDTGTAIKWaqqldlFTDA--AETEKMAKS--------LED--------SEGVcfV 374
Cdd:PRK10939 280 --PNMNIRINPHVIpgmVQAESISFFTGLTMRW------FRDAfcAEEKLLAERlgidayslLEEmasrvpvgSHGI--I 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 375 PSFSGLQAPLNdpW--ACASFMGLK--PSTS-KYHLVRAILESIAFRNKQLYEMMKKEIHIPVRKIRADGGVCKNGFVMQ 449
Cdd:PRK10939 350 PIFSDVMRFKS--WyhAAPSFINLSidPEKCnKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQ 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196792 450 MTSDLINENIDRPADIDMSCLGAASLAGLAVGFWTD-KEELKKLRQSEVVFKPQ-KKCQEYEMSLENWAKA 518
Cdd:PRK10939 428 ILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSlAETGERLVRWERTFEPNpENHELYQEAKEKWQAV 498
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
22-502 |
4.32e-10 |
|
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: 61.87 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 22 LGLDVGSSVIRCHVYDRAA--RVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRA 99
Cdd:cd07768 3 IGVDVGTSSARAGVYDLYAglEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDATCS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 100 TFITWNKKT-------GNHFHNFISWQDLRAVELVKSWNNsllmkifhsscrvlhffTRSKRLFTASLFTFTTQQTSLRL 172
Cdd:cd07768 83 LAIFDREGTplmalipYPNEDNVIFWMDHSAVNEAQWINM-----------------QCPQQLLDYLGGKISPEMGVPKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 173 VWILQNLTEVQKAVEEenccFGTIDTWLLYKLTKGSVYatdfsNASTTG---LFDPYKMCWSGMITSLISIPLSLLP--- 246
Cdd:cd07768 146 KYFLDEYSHLRDKHFH----IFDLHDYIAYELTRLYEW-----NICGLLgkeNLDGEESGWSSSFFKNIDPRLEHLTttk 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 247 ------PVRDTSHNFGSVDEEIFGVPIPIVALVA--DQQSAMFGECCFQTgDVKLTMGTGTFLDINTGNSLQQTTGGFY- 317
Cdd:cd07768 217 nlpsnvPIGTTSGVALPEMAEKMGLHPGTAVVVSciDAHASWFAVASPHL-ETSLFMIAGTSSCHMYGTTISDRIPGVWg 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 318 PLIGWKIGQEVVCLAESNAgdTGTAIKW-------AQQLDLFTDAAET-----EKMAKSLED----SEGVCFVPSFSGLQ 381
Cdd:cd07768 296 PFDTIIDPDYSVYEAGQSA--TGKLIEHlfeshpcARKFDEALKKGADiyqvlEQTIRQIEKnnglSIHILTLDMFFGNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 382 APLNDPWACASFMGLKPSTSKYHLV---RAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGVCKNGFVMQMTSDLINEN 458
Cdd:cd07768 374 SEFADPRLKGSFIGESLDTSMLNLTykyIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 88196792 459 IDRPADIDMSCLGAASLAGLAVGFWTDKEEL----KKLRQSEVVFKPQ 502
Cdd:cd07768 453 IIKPKENMMGILGAAVLAKVAAGKKQLADSIteadISNDRKSETFEPL 500
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
373-508 |
1.26e-09 |
|
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: 60.63 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 373 FVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVR---AILESIAFRNKQLYEMMKKEIHiPVRKIRADGGVCKNGFVMQ 449
Cdd:cd07782 383 VLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAAGH-KIDTIFMCGGLSKNPLFVQ 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 450 MTSDLINENIDRPADIDMSCLGAASLAGLAVG-FWTDKEELKKLRQSEVVFKPQKKCQEY 508
Cdd:cd07782 462 LHADVTGCPVVLPKEPEAVLLGAAILGAVASGdFPSLWDAMAAMSGPGKVVEPNEELKKY 521
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
404-481 |
1.53e-06 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 50.61 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 404 HLVRAILESIAFRNKQLYEMMKKEiHIPVRKIRADGGVC-KNGFVMQMTSDLINENIDrPADIDMSC-LGAASLAGLAVG 481
Cdd:PRK04123 412 DIYRALIEATAFGTRAIMECFEDQ-GVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQ-VVASDQCPaLGAAIFAAVAAG 489
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
20-125 |
2.52e-05 |
|
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: 46.76 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 20 FVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWVEIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGIStqrA 99
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFD---A 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 88196792 100 T--FITWNK--------KTGNHFHNFISWQDLRAVE 125
Cdd:cd07782 78 TcsLVVLDAegkpvsvsPSGDDERNVILWMDHRAVE 113
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
22-479 |
2.22e-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: 40.85 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 22 LGLDVGSSVIRCHVYDRAARVCGSSVQKVE-NLYPQIGW-VEIDPDVLWiqfvAVIKEAVKAAGIQMNQ--IVGLGIStq 97
Cdd:cd07778 3 IGIDVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWfVTQSSTEIW----KAIKTALKELIEELSDyiVSGIGVS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 98 rAT--------------FITWNKKTG--NHFHNFISWQDLRAVELVKsWNNSLLMKifhsscrvlhfftrSKRLFTASlf 161
Cdd:cd07778 77 -ATcsmvvmqrdsdtsyLVPYNVIHEksNPDQDIIFWMDHRASEETQ-WLNNILPD--------------DILDYLGG-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 162 TFTTQQTSLRLVWILQNLTEVQkaveEENCCFGTIDTWLLYKLtkgsvyATDFSNASTTGLFDPYKMC---------WSg 232
Cdd:cd07778 139 GFIPEMAIPKLKYLIDLIKEDT----FKKLEVFDLHDWISYML------ATNLGHSNIVPVNAPPSIGigidgslkgWS- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 233 mITSLISIPLSLLPPVRDTSHNFGSVdEEIFGVPIPIVALVADQQSAMFGE------------------CCFQTGDVKLT 294
Cdd:cd07778 208 -KDFYSKLKISTKVCNVGNTFKEAPP-LPYAGIPIGKVNVILASYLGIDKStvvghgcidcyagwfstfAAAKTLDTTLF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 295 M--GTGTFLDINTGNSLQQTT----GGFYPLIG----WKIGQ-------EVV-----CLAESNAGDTgtaikwaqqldLF 352
Cdd:cd07778 286 MvaGTSTCFLYATSSSQVGPIpgiwGPFDQLLKnysvYEGGQsatgkliEKLfnshpAIIELLKSDA-----------NF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196792 353 TDAAET--EKMAKSLEDSEGVCFVPSF-----SGLQAPLNDPWACASFMGLKPSTSKYHLVR---AILESIAFRNKQLYE 422
Cdd:cd07778 355 FETVEEkiDKYERLLGQSIHYLTRHMFfygdyLGNRTPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIID 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 88196792 423 MMKKEiHIPVRKIRADGGVCKNGFVMQMTSDLINE-NIDRPA-DIDMSCLGAASLAGLA 479
Cdd:cd07778 435 NFQKE-KIIIQKVVISGSQAKNARLLQLLSTVLSKiHIIVPLsDSKYAVVKGAALLGKA 492
|
|
| |
