|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
18-519 |
0e+00 |
|
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: 902.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 18 PFVGAIDEGTTSARFIIFRAgTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLVAVGGKVEEIITIGI 97
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPNNArniNYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQA 177
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGK---DHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 178 MEKGTAMFGTIDTWLMYNLTGGKDCGVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGV 257
Cdd:cd07792 157 VDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 258 LQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVPFYALEGSVSIAGA 337
Cdd:cd07792 237 LAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 338 AFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDI 417
Cdd:cd07792 317 AVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 418 LDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENRYQMEAP-LSKSGPREAI 496
Cdd:cd07792 397 LDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELkSLNEGGRTVF 476
|
490 500
....*....|....*....|...
gi 17864214 497 KPSISATDRNLRYQKWKMAIDRS 519
Cdd:cd07792 477 EPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
18-522 |
0e+00 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 806.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 18 PFVGAIDEGTTSARFIIFRAgTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLvavGGKVEEIITIGI 97
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDK-DGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKA---GIKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPnnarnINYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQA 177
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGY-----GEFIREKTGLPLDPYFSATKLRWLLDNVPGVREA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 178 MEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQG- 256
Cdd:TIGR01311 152 AERGELLFGTIDTWLIWNLTGGK---VHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 257 VLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAvPFYALEGSVSIAG 336
Cdd:TIGR01311 229 LGAEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKK-PVYALEGSVFVAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 337 AAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRD 416
Cdd:TIGR01311 308 AAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 417 ILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVE-NRYQMEAPLSKSGPReA 495
Cdd:TIGR01311 388 VLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGyWKSLEEIEALWRVEK-T 466
|
490 500
....*....|....*....|....*..
gi 17864214 496 IKPSISATDRNLRYQKWKMAIDRSLNW 522
Cdd:TIGR01311 467 FEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
18-523 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 714.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 18 PFVGAIDEGTTSARFIIF-RAGtdEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGAckkLVAVGGKVEEIITIG 96
Cdd:COG0554 3 KYILAIDQGTTSTRAILFdRDG--NIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREA---LAKAGISAEDIAAIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 97 ITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELletipNNARNINYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQ 176
Cdd:COG0554 78 ITNQRETTVVWDRKTGKPLYNAIVWQDRRTADICEEL-----KADGLEDLIREKTGLVLDPYFSATKIKWILDNVPGARE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 177 AMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQG 256
Cdd:COG0554 153 RAEAGELLFGTIDSWLIWKLTGGK---VHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 257 VL-QGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVpfYALEGSVSIA 335
Cdd:COG0554 230 LFgAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGKVT--YALEGSIFVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 336 GAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVR 415
Cdd:COG0554 308 GAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 416 DILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENRYQMEAPLSKSGPREA 495
Cdd:COG0554 388 DVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWKVDRR 467
|
490 500
....*....|....*....|....*...
gi 17864214 496 IKPSISATDRNLRYQKWKMAIDRSLNWE 523
Cdd:COG0554 468 FEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
19-516 |
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: 694.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGAIDEGTTSARFIIF-RAGtdEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGAckkLVAVGGKVEEIITIGI 97
Cdd:cd07769 1 YILAIDQGTTSTRAILFdEDG--NIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREA---LAKAGISASDIAAIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELletipNNARNINYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQA 177
Cdd:cd07769 76 TNQRETTVVWDKKTGKPLYNAIVWQDRRTADICEEL-----KAKGLEERIREKTGLPLDPYFSATKIKWILDNVPGARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 178 MEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSI-AQG 256
Cdd:cd07769 151 AERGELLFGTIDTWLIWKLTGGK---VHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTdPEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 257 VLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVpfYALEGSVSIAG 336
Cdd:cd07769 228 LGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIGGKVT--YALEGSIFIAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 337 AAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRD 416
Cdd:cd07769 306 AAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 417 ILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENrYQMEAPLSKSGPREAI 496
Cdd:cd07769 386 VLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGF-WKDLDELASLWQVDKR 464
|
490 500
....*....|....*....|.
gi 17864214 497 -KPSISATDRNLRYQKWKMAI 516
Cdd:cd07769 465 fEPSMDEEERERLYRGWKKAV 485
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
18-523 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 677.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 18 PFVGAIDEGTTSARFIIFragtDE---IVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLVAVGGKVEeIIT 94
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIF----DEkgnVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 95 IGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPNNarniNYLRPLCGLPLSPYFSGVKLRWLRDNVPVV 174
Cdd:PTZ00294 77 IGITNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGS----NFFQKITGLPISTYFSAFKIRWMLENVPAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 175 SQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSI- 253
Cdd:PTZ00294 153 KDAVKEGTLLFGTIDTWLIWNLTGGK---SHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTIs 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 254 --AQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVPFYALEGS 331
Cdd:PTZ00294 230 geAVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 332 VSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVC 411
Cdd:PTZ00294 310 IAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 412 FQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAA------YKAVEnryqmEA 485
Cdd:PTZ00294 390 LQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAglavgvWKSLE-----EV 464
|
490 500 510
....*....|....*....|....*....|....*...
gi 17864214 486 PLSKSGPREAIKPSISATDRNLRYQKWKMAIDRSLNWE 523
Cdd:PTZ00294 465 KKLIRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
19-522 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 661.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGAIDEGTTSARFIIFrAGTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLVAVGGKVEEII-TIGI 97
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIY-DRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDSGLkAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPNNARNinyLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQA 177
Cdd:PLN02295 80 TNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKH---FVETCGLPISTYFSATKLLWLLENVDAVKEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 178 MEKGTAMFGTIDTWLMYNLTGGKDCGVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGV 257
Cdd:PLN02295 157 VKSGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 258 -LQGIGITSVLGDQQAALVGQQClAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVPFYALEGSVSIAG 336
Cdd:PLN02295 237 pLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 337 AAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRD 416
Cdd:PLN02295 316 AAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 417 ILDSMHKDCKIP-----LAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVeNRYQMEAPLSKSG 491
Cdd:PLN02295 396 VLDAMRKDAGEEkshkgLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAV-GLWTEEEIFASEK 474
|
490 500 510
....*....|....*....|....*....|...
gi 17864214 492 PREAIK--PSISATDRNLRYQKWKMAIDRSLNW 522
Cdd:PLN02295 475 WKNTTTfrPKLDEEERAKRYASWCKAVERSFDL 507
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
19-523 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 654.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGAIDEGTTSARFIIF-RAGtdEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGAckkLVAVGGKVEEIITIGI 97
Cdd:PRK00047 6 YILALDQGTTSSRAIIFdHDG--NIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEA---LAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLEtipnnARNINYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQA 177
Cdd:PRK00047 81 TNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELKR-----DGYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 178 MEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQG- 256
Cdd:PRK00047 156 AEKGELLFGTIDTWLVWKLTGGK---VHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 257 -VLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVpfYALEGSVSIA 335
Cdd:PRK00047 233 fFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGIDGKVV--YALEGSIFVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 336 GAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVR 415
Cdd:PRK00047 311 GSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 416 DILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAV---ENRYQMEaplSKSGP 492
Cdd:PRK00047 391 DVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVgfwKDLDELK---EQWKI 467
|
490 500 510
....*....|....*....|....*....|.
gi 17864214 493 REAIKPSISATDRNLRYQKWKMAIDRSLNWE 523
Cdd:PRK00047 468 DRRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
19-517 |
0e+00 |
|
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: 646.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGAIDEGTTSARFIIF-RAGtdEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKlvaVGGKVEEIITIGI 97
Cdd:cd07786 1 YILAIDQGTTSSRAILFdHDG--NIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAK---AGIRASDIAAIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLEtipnnARNINYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQA 177
Cdd:cd07786 76 TNQRETTVVWDRETGKPVYNAIVWQDRRTADICEELKA-----EGHEEMIREKTGLVLDPYFSATKIRWILDNVPGARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 178 MEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGV 257
Cdd:cd07786 151 AERGELAFGTIDSWLIWKLTGGK---VHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 258 L-QGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVpfYALEGSVSIAG 336
Cdd:cd07786 228 LgAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLGGKVT--YALEGSIFIAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 337 AAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRD 416
Cdd:cd07786 306 AAVQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 417 ILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAA---------YKAVENRYQMEapl 487
Cdd:cd07786 386 LLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAglavglwksLDELAKLWQVD--- 462
|
490 500 510
....*....|....*....|....*....|
gi 17864214 488 sksgprEAIKPSISATDRNLRYQKWKMAID 517
Cdd:cd07786 463 ------RRFEPSMSEEEREALYAGWKKAVK 486
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
19-516 |
1.36e-146 |
|
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: 430.83 E-value: 1.36e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGAIDEGTTSARFIIFRAGTDEIVCFHQiEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLvavGGKVEEIITIGIT 98
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSE-KVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNA---GLTPEDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 99 NQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELletipNNARNINYLRPLCG----------------LPLSPYFSGV 162
Cdd:cd07793 77 TQRNTFLTWDKKTGKPLHNFITWQDLRAAELCESW-----NRSLLLKALRGGSKflhfltrnkrflaasvLKFSTAHVSI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 163 KLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPE 242
Cdd:cd07793 152 RLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGGK---VHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 243 ICSSSEFYGSIAQGVLQG-IGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRK 321
Cdd:cd07793 229 VKDTSGDFGSTDPSIFGAeIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIGGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 322 AVpfYALEGSVSIAGAAFNWLRDnMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEH 401
Cdd:cd07793 309 IT--YLAEGNASDTGTVIDWAKS-IGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 402 IVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENRY 481
Cdd:cd07793 386 LVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWK 465
|
490 500 510
....*....|....*....|....*....|....*.
gi 17864214 482 QMEApLSKSGPREAI-KPSISATDRNLRYQKWKMAI 516
Cdd:cd07793 466 SKEE-LKKLRKIEKIfEPKMDNEKREELYKNWKKAV 500
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
22-473 |
4.71e-94 |
|
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: 295.59 E-value: 4.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIFRAgTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECItgacKKLVA-VGGKVEEIITIGITNQ 100
Cdd:COG1070 5 GIDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAI----RELLAkAGVDPEEIAAIGVSGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 101 RESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNArninyLRPLCGLPLSPYFSGVKLRWLRDNVP-VVSQame 179
Cdd:COG1070 80 MHGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGEEA-----LYEITGNPLHPGFTAPKLLWLKENEPeIFAR--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 180 kgTAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYG----SIAQ 255
Cdd:COG1070 151 --IAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGtltaEAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 256 --GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTgPSIVHSTHGLLTTVGYQLGRKavpfYALEGSVS 333
Cdd:COG1070 224 etGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS-DKPLPDPEGRVHTFCHAVPGR----WLPMGATN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 334 IAGAAFNWLRDNMNLIQNS--GQIETMASTVD-NSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAV 410
Cdd:COG1070 299 NGGSALRWFRDLFADGELDdyEELNALAAEVPpGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGV 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864214 411 CFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAA 473
Cdd:COG1070 379 AFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLA 440
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
22-477 |
4.77e-92 |
|
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: 288.26 E-value: 4.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIF-RAGTdeIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLvavGGKVEEIITIGITNQ 100
Cdd:cd07779 4 GIDVGTTSTRAIIFdLDGN--IVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKA---GVDPEDIAAIGLTSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 101 RESTVVWDRNsGQPLVNAIIWLDNRTtstveelletipnnarninylrplcglplspyfsgvklrwlrdnvpvvsqamek 180
Cdd:cd07779 79 RSTFVPVDED-GRPLRPAISWQDKRT------------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 181 gtAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSI----AQ- 255
Cdd:cd07779 104 --AKFLTVQDYLLYRLTG-----EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLtkeaAEe 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 256 -GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGyqlgrkAVPF-YALEGSVS 333
Cdd:cd07779 177 tGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPS------AVPGkWVLEGSIN 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 334 IAGAAFNWLRDNM--NLIQNSGQ-------IETMASTVDN-SLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIV 403
Cdd:cd07779 251 TGGSAVRWFRDEFgqDEVAEKELgvspyelLNEEAAKSPPgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLA 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17864214 404 RATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAV 477
Cdd:cd07779 331 RAILEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGA 403
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
19-477 |
7.83e-83 |
|
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: 264.83 E-value: 7.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIFRAGTdEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLvavggKVEEIITIGIT 98
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFDEDG-RILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA-----GPDPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 99 NQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNArninyLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAM 178
Cdd:cd07773 75 SQGESGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGAEE-----LYRITGLPPSPMYSLAKLLWLREHEPEIFAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 179 EKgtamFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGVL 258
Cdd:cd07773 149 AK----WLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 259 QGIGITS----VLG--DQQAALVGQQCLAKGQAkaTYGTG---CFLLYNTGPSIVHSTHGLLTTVGYQLGRKavpFYALE 329
Cdd:cd07773 220 EELGLPAgtpvVVGghDHLCAALGAGVIEPGDV--LDSTGtaeALLAVVDEPPLDEMLAEGGLSYGHHVPGG---YYYLA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 330 GSVSiAGAAFNWLRDNM--NLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATL 407
Cdd:cd07773 295 GSLP-GGALLEWFRDLFggDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAIL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 408 EAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAV 477
Cdd:cd07773 374 EGLAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGA 442
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
22-473 |
9.30e-81 |
|
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: 257.49 E-value: 9.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIFRAgTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKlvaVGGKVEEIITIGITNQR 101
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAK---AGIDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 102 ESTVVWDRNsGQPLVNAIIWLDNRttstveelletipnnarninylrplcglplspyfsgvklrwlrdnvpvvsqamekg 181
Cdd:cd00366 80 PGVVLVDAD-GNPLRPAIIWLDRR-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 182 tAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQ------ 255
Cdd:cd00366 103 -AKFLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPeaaeet 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 256 GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTgPSIVHSTHGLLTTVGYQLGRkavpfYALEGSVSIA 335
Cdd:cd00366 177 GLPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCT-DEPVPPDPRLLNRCHVVPGL-----WLLEGAINTG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 336 GAAFNWLRDN----MNLIQNSGQIETMASTVD-NSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAV 410
Cdd:cd00366 251 GASLRWFRDEfgeeEDSDAEYEGLDELAAEVPpGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGV 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864214 411 CFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAA 473
Cdd:cd00366 331 AYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
19-474 |
7.98e-75 |
|
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: 244.76 E-value: 7.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIFRAgTDEIVCFHQIEVESIFQKEGWCEQDPM----AIVNTVNECitgackkLVAVGGKVEEIIT 94
Cdd:cd07808 2 LLG-IDLGTSSVKAVLVDE-DGRVLASASAEYPTSSPKPGWAEQDPEdwwqATKEALREL-------LAKAGISPSDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 95 IGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNARNINYLRPLCGLPLSpyfsgvKLRWLRDNVPvv 174
Cdd:cd07808 73 IGLTGQMHGLVLLDKN-GRPLRPAILWNDQRSAAECEELEARLGDEILIITGNPPLPGFTLP------KLLWLKENEP-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 175 sQAMEKgtamfgtIDTWLM------YNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSE 248
Cdd:cd07808 144 -EIFAR-------IRKILLpkdylrYRLTG-----ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 249 FYGSIAQGVLQGIGI---TSVL---GDQQAALVGQQCLAKGQAKATYGTGCFLLYNTgPSIVHSTHGLLTTVGYqlgrkA 322
Cdd:cd07808 211 IVGTLTPEAAEELGLpegTPVVagaGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPH-----A 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 323 VP--FYALeGSVSIAGAAFNWLRDNMNLIQNS-GQIETMASTVDNSLD-VYFVPAFNGLYAPYWNQDARGVICGLSEETT 398
Cdd:cd07808 285 VPgkWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPPGSEgLLFLPYLSGERTPYWDPNARGSFFGLSLSHT 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17864214 399 SEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAY 474
Cdd:cd07808 364 RAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAA 438
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
19-276 |
3.17e-73 |
|
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: 233.00 E-value: 3.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGAIDEGTTSARFIIF-RAGtdEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLvavGGKVEEIITIGI 97
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFnEQG--KIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQL---GISLKQIKGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIpnnarNINYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQA 177
Cdd:pfam00370 76 SNQGHGTVLLDKN-DKPLYNAILWKDRRTAEIVENLKEEG-----NNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 178 MEKgtamFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYG----SI 253
Cdd:pfam00370 150 IHK----FLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGelnpEL 220
|
250 260
....*....|....*....|....*
gi 17864214 254 AQ--GVLQGIGITSVLGDQQAALVG 276
Cdd:pfam00370 221 AAmwGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
22-512 |
1.58e-71 |
|
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: 236.30 E-value: 1.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIFRAGtDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLvavggKVEEIITIGITNQR 101
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKL-----GGGEVDAIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 102 ESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETipNNARNInYLRPLCglPLSPYFSGVKLRWLRDNVPVVSQAmekg 181
Cdd:cd07770 78 HSLLGVDED-GEPLTPVITWADTRAAEEAERLRKE--GDGSEL-YRRTGC--PIHPMYPLAKLLWLKEERPELFAK---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 182 TAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQGI 261
Cdd:cd07770 148 AAKFVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 262 GITS----VLG--DQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTtvgYQLGRKavpFYALEGSVSIA 335
Cdd:cd07770 223 GLLAgtpvVLGasDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWC---YRLDEN---RWLVGGAINNG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 336 GAAFNWLRDNMNLIQNS-GQIETMASTVDN-SLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQ 413
Cdd:cd07770 297 GNVLDWLRDTLLLSGDDyEELDKLAEAVPPgSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 414 VRDILDSMhKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVeNRYQMEAPLSKSGPR 493
Cdd:cd07770 377 LKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEAL-GLISSLEADELVKIG 454
|
490
....*....|....*....
gi 17864214 494 EAIKPSISATDrnlRYQKW 512
Cdd:cd07770 455 KVVEPDPENHA---IYAEL 470
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
22-477 |
1.09e-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: 218.16 E-value: 1.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIF-RAGtdEIVCFHQIEVESIFQKEGWCEQDPM----AIVNTVNECITGAckklvavGGKVEEIITIG 96
Cdd:cd07805 4 AIDLGTSGVKAALVdLDG--ELVASAFAPYPTYYPKPGWAEQDPEdwwdAVCRATRALLEKS-------GIDPSDIAAIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 97 ITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNnarnINYLRPLCGLPLSPYFSGVKLRWLRDNVPvvsQ 176
Cdd:cd07805 75 FSGQMQGVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGLGG----IEGYRLGGGNPPSGKDPLAKILWLKENEP---E 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 177 AMEKGTAMFGTIDtWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQG 256
Cdd:cd07805 147 IYAKTHKFLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 257 VLQGIGI---TSVL---GDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGyqlgrkAVP-FYALE 329
Cdd:cd07805 221 AAAELGLpagTPVVgggGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLAS------ADPgRYLLA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 330 GSVSIAGAAFNWLRDNMNLIQNSGQ-----IETMASTVD-NSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIV 403
Cdd:cd07805 295 AEQETAGGALEWARDNLGGDEDLGAddyelLDELAAEAPpGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLA 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17864214 404 RATLEAVCFQVRDILDSMHKDCKiPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIA-ETTALGAAMAAYKAV 477
Cdd:cd07805 375 RAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGL 448
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
19-477 |
5.90e-63 |
|
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: 212.77 E-value: 5.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIFRAgTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECItgacKKLVAVGG-KVEEIITIGI 97
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDE-DGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEII----RELLAKAGiSPKEIAAIGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNArninyLRPLCGLPLSPYFSGVKLRWLRDNVPVVSqa 177
Cdd:cd07804 76 SGLVPALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDR-----IFEITGNPLDSQSVGPKLLWIKRNEPEVF-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 178 meKGTAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTM-LMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSI--- 253
Cdd:cd07804 148 --KKTRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVtke 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 254 ---AQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGT-GCFLLYNTGPsivHSTHGLLTTVGYQLGRkavpfYALE 329
Cdd:cd07804 221 aaeETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVVTDKL---PTDPRLWLDYHDIPGT-----YVLN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 330 GSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDnSLD------------VYFVPAFNGLYAPYWNQDARGVICGLSEET 397
Cdd:cd07804 293 GGMATSGSLLRWFRDEFAGEEVEAEKSGGDSAYD-LLDeeaekippgsdgLIVLPYFMGERTPIWDPDARGVIFGLTLSH 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 398 TSEHIVRATLEAVCFQVRDILDSMHKDCkIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAV 477
Cdd:cd07804 372 TRAHLYRALLEGVAYGLRHHLEVIREAG-LPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGV 450
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
19-477 |
4.86e-53 |
|
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: 186.22 E-value: 4.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIF-RAGTdEIVCfHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLvavGGKVEEIITIGI 97
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFdLDGR-EIAV-ASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKS---GVDPSDIAGVGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNArninyLRPLCGLPLSPYFSGVKLRWLRDNVP-VVSQ 176
Cdd:cd07802 76 TGHGNGLYLVDKD-GKPVRNAILSNDSRAADIVDRWEEDGTLEK-----VYPLTGQPLWPGQPVALLRWLKENEPeRYDR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 177 AmekGTAMFGTiDtWLMYNLTGgkdcgVHKTDVTNASrTMLMNIETLQWDANLLKFFGLP--KTILPEICSSSEFYGSI- 253
Cdd:cd07802 150 I---RTVLFCK-D-WIRYRLTG-----EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVt 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 254 -----AQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTgcfllynTGPSIVHSTHGLLTTVGYQLGRKAVP--FY 326
Cdd:cd07802 219 aeaaaLTGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGT-------WSINEVVTDEPVVPDSVGSNSLHADPglYL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 327 ALEGSVSIAGAaFNWLRDN-MNLIQNSGQI------ETMASTVDNSLDVYFVPaFngLYAPYWNQDARGVICGLSEETTS 399
Cdd:cd07802 292 IVEASPTSASN-LDWFLDTlLGEEKEAGGSdydeldELIAAVPPGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTR 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17864214 400 EHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMvdGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAV 477
Cdd:cd07802 368 AHLLRAVYEGIAFSHRDHLERLLVARKPETIRLT--GGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAA 443
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
285-476 |
1.15e-51 |
|
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: 174.82 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 285 AKATYGTGCFLLYnTGPSIVHSTHGLLTTVGYQLGRkavPFYALEGSVSIAGAAFNWLRDNMNL---IQNSGQIETMAST 361
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYTNEMLP---GYWGLEGGQSAAGSLLAWLLQFHGLreeLRDAGNVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 362 VDNSLD-----VYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDG 436
Cdd:pfam02782 77 AALAAVapaggLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17864214 437 GMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKA 476
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
19-473 |
8.26e-45 |
|
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: 163.55 E-value: 8.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIF-RAGTdeIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECItgacKKLVAvGGKVEEIITIGI 97
Cdd:cd07783 2 FLG-IDLGTSGVRAVVVdEDGT--VLASASEPYPTSRPGPGWVEQDPEDWWEALRSLL----RELPA-ELRPRRVVAIAV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 TNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPnnarninYLRPLCGLPLSPYFSGVKLRWLRDNVP----- 172
Cdd:cd07783 74 DGTSGTLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAG-------AVAPRTGLAVSPSSSLAKLLWLKRHEPevlak 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 173 ---VVSQAmekgtamfgtidTWLMYNLTGgkDCGVhkTDVTNASRTMLmNIETLQWDANLLKFFGLPKTILPEICSSSEF 249
Cdd:cd07783 146 takFLHQA------------DWLAGRLTG--DRGV--TDYNNALKLGY-DPETGRWPSWLLALLGIPPDLLPRVVAPGTV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 250 YGSIAQGVLQGIGITS----VLG--DQQAALVGQQCLAKGQAKATYGTG-CFLLYNTGPsIVHSTHGLlttvgYQLgRKA 322
Cdd:cd07783 209 IGTLTAEAAEELGLPAgtpvVAGttDSIAAFLASGAVRPGDAVTSLGTTlVLKLLSDKR-VPDPGGGV-----YSH-RHG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 323 VPFYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTvdnSLDVYfvP-AFNGLYAPYWNQDARGVIcgLSEETTSEH 401
Cdd:cd07783 282 DGYWLVGGASNTGGAVLRWFFSDDELAELSAQADPPGPS---GLIYY--PlPLRGERFPFWDPDARGFL--LPRPHDRAE 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17864214 402 IVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIaETTALGAAMAA 473
Cdd:cd07783 355 FLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEE-EEAALGAALLA 425
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
22-473 |
3.69e-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: 162.01 E-value: 3.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIF-RAGtdEIVCFHQIEVEsiFQKEgwcEQDPMAIV---NTVNECITGACKKLVAVGGKV-EEIITIG 96
Cdd:cd07798 4 VIDIGTGGGRCALVdSEG--KIVAIAYREWE--YYTD---DDYPDAKEfdpEELWEKICEAIREALKKAGISpEDISAVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 97 ITNQRESTVVWDRNSgqplvNAIIWLDNRTTSTVEELLEtIPNNARNINYLRPlcGLPLSPYFSGVKLRWLRDNVPvvsQ 176
Cdd:cd07798 77 STSQREGIVFLDKDG-----RELYAGPNIDARGVEEAAE-IDDEFGEEIYTTT--GHWPTELFPAARLLWFKENRP---E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 177 AMEKgTAMFGTIDTWLMYNLtggkdCGVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQG 256
Cdd:cd07798 146 IFER-IATVLSISDWIGYRL-----TGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 257 VLQGIGITS----VLG--DQQAALVGQQCLAKGQAKATYGTgcfllynTGPsIVHSTHGLLTTVGYQL--GRKAVP-FYA 327
Cdd:cd07798 220 AARELGLPEgtpvVVGgaDTQCALLGSGAIEPGDIGIVAGT-------TTP-VQMVTDEPIIDPERRLwtGCHLVPgKWV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 328 LEGSVSIAGAAFNWLRDNMNLIQNS--GQIETMASTVD-NSLDVYfvpAFNGLYAPywNQDARGVICGL--------SEE 396
Cdd:cd07798 292 LESNAGVTGLNYQWLKELLYGDPEDsyEVLEEEASEIPpGANGVL---AFLGPQIF--DARLSGLKNGGflfptplsASE 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864214 397 TTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAA 473
Cdd:cd07798 367 LTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICA 443
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
22-473 |
5.69e-42 |
|
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: 155.84 E-value: 5.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIFRAGTDEIVCFHQIEVESIF--QKEGWCEQDPMAIVNTVNECITGACKKLVAvggkveEIITIGITN 99
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILESVSRPTPAPIssDDPGRSEQDPEKILEAVRNLIDELPREYLS------DVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 100 QRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNarninyLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAme 179
Cdd:cd07777 78 QMHGIVLWDED-GNPVSPLITWQDQRCSEEFLGGLSTYGEE------LLPKSGMRLKPGYGLATLFWLLRNGPLPSKA-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 180 kgtAMFGTIDTWLMYNLTGGKDcgvHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQ 259
Cdd:cd07777 149 ---DRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 260 GIGITSVLGDQQAALVGqqCLAKGQAKA--TYGTGCFLlyntgpSIVhsTHGLLTTVGYQLgrkaVPFYalEGSV----- 332
Cdd:cd07777 223 GIPVYVALGDNQASVLG--SGLNEENDAvlNIGTGAQL------SFL--TPKFELSGSVEI----RPFF--DGRYllvaa 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 333 SI-AGAAFNWL----RDNMNLI---QNSGQI-ETMASTVDNSL--DVYFVPAFNGlyaPYWNQDARGVICGLSEETTS-E 400
Cdd:cd07777 287 SLpGGRALAVLvdflREWLRELggsLSDDEIwEKLDELAESEEssDLSVDPTFFG---ERHDPEGRGSITNIGESNFTlG 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17864214 401 HIVRATLEAVCFQVRDILDSMHKDcKIPLAKLMVDGGMTVNNLFLQLQ-SDLVGIQVLRAKIAETTALGAAMAA 473
Cdd:cd07777 364 NLFRALCRGIAENLHEMLPRLDLD-LSGIERIVGSGGALRKNPVLRRIiEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
19-473 |
1.87e-39 |
|
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: 149.24 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIFRAGTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGAckkLVAVGGKVEEIITIGIT 98
Cdd:cd07809 2 VLG-IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAAIGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 99 NQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNARNINYLRPLCGlplspyFSGVKLRWLRDNVPvvsQAM 178
Cdd:cd07809 78 GQMHGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPAR------FTASKLLWLKENEP---EHY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 179 EKgTAMFGTIDTWLMYNLTGGKdcgvhKTDVTNASRTMLMNIETLQWDANLLKFFGLPKT---ILPEICSSSEFYGSIAQ 255
Cdd:cd07809 148 AR-IAKILLPHDYLNWKLTGEK-----VTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDlrdLLPEVLPAGEVAGRLTP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 256 ------GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGT-GCFLLYNTGPsiVHSTHGLLTT-----VGYqlgrkaV 323
Cdd:cd07809 222 egaeelGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGTAYGVSDKP--VSDPHGRVATfcdstGGM------L 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 324 PfyalegSVSIAGAAFNWLRDNMNLIQNS-GQIETMASTVD-NSLDVYFVPAFNGLYAPYWnQDARGVICGLSEE-TTSE 400
Cdd:cd07809 294 P------LINTTNCLTAWTELFRELLGVSyEELDELAAQAPpGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRA 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864214 401 HIVRATLEAVCFQVRDILDSMHKDCkIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAA 473
Cdd:cd07809 367 NLARAALEGATFGLRYGLDILRELG-VEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQA 438
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
23-476 |
1.30e-35 |
|
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: 139.21 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 23 IDEGTTSARFIIFRAGTDEIVCFHQIEVESIFQ--KEGWCEQDPMAIVNTVNECITGACKKLvavGGKVEEIITIGI--T 98
Cdd:cd07781 5 IDFGTQSVRAGLVDLADGEELASAVVPYPTGYIppRPGWAEQNPADYWEALEEAVRGALAEA---GVDPEDVVGIGVdtT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 99 nqrESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETI-PNNARNINYlrplCGLPLSP--YFSgvKLRWLRDNVPVVS 175
Cdd:cd07781 82 ---SSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAhPALEYYLAY----YGGVYSSewMWP--KALWLKRNAPEVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 176 QA----MEKGtamfgtiDtWLMYNLTGgkdcgVHKTDVTNAS-RTMLMNIETLqWDANLLK-----FFGLPKTILPEICS 245
Cdd:cd07781 153 DAaytiVEAC-------D-WINARLTG-----RWVRSRCAAGhKWMYNEWGGG-PPREFLAaldpgLLKLREKLPGEVVP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 246 SSEFYGSI----AQ--GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGT-GCFLLynTGPSIVHsTHGLLTTV---- 314
Cdd:cd07781 219 VGEPAGTLtaeaAErlGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTsTCHLM--VSPKPVD-IPGICGPVpdav 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 315 --GYqlgrkavpfYALEGSVSIAGAAFNWLRDNMNLIQNSGQIET------MASTVDN------SLDvyfvpAFNGLYAP 380
Cdd:cd07781 296 vpGL---------YGLEAGQSAVGDIFAWFVRLFVPPAEERGDSIyallseEAAKLPPgesglvALD-----WFNGNRTP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 381 YWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGGMTVNN-LFLQLQSDLVGIQVLRA 459
Cdd:cd07781 362 LVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAEKNpLWMQIYADVLGRPIKVP 440
|
490
....*....|....*..
gi 17864214 460 KIAETTALGAAMAAYKA 476
Cdd:cd07781 441 KSDQAPALGAAILAAVA 457
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
22-473 |
3.41e-35 |
|
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: 137.37 E-value: 3.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIFRAGTDEIVCfHQIEVESIFQKEGWCEQDPMAIVNTVNECItgacKKLVA-VGGKVEEIITIGITNQ 100
Cdd:cd24121 4 GIDAGTSVVKAVAFDLDGRELAV-AARRNAVLYPQPGWAEQDMNETWQAVVATI----REVVAkLDVLPDRVAAIGVTGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 101 RESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETiPNNARNINYlrplCGLPLSPYFSGVKLRWLRDNVPvvsQAMEK 180
Cdd:cd24121 79 GDGTWLVDED-GRPVRDAILWLDGRAADIVERWQAD-GIAEAVFEI----TGTGLFPGSQAAQLAWLKENEP---ERLER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 181 GTAMFGTIDtWLMYNLTggkdcGVHKTDVTNASRTMLmNIETLQWDANLLKFFGLP--KTILPEICSSSE------FYGS 252
Cdd:cd24121 150 ARTALHCKD-WLFYKLT-----GEIATDPSDASLTFL-DFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEvigpltPEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 253 IAQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLL----------YNTGPSIVHSTHGLLTtvgyqlgrKA 322
Cdd:cd24121 223 AATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEvvvdepdlepEGVGYTICLGVPGRWL--------RA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 323 VPfyALEGSVSI--------AGAAFNWLRDNMNLIQNsgqIETMASTVD-NSLDVYFVP--AFNGLYAPYWNQDARGVIC 391
Cdd:cd24121 295 MA--NMAGTPNLdwflrelgEVLKEGAEPAGSDLFQD---LEELAASSPpGAEGVLYHPylSPAGERAPFVNPNARAQFT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 392 GLSEETTSEHIVRATLEAVCFQVRDILDSMhkdcKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAM 471
Cdd:cd24121 370 GLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAM 445
|
..
gi 17864214 472 AA 473
Cdd:cd24121 446 NA 447
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
22-477 |
5.73e-24 |
|
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: 105.11 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFIIFragtDEIvcFHQIeveSIFQKEgW----CEQDPMAIVNTVN-------ECITGACKKlvaVGGKVE 90
Cdd:cd07775 4 ALDAGTGSGRAVIF----DLE--GNQI---AVAQRE-WrhkeVPDVPGSMDFDTEknwklicECIREALKK---AGIAPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 91 EIITIGITNQRESTVVWDRNsGQPlvnaiIW----LDNRTTSTVEELLETIPNNARNInYLR-----PLCGLPlspyfsg 161
Cdd:cd07775 71 SIAAISTTSMREGIVLYDNE-GEE-----IWacanVDARAAEEVSELKELYNTLEEEV-YRIsgqtfALGAIP------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 162 vKLRWLRDNVPVVSQAmekgTAMFGTIDTWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILP 241
Cdd:cd07775 137 -RLLWLKNNRPEIYRK----AAKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 242 EICSSSEFYGSIAQ------GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVG 315
Cdd:cd07775 207 PVVESGTVIGKVTKeaaeetGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 316 yqlGRKAVPFYalEGSVSIAGAAFNWLRDNM-----NLIQNSGQ-----IETMASTvdnsldvyfVPAfnglyapywnqD 385
Cdd:cd07775 287 ---VIPDMWQA--EGISFFPGLVMRWFRDAFcaeekEIAERLGIdaydlLEEMAKD---------VPP-----------G 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 386 ARGVICGLS----------------------EETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNL 443
Cdd:cd07775 342 SYGIMPIFSdvmnyknwrhaapsflnldidpEKCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKL 421
|
490 500 510
....*....|....*....|....*....|....
gi 17864214 444 FLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAV 477
Cdd:cd07775 422 WCQILADVLGLPVKVPVVKEATALGAAIAAGVGA 455
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
19-511 |
3.07e-23 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 102.74 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIFRAgTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECItgackKLVAVGGKVEEIITIGIT 98
Cdd:PRK15027 2 YIG-IDLGTSGVKVILLNE-QGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAM-----KALGDQHSLQDVKALGIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 99 NQRESTVVWDRNSgQPLVNAIIWLDNRTTSTVEELLETIPNNarninylRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAM 178
Cdd:PRK15027 75 GQMHGATLLDAQQ-RVLRPAILWNDGRCAQECALLEARVPQS-------RVITGNLMMPGFTAPKLLWVQRHEPEIFRQI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 179 EKgtaMFGTIDtWLMYNLTGgkdcgVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGVL 258
Cdd:PRK15027 147 DK---VLLPKD-YLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 259 QGIGITSVL-----GDQQAALVGQQCLAKGQAKATYGT-GCFLLYNTG-----PSIVHS-THGLLttvgyqlGRkavpfY 326
Cdd:PRK15027 218 KAWGMATVPvvaggGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSfCHALP-------QR-----W 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 327 ALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRAT 406
Cdd:PRK15027 286 HLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 407 LEAVCFQVRDILDSMHkDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQV-LRAKIAETTALGAAMAAYKAVENryqmEA 485
Cdd:PRK15027 366 LEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAANP----EK 440
|
490 500
....*....|....*....|....*..
gi 17864214 486 PLSKSGPREAIKPS-ISATDRNLRYQK 511
Cdd:PRK15027 441 SLIELLPQLPLEQShLPDAQRYAAYQP 467
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
45-477 |
6.28e-22 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 98.56 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 45 FHQIEVESIFQKEGWCeqdpmaivntvnecitgACKKLVAVGGKveEIITIGITNQRESTVVWDRNsGQPLVNAIIWLDN 124
Cdd:PRK10331 44 WHQWSLDAILQRFADC-----------------CRQINSELTEC--HIRGITVTTFGVDGALVDKQ-GNLLYPIISWKCP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 125 RTTSTVEELLETIPnnarnINYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKgtamFGTIDTWLMYNLTGgkdcgV 204
Cdd:PRK10331 104 RTAAVMENIERYIS-----AQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHA----WLFISSLINHRLTG-----E 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 205 HKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYG----SIAQ--GVLQGIGITSVLGDQQAALVGQQ 278
Cdd:PRK10331 170 FTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGtlqpSAAAllGLPVGIPVISAGHDTQFALFGSG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 279 ClAKGQAKATYGTGCFLLYNTG---PSIVHSTHGLLTTVGYQLGrkavpFYAlEGSVSIAGAAFNWLRdnmNLIQNSGQI 355
Cdd:PRK10331 250 A-GQNQPVLSSGTWEILMVRSAqvdTSLLSQYAGSTCELDSQSG-----LYN-PGMQWLASGVLEWVR---KLFWTAETP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 356 -ETM---ASTVDNSLD-VYFVPAFNGLyapywnqdARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLA 430
Cdd:PRK10331 320 yQTMieeARAIPPGADgVKMQCDLLAC--------QNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKAS 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 17864214 431 KLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAV 477
Cdd:PRK10331 392 ELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGV 438
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
19-498 |
1.46e-18 |
|
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: 88.84 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIFRAGTDEIVCFHQIEV-ESIFQKEGWCEQDPMAIVNTVNECITGACKKlvaVGGKVEEIITIGI 97
Cdd:cd07768 2 GIG-VDVGTSSARAGVYDLYAGLEMAQEPVPYyQDSSKKSWKFWQKSTEIIKALQKCVQKLNIR---EGVDAYEVKGCGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 98 tNQRESTVVWDRNsGQPLV---------NAIIWLDNRTTSTVEELLETIPNNarninyLRPLCGLPLSPYFSGVKLRWLR 168
Cdd:cd07768 78 -DATCSLAIFDRE-GTPLMalipypnedNVIFWMDHSAVNEAQWINMQCPQQ------LLDYLGGKISPEMGVPKLKYFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 169 DNVPVVSQAmekgTAMFGTIDTWLMYNLTggkdcgvhktdvtnasRTMLMNIETLQWDANLLKFFGLPktilpeicsSSE 248
Cdd:cd07768 150 DEYSHLRDK----HFHIFDLHDYIAYELT----------------RLYEWNICGLLGKENLDGEESGW---------SSS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 249 FYGSIAQGVLQG-----------IGITSVLGDQQAA----LVGQQCLAKGQAKATYGTGCFLLYNTGPSIV-----HSTH 308
Cdd:cd07768 201 FFKNIDPRLEHLtttknlpsnvpIGTTSGVALPEMAekmgLHPGTAVVVSCIDAHASWFAVASPHLETSLFmiagtSSCH 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 309 GLLTTVGYQLGRKAVPFYAL--------EGSVSIAGAAFNWLRDN------MNLIQNSGQ---------IETMASTVDNS 365
Cdd:cd07768 281 MYGTTISDRIPGVWGPFDTIidpdysvyEAGQSATGKLIEHLFEShpcarkFDEALKKGAdiyqvleqtIRQIEKNNGLS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 366 LDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSE---HIVRATLEAVCFQVRDILDSMHKDcKIPLAKLMVDGGMTVNN 442
Cdd:cd07768 361 IHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLnltYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNE 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 443 LFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENRYQM----EAPLSKSGPREAIKP 498
Cdd:cd07768 440 RLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQLAdsitEADISNDRKSETFEP 499
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
19-499 |
9.59e-17 |
|
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: 82.97 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 19 FVGaIDEGTTSARFIIFrAGTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKlvaVGGKVEEIITIGIT 98
Cdd:cd07782 2 YIG-VDVGTGSARAGLF-DLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEG---AGVDPEQVKGIGFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 99 nQRESTVVWDRNsGQPLV---------NAIIWLDNRTTSTVEELletipnNARNINYLRplcglplspYFSGV------- 162
Cdd:cd07782 77 -ATCSLVVLDAE-GKPVSvspsgdderNVILWMDHRAVEEAERI------NATGHEVLK---------YVGGKispemep 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 163 -KLRWLRDNVPvvsQAMEKGTAMFGTIDtWLMYNLTGgkdcgvhktdvtNASRT----------MLMNIETLQWDANLLK 231
Cdd:cd07782 140 pKLLWLKENLP---ETWAKAGHFFDLPD-FLTWKATG------------SLTRSlcslvckwtyLAHEGSEGGWDDDFFK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 232 FFGLPktilpEICSssEFYGSIAQGVL-QGIGITSVLGDQQAALVGqqcLAKGQAKAT-----Y----GT-GCFLlyNTG 300
Cdd:cd07782 204 EIGLE-----DLVE--DNFAKIGSVVLpPGEPVGGGLTAEAAKELG---LPEGTPVGVslidaHagglGTlGADV--GGL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 301 PSIVHSTHGLLTTVG------YQLGRKAV-------PFY-AL-------EGSVSIAGA----------AFNWLRdnmNLI 349
Cdd:cd07782 272 PCEADPLTRRLALICgtsschMAVSPEPVfvpgvwgPYYsAMlpglwlnEGGQSATGAlldhiiethpAYPELK---EEA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 350 QNSGQ---------IETMASTVDNSL-----DVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVR---ATLEAVCF 412
Cdd:cd07782 349 KAAGKsiyeylnerLEQLAEEKGLPLayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAY 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 413 QVRDILDSMHKdCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENRYQM-EAPLSKSG 491
Cdd:cd07782 429 GTRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLwDAMAAMSG 507
|
....*...
gi 17864214 492 PREAIKPS 499
Cdd:cd07782 508 PGKVVEPN 515
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
323-477 |
1.82e-16 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 82.09 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 323 VP-FYALEGSVSIAGAAFNWLRDNMNLiqnSGQIETMASTVDNSL----------------DVYFVPAFNGLYAPYWNQD 385
Cdd:COG1069 314 VPgMWGYEAGQSAVGDIFAWFVRLLVP---PLEYEKEAEERGISLhpllteeaaklppgesGLHALDWFNGNRSPLADQR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 386 ARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMhKDCKIPLAKLMVDGG-MTVNNLFLQLQSDLVGIQVLRAKIAET 464
Cdd:COG1069 391 LKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERF-EEEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQA 469
|
170
....*....|...
gi 17864214 465 TALGAAMAAykAV 477
Cdd:COG1069 470 CALGAAMFA--AV 480
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
16-473 |
8.50e-15 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 76.97 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 16 SGPFVGAIDEGTTSARFIIF-RAGtdeivcfHQIEVEsifQKEGWCEQDP-----MAIVNTVN-----ECITGACKKlva 84
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFdLNG-------NQIAVG---QAEWRHLAVPdvpgsMEFDLEKNwqlacQCIRQALQK--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 85 VGGKVEEIITIGITNQRESTVVWDRNsGQPlvnaiIW----LDNRTTSTVEELLETIPNNARNInYLR-----PLCGLPl 155
Cdd:PRK10939 68 AGIPASDIAAVSATSMREGIVLYDRN-GTE-----IWacanVDARASREVSELKELHNNFEEEV-YRCsgqtlALGALP- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 156 spyfsgvKLRWLRDNVPVVSQAMEKGTaMfgtIDTWLMYNLtggkdCGVHKTDVTNASRTMLMNIETLQWDANLLKFFGL 235
Cdd:PRK10939 140 -------RLLWLAHHRPDIYRQAHTIT-M---ISDWIAYML-----SGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 236 PKTILPEICSSSEFYGSIAQ------GVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHG 309
Cdd:PRK10939 204 RADILPPVKETGTVLGHVTAkaaaetGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 310 LlttvgyqlgrkAVPFYALEGSV---SIA---GAAFNWLRDNM-----NLIQNSGQ-----IETMASTVD-NSLDVyfVP 372
Cdd:PRK10939 284 I-----------RINPHVIPGMVqaeSISfftGLTMRWFRDAFcaeekLLAERLGIdayslLEEMASRVPvGSHGI--IP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 373 AF-NGLYAPYWNQDARGVIcGLS---EETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQ 448
Cdd:PRK10939 351 IFsDVMRFKSWYHAAPSFI-NLSidpEKCNKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQIL 429
|
490 500
....*....|....*....|....*
gi 17864214 449 SDLVGIQVLRAKIAETTALGAAMAA 473
Cdd:PRK10939 430 ADVTGLPVKVPVVKEATALGCAIAA 454
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
22-472 |
1.62e-14 |
|
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: 75.64 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 22 AIDEGTTSARFII--FRAGTDEIVCFHQIEVESIFQKEGWCeQDPMAIVNtvnECITGackkLVAVGGKVEEIITIGITn 99
Cdd:cd07771 4 AVDLGASSGRVILgsLDGGKLELEEIHRFPNRPVEINGHLY-WDIDRLFD---EIKEG----LKKAAEQGGDIDSIGID- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 100 qresTvvW-------DRNsGQPLVNAIIWLDNRTTSTVEELLETIPNNarninYLRPLCGLPLSPYFSGVKLRWLRDNVP 172
Cdd:cd07771 75 ----T--WgvdfgllDKN-GELLGNPVHYRDPRTEGMMEELFEKISKE-----ELYERTGIQFQPINTLYQLYALKKEGP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 173 vvsqamekgtAMFGTIDTWLM------YNLTGGKdcgvhKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSS 246
Cdd:cd07771 143 ----------ELLERADKLLMlpdllnYLLTGEK-----VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 247 SEFYGSI-----AQGVLQGIGITSVLG-DQQAALVGQQCLAKGQAkatY---GT----GCFLlynTGPsivhsthgLLTT 313
Cdd:cd07771 208 GTVLGTLkpevaEELGLKGIPVIAVAShDTASAVAAVPAEDEDAA---FissGTwsliGVEL---DEP--------VITE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 314 VGYQLGrkavpfYALEGSV--------SIAG------AAFNWLRDNMNLiqNSGQIETMASTVDnSLDVYFVPAFNGLYA 379
Cdd:cd07771 274 EAFEAG------FTNEGGAdgtirllkNITGlwllqeCRREWEEEGKDY--SYDELVALAEEAP-PFGAFIDPDDPRFLN 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 380 PywnQDARGVICGLSEET------TSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKL-MVDGGmtVNNLFL-QLQSDL 451
Cdd:cd07771 345 P---GDMPEAIRAYCRETgqpvpeSPGEIARCIYESLALKYAKTIEELEELTGKRIDRIhIVGGG--SRNALLcQLTADA 419
|
490 500
....*....|....*....|.
gi 17864214 452 VGIQVlRAKIAETTALGAAMA 472
Cdd:cd07771 420 TGLPV-IAGPVEATAIGNLLV 439
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
374-513 |
3.01e-10 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 62.56 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 374 FNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHkDCKIPLAKLMVDGGMTVNNLFL-QLQSDLV 452
Cdd:PRK04123 385 FNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGIARKNPVLmQIYADVL 463
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17864214 453 G--IQVLRAKiaETTALGAAM----AA--YKAVEnryqmEAPLS-KSGPREAIKPSISATDR-NLRYQKWK 513
Cdd:PRK04123 464 NrpIQVVASD--QCPALGAAIfaavAAgaYPDIP-----EAQQAmASPVEKTYQPDPENVARyEQLYQEYK 527
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
199-505 |
3.77e-07 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 52.56 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 199 GKDCGVhktDVTNASRTMLMNIETLQWDANLLKFFGLP--KTILPEICSSSEFYGSIAQGVLQGIGITS---VL---GDQ 270
Cdd:cd07776 198 GRYAPI---DESDGSGMNLMDIRSRKWSPELLDAATAPdlKEKLGELVPSSTVAGGISSYFVERYGFSPdclVVaftGDN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 271 QAALVGQqCLAKGQAKATYGT-GCFLLYNTGPSIVHSTHglltTVGYQLGRKAvpFYAL----EGSvsiagAAFNWLRDN 345
Cdd:cd07776 275 PASLAGL-GLEPGDVAVSLGTsDTVFLVLDEPKPGPEGH----VFANPVDPGS--YMAMlcykNGS-----LARERVRDR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 346 MNLiqnsGQIET----MASTV---DNSLDVYF-----VPafNGLYAPYWNQDARGVIcglsEETTSEHIVRATLEAVCFQ 413
Cdd:cd07776 343 YAG----GSWEKfnelLESTPpgnNGNLGLYFdepeiTP--PVPGGGRRFFGDDGVD----AFFDPAVEVRAVVESQFLS 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 414 VRdiLDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENR-----YQMEAPLS 488
Cdd:cd07776 413 MR--LHAERLGSDIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAgsgdfSPEFVVFS 490
|
330
....*....|....*..
gi 17864214 489 KSGPREAIKPSISATDR 505
Cdd:cd07776 491 AEEPKLVAEPDPEAAEV 507
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|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
92-237 |
9.19e-07 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 51.26 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 92 IITIGITNQRESTVVWDRNsGQPLVNAIIWLDNRTTSTVEELLETIpnnARNINYLRplCGLPLSPYFSGVKLRWLRDNV 171
Cdd:PRK10640 56 IDSIGIDTWGVDYVLLDKQ-GQRVGLPVSYRDSRTDGVMAQAQQQL---GKRDIYRR--SGIQFLPFNTLYQLRALTEQQ 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17864214 172 P-VVSQAmekgtAMFGTIDTWLMYNLTGGKDCgvhktDVTNASRTMLMNIETLQWDANLLKFFGLPK 237
Cdd:PRK10640 130 PeLIAQV-----AHALLIPDYFSYRLTGKMNW-----EYTNATTTQLVNINSDDWDESLLAWSGAPK 186
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
387-473 |
1.10e-04 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 44.56 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 387 RGVICGLSEETTSEHIVRATLEAVCFQvRDILDSMHKDCKiplaKLMVDGGMTVNNLFLQ-LQSDLVGIQVLRAKIAETT 465
Cdd:cd07772 342 GGRGVLSAFPSAEEAYALAILYLALMT-DYALDLLGSGVG----RIIVEGGFAKNPVFLRlLAALRPDQPVYLSDDSEGT 416
|
....*...
gi 17864214 466 ALGAAMAA 473
Cdd:cd07772 417 ALGAALLA 424
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
380-516 |
3.19e-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: 40.08 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17864214 380 PYWNQDARGVICGLSEETTSEHIVR---ATLEAVCFQVRDILDSMHKDCkIPLAKLMVDGGMTVNNLFLQLQS---DLVG 453
Cdd:cd07778 392 PYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKEK-IIIQKVVISGSQAKNARLLQLLStvlSKIH 470
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17864214 454 IQVLRAKIAETTALGAAMAAYKAVENRYQMEAPLSKSGPREAIKPSISATDRNLRYQKWKMAI 516
Cdd:cd07778 471 IIVPLSDSKYAVVKGAALLGKAAFLHNQSIEERLISLKNEDQISICASASIVKLVSDETKLAI 533
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