|
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; ... |
11-510 |
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: 985.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 11 PLVGAVDQGTSSTRFLVFNpQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGQQSIDISNIKAIGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFD-STGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 91 TNQRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIED 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 171 GRAIFGTVDSWLIWCMTGGINGGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSGVLEG 250
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 251 VPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGRQEPVYYALEGSVAIAGAVVS 330
Cdd:cd07792 240 VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 331 WIKNNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDA 410
Cdd:cd07792 320 WLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 411 MNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGVSVWSLDPKDLSSVQMEKFEPQ 490
Cdd:cd07792 400 MNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQ 479
|
490 500
....*....|....*....|
gi 49355801 491 INVEESEGRYATWKKAVLKS 510
Cdd:cd07792 480 ISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
11-513 |
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: 817.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 11 PLVGAVDQGTSSTRFLVFNPqTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFDK-DGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 91 TNQRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSISVsnNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIED 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYG--EFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 171 GRAIFGTVDSWLIWCMTGGingGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSG-VLE 249
Cdd:TIGR01311 155 GELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGlLGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 250 GVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGRQEPVYyALEGSVAIAGAVV 329
Cdd:TIGR01311 232 EIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPVY-ALEGSVFVAGAAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 330 SWIKNNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILD 409
Cdd:TIGR01311 311 QWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 410 AMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGVSVWSLDPKDLSSVQmEKFEP 489
Cdd:TIGR01311 391 AMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVE-KTFEP 469
|
490 500
....*....|....*....|....
gi 49355801 490 QINVEESEGRYATWKKAVLKSMGW 513
Cdd:TIGR01311 470 EMDEEEREARYAGWKEAVKRSLGW 493
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
13-514 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 761.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 13 VGAVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVTN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 93 QRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSISvsNNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIEDGR 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGL--EDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 173 AIFGTVDSWLIWCMTGGingGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSGVL-EGV 251
Cdd:COG0554 159 LLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFgAEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 252 PISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGRQepVYYALEGSVAIAGAVVSW 331
Cdd:COG0554 236 PIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGK--VTYALEGSIFVAGAAVQW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 332 IKNNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDAM 411
Cdd:COG0554 314 LRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 412 NSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGvsVWSlDPKDLSSV-QMEK-FEP 489
Cdd:COG0554 394 EADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVG--FWK-SLEELAALwKVDRrFEP 470
|
490 500
....*....|....*....|....*
gi 49355801 490 QINVEESEGRYATWKKAVLKSMGWV 514
Cdd:COG0554 471 QMDEEERERLYAGWKKAVERTLGWA 495
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
13-507 |
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: 750.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 13 VGAVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVTN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAG---ISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 93 QRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSisVSNNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIEDGR 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK--GLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 173 AIFGTVDSWLIWCMTGGingGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVK-SGVLEGV 251
Cdd:cd07769 156 LLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDpEGLGAGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 252 PISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGrqEPVYYALEGSVAIAGAVVSW 331
Cdd:cd07769 233 PIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIG--GKVTYALEGSIFIAGAAIQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 332 IKNNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDAM 411
Cdd:cd07769 311 LRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 412 NSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGvsVWSlDPKDLSS-VQMEK-FEP 489
Cdd:cd07769 391 EKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVG--FWK-DLDELASlWQVDKrFEP 467
|
490
....*....|....*...
gi 49355801 490 QINVEESEGRYATWKKAV 507
Cdd:cd07769 468 SMDEEERERLYRGWKKAV 485
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-514 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 714.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 12 LVGAVDQGTSSTRFLVFnPQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGQQSIDI-SNIKAIGV 90
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIY-DRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVdSGLKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 91 TNQRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIED 170
Cdd:PLN02295 80 TNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 171 GRAIFGTVDSWLIWCMTGGINGGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLV-KSGVLE 249
Cdd:PLN02295 160 GDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIaKGWPLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 250 GVPISGCLGDQSAALVGQLClQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGRQEPVYYALEGSVAIAGAVV 329
Cdd:PLN02295 240 GVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 330 SWIKNNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILD 409
Cdd:PLN02295 319 QWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 410 AMNSDCGIPLTH-----LQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAegVSVWSldPKDLSSVQM 484
Cdd:PLN02295 399 AMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLA--VGLWT--EEEIFASEK 474
|
490 500 510
....*....|....*....|....*....|....
gi 49355801 485 EK----FEPQINVEESEGRYATWKKAVLKSMGWV 514
Cdd:PLN02295 475 WKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-516 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 708.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 11 PLVGAVDQGTSSTRFLVFNpQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGQQSIDISnIKAIGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFD-EKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 91 TNQRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSISvSNNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIED 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYG-GSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 171 GRAIFGTVDSWLIWCMTGGingGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS---GV 247
Cdd:PTZ00294 159 GTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGeavPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 248 LEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGRQEPVYYALEGSVAIAGA 327
Cdd:PTZ00294 236 LEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAVAGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 328 VVSWIKNNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREI 407
Cdd:PTZ00294 316 GVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 408 LDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAegVSVW-SLDP-KDLSSVQME 485
Cdd:PTZ00294 396 IESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLA--VGVWkSLEEvKKLIRRSNS 473
|
490 500 510
....*....|....*....|....*....|.
gi 49355801 486 KFEPQINVEESEGRYATWKKAVLKSMGWVLT 516
Cdd:PTZ00294 474 TFSPQMSAEERKAIYKEWNKAVERSLKWAKL 504
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-514 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 697.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 13 VGAVDQGTSSTRFLVFNpQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVTN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAG---ISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 93 QRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSisVSNNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIEDGR 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRD--GYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 173 AIFGTVDSWLIWCMTGGingGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSG--VLEG 250
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgfFGGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 251 VPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGrqEPVYYALEGSVAIAGAVVS 330
Cdd:PRK00047 238 VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGID--GKVVYALEGSIFVAGSAIQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 331 WIKNNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDA 410
Cdd:PRK00047 316 WLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 411 MNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAegVSVWSlDPKDL-SSVQMEK-FE 488
Cdd:PRK00047 396 MQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLA--VGFWK-DLDELkEQWKIDRrFE 472
|
490 500
....*....|....*....|....*.
gi 49355801 489 PQINVEESEGRYATWKKAVLKSMGWV 514
Cdd:PRK00047 473 PQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
15-507 |
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: 692.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVTNQR 94
Cdd:cd07786 4 AIDQGTTSSRAILFDHD-GNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAG---IRASDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 95 ETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSISVSnnFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIEDGRAI 174
Cdd:cd07786 80 ETTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEE--MIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 175 FGTVDSWLIWCMTGGingGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSGVL-EGVPI 253
Cdd:cd07786 158 FGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLgAEIPI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 254 SGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGrqEPVYYALEGSVAIAGAVVSWIK 333
Cdd:cd07786 235 AGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLG--GKVTYALEGSIFIAGAAVQWLR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 334 NNLQIIQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDAMNS 413
Cdd:cd07786 313 DGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 414 DCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGvsVWSlDPKDL-SSVQMEK-FEPQI 491
Cdd:cd07786 393 DSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVG--LWK-SLDELaKLWQVDRrFEPSM 469
|
490
....*....|....*.
gi 49355801 492 NVEESEGRYATWKKAV 507
Cdd:cd07786 470 SEEEREALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
15-507 |
5.85e-157 |
|
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: 457.41 E-value: 5.85e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNpQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVTNQR 94
Cdd:cd07793 4 AVDVGTTNIRCHIFD-KKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAG---LTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 95 ETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLSKSI---------SVSNNFVKNKTGLPISTY-----FSAVKLHWLIEN 160
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSLllkalrggsKFLHFLTRNKRFLAASVLkfstaHVSIRLLWILQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 161 VRKVQKAIEDGRAIFGTVDSWLIWCMTGGingGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIY 240
Cdd:cd07793 160 NPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 241 GLV-KSGVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGrQEPVYyALE 319
Cdd:cd07793 237 GSTdPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIG-GEITY-LAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 320 GSVAIAGAVVSWIKNNLQIiQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEA 399
Cdd:cd07793 315 GNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 400 VCFQTREILDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGvsVWSlDPKDL 479
Cdd:cd07793 394 IAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASG--IWK-SKEEL 470
|
490 500 510
....*....|....*....|....*....|
gi 49355801 480 SSVQ--MEKFEPQINVEESEGRYATWKKAV 507
Cdd:cd07793 471 KKLRkiEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-506 |
7.64e-102 |
|
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: 316.00 E-value: 7.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 6 KAVLGplvgaVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNI 85
Cdd:COG1070 1 KYVLG-----IDIGTTSVKAVLFDAD-GEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAG---VDPEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 86 KAIGVTNQRETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFvkNKTGLPISTYFSAVKLHWLIEN----V 161
Cdd:COG1070 72 AAIGVSGQMHGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALY--EITGNPLHPGFTAPKLLWLKENepeiF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 162 RKVQKaiedgraiFGTVDSWLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYG 241
Cdd:COG1070 149 ARIAK--------VLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 242 LVKS------GVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKcVNSEHGLLTTVAYQL-GRqepv 314
Cdd:COG1070 216 TLTAeaaaetGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKP-LPDPEGRVHTFCHAVpGR---- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 315 yYALEGSVAIAGAVVSWIKNNLQIIQSSS--EIEKLAE-VAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFH 391
Cdd:COG1070 291 -WLPMGATNNGGSALRWFRDLFADGELDDyeELNALAAeVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 392 IAFAALEAVCFQTREILDAMNsDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGV-S 470
Cdd:COG1070 370 LARAVLEGVAFALRDGLEALE-EAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLyD 448
|
490 500 510
....*....|....*....|....*....|....*..
gi 49355801 471 VWSLDPKDLSSVQmEKFEPQ-INVEESEGRYATWKKA 506
Cdd:COG1070 449 DLEEAAAAMVRVG-ETIEPDpENVAAYDELYERYREL 484
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-266 |
1.05e-101 |
|
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: 306.57 E-value: 1.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 12 LVGAVDQGTSSTRFLVFNpQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVT 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLG---ISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 92 NQRETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISvsNNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIEdg 171
Cdd:pfam00370 77 NQGHGTVLLDK-NDKPLYNAILWKDRRTAEIVENLKEEGN--NQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 172 raIFGTVDSWLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS------ 245
Cdd:pfam00370 152 --KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPelaamw 224
|
250 260
....*....|....*....|.
gi 49355801 246 GVLEGVPISGCLGDQSAALVG 266
Cdd:pfam00370 225 GLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
15-469 |
3.32e-97 |
|
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: 301.74 E-value: 3.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVTNQR 94
Cdd:cd07779 4 GIDVGTTSTRAIIFDLD-GNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 95 ETTIVWDKfTGEPLYNAVVWLDLRTqstvenlsksisvsnnfvknktglpistyfsavklhwlienvrkvqkaiedgrAI 174
Cdd:cd07779 80 STFVPVDE-DGRPLRPAISWQDKRT-----------------------------------------------------AK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 175 FGTVDSWLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLV------KSGVL 248
Cdd:cd07779 106 FLTVQDYLLYRLTG-----EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLtkeaaeETGLP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 249 EGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQLGRqepvyYALEGSVAIAGAV 328
Cdd:cd07779 181 EGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGK-----WVLEGSINTGGSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 329 VSWIKNNL--------QIIQSSSEI--EKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALE 398
Cdd:cd07779 256 VRWFRDEFgqdevaekELGVSPYELlnEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILE 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49355801 399 AVCFQTREILDAMnSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGV 469
Cdd:cd07779 336 GIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGI 405
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
15-463 |
1.86e-94 |
|
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: 293.32 E-value: 1.86e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNPqTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVTNQR 94
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAG---IDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 95 ETTIVWDKfTGEPLYNAVVWLDlrtqstvenlsksisvsnnfvknktglpistyfsavklhwlienvrkvqkaiedGRAI 174
Cdd:cd00366 80 PGVVLVDA-DGNPLRPAIIWLD------------------------------------------------------RRAK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 175 FGTVDSWLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS------GVL 248
Cdd:cd00366 105 FLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPeaaeetGLP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 249 EGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTgQKCVNSEHGLLTTVAYQLGRqepvyYALEGSVAIAGAV 328
Cdd:cd00366 180 AGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCT-DEPVPPDPRLLNRCHVVPGL-----WLLEGAINTGGAS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 329 VSWIKNNL-QIIQSSSEIEKLAEVAGT----SYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQ 403
Cdd:cd00366 254 LRWFRDEFgEEEDSDAEYEGLDELAAEvppgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYA 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 404 TREILDAMNSdCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAA 463
Cdd:cd00366 334 LRDNLEILEE-LGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-468 |
4.06e-88 |
|
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: 278.70 E-value: 4.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 12 LVGaVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGQqsidiSNIKAIGVT 91
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFDED-GRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 92 NQRETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFvkNKTGLPISTYFSAVKLHWLienvRKVQKAIEDG 171
Cdd:cd07773 75 SQGESGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELY--RITGLPPSPMYSLAKLLWL----REHEPEIFAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 172 RAIFGTVDSWLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS------ 245
Cdd:cd07773 148 AAKWLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPeaaeel 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 246 GVLEGVPIsgCLG--DQSAALVGQLCLQDGQAksTYGTGCFL-LCNTGQKCVNSE---HGLLTTVAYQLGRqepvYYALE 319
Cdd:cd07773 223 GLPAGTPV--VVGghDHLCAALGAGVIEPGDV--LDSTGTAEaLLAVVDEPPLDEmlaEGGLSYGHHVPGG----YYYLA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 320 GSVAiAGAVVSWIKNNLQI--IQSSSEIEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAAL 397
Cdd:cd07773 295 GSLP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAIL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49355801 398 EAVCFQTREILDAMnSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEG 468
Cdd:cd07773 374 EGLAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-506 |
4.20e-85 |
|
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: 272.10 E-value: 4.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 8 VLGplvgaVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKA 87
Cdd:cd07808 2 LLG-----IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAG---ISPSDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 88 IGVTNQRETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISvsnNFVKNKTGLPISTYFSAVKLHWLIENVRKVQKA 167
Cdd:cd07808 73 IGLTGQMHGLVLLDK-NGRPLRPAILWNDQRSAAECEELEARLG---DEILIITGNPPLPGFTLPKLLWLKENEPEIFAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 168 IedgRAIFGTVDsWLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS-- 245
Cdd:cd07808 149 I---RKILLPKD-YLRYRLTG-----ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPea 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 246 ----GVLEGVP-ISGClGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTgQKCVNSEHGLLTTVAYQLGRQepvYYALeG 320
Cdd:cd07808 220 aeelGLPEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVPGK---WYAM-G 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 321 SVAIAGAVVSWIKNNL-QIIQSSSEIEKLAE-VAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALE 398
Cdd:cd07808 294 VTLSAGLSLRWLRDLFgPDRESFDELDAEAAkVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 399 AVCFQTREILDAMNsDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGVSVwSLDPKD 478
Cdd:cd07808 374 GVAFSLRDSLEVLK-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFD-DLEEAA 451
|
490 500 510
....*....|....*....|....*....|
gi 49355801 479 LSSVQMEK-FEPQI-NVEESEGRYATWKKA 506
Cdd:cd07808 452 AACIKIEKtIEPDPeRHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
15-503 |
2.26e-75 |
|
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: 246.70 E-value: 2.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGQQSIDisnikAIGVTNQR 94
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVD-----AIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 95 ETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNnfVKNKTGLPISTYFSAVKLHWLienvRKVQKAIEDGRAI 174
Cdd:cd07770 78 HSLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSE--LYRRTGCPIHPMYPLAKLLWL----KEERPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 175 FGTVDSWLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS------GVL 248
Cdd:cd07770 151 FVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPefaerlGLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 249 EGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTgcfllcnTGQKCVNSEHGLLT----TVAYQLGRQepvYYALEGSVAI 324
Cdd:cd07770 226 AGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPVLDppgrLWCYRLDEN---RWLVGGAINN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 325 AGAVVSWIKNNLQIIQSS-SEIEKLAE-VAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCF 402
Cdd:cd07770 296 GGNVLDWLRDTLLLSGDDyEELDKLAEaVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 403 QTREILDAMnSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGVSVwSLDPKDLSSV 482
Cdd:cd07770 376 NLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLIS-SLEADELVKI 453
|
490 500
....*....|....*....|.
gi 49355801 483 QmEKFEPqiNVEESEgRYATW 503
Cdd:cd07770 454 G-KVVEP--DPENHA-IYAEL 470
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
15-504 |
7.35e-71 |
|
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: 235.11 E-value: 7.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNpQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYEciekACEKLGQQS-IDISNIKAIGVTNQ 93
Cdd:cd07805 4 AIDLGTSGVKAALVD-LDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCR----ATRALLEKSgIDPSDIAAIAFSGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 94 RETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNnFVKNKTGLPISTYFSAVKLHWLIEN----VRKVQKaie 169
Cdd:cd07805 79 MQGVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIAGGLGGIE-GYRLGGGNPPSGKDPLAKILWLKENepeiYAKTHK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 170 dgraIFGTVDsWLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS---- 245
Cdd:cd07805 154 ----FLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPeaaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 246 --GVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAyqlgrQEPVYYALEGSVA 323
Cdd:cd07805 224 elGLPAGTPVVGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLAS-----ADPGRYLLAAEQE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 324 IAGAVVSWIKNNL-----QIIQSSSEIEKLAE-VAGTSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAAL 397
Cdd:cd07805 299 TAGGALEWARDNLggdedLGADDYELLDELAAeAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 398 EAVCFQTREILDAMNSDCGiPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMP-ETTALGVAMAAGAAEGVSVWSLDP 476
Cdd:cd07805 379 EGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGLGLLKSFDEA 457
|
490 500
....*....|....*....|....*....
gi 49355801 477 KDLSSVQmEKFEPQ-INVEESEGRYATWK 504
Cdd:cd07805 458 KALVKVE-KVFEPDpENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-468 |
1.12e-69 |
|
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: 230.88 E-value: 1.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 12 LVGaVDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVT 91
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAG---ISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 92 NQRETTIVWDKFtGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFvkNKTGLPISTYFSAVKLHWLIEN----VRKVQKa 167
Cdd:cd07804 77 GLVPALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGEDRIF--EITGNPLDSQSVGPKLLWIKRNepevFKKTRK- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 168 iedgraiFGTVDSWLIWCMTGginggVHCTDVSNASRTM-LFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLV--- 243
Cdd:cd07804 153 -------FLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVtke 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 244 ---KSGVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGT-GCFLLCntgQKCVNSEHGLLTTVAYqlgrqEPVYYALE 319
Cdd:cd07804 221 aaeETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVV---TDKLPTDPRLWLDYHD-----IPGTYVLN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 320 GSVAIAGAVVSWIKNNL----------QIIQSSSEIEKLAEV--AGtSYGCYFVPAFSGLYAPYWDPSARGIICGLTQFT 387
Cdd:cd07804 293 GGMATSGSLLRWFRDEFageeveaeksGGDSAYDLLDEEAEKipPG-SDGLIVLPYFMGERTPIWDPDARGVIFGLTLSH 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 388 NKFHIAFAALEAVCFQTREILDAMNSDcGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAE 467
Cdd:cd07804 372 TRAHLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGV 450
|
.
gi 49355801 468 G 468
Cdd:cd07804 451 G 451
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-468 |
8.47e-59 |
|
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: 202.01 E-value: 8.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 12 LVGaVDQGTSSTRFLVFNPQTAELLCHHqVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIGVT 91
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSG---VDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 92 NQRETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNnfVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIedg 171
Cdd:cd07802 77 GHGNGLYLVDK-DGKPVRNAILSNDSRAADIVDRWEEDGTLEK--VYPLTGQPLWPGQPVALLRWLKENEPERYDRI--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 172 RAIFGTVDsWLIWCMTGginggVHCTDVSNASrTMLFNIHSLQWDEELCDFFGIP--MTILPRIRSSSEIYGLV------ 243
Cdd:cd07802 151 RTVLFCKD-WIRYRLTG-----EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVtaeaaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 244 KSGVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCfllCNTGqkCVNSEHGLLTTVAYQLGRQEPVYYALEGSVA 323
Cdd:cd07802 224 LTGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEV--VTDEPVVPDSVGSNSLHADPGLYLIVEASPT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 324 IAGaVVSWIKNNLQIIQSSSEI-------EKLAEVAGTSYGCYFVPaFsgLYAPYWDPSARGIICGLTQFTNKFHIAFAA 396
Cdd:cd07802 299 SAS-NLDWFLDTLLGEEKEAGGsdydeldELIAAVPPGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLRAV 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49355801 397 LEAVCFQTREILDAMNSDCgiPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEG 468
Cdd:cd07802 375 YEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
275-466 |
2.15e-50 |
|
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: 171.74 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 275 AKSTYGTGCFLLCnTGQKCVNSEHGLLTTVAyqlGRQEPVYYALEGSVAIAGAVVSWIKNNLQI---IQSSSEIEKLAEV 351
Cdd:pfam02782 1 LAISAGTSSFVLV-ETPEPVLSVHGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreeLRDAGNVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 352 AGTS-----YGCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDAMNSDCGIPLTHLQVDG 426
Cdd:pfam02782 77 AALAavapaGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 49355801 427 GMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAA 466
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
15-466 |
8.98e-48 |
|
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: 171.64 E-value: 8.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNPqTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLgqqsiDISNIKAIGVTNQR 94
Cdd:cd07783 4 GIDLGTSGVRAVVVDE-DGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 95 ETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISvsnnFVKNKTGLPISTYFSAVKLHWLIENVRKVQKAIedgRAI 174
Cdd:cd07783 78 GTLVLVDR-EGEPLRPAIMYNDARAVAEAEELAEAAG----AVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKT---AKF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 175 FGTVDsWLIWCMTgginGGVHCTDVSNASRTmLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS------GVL 248
Cdd:cd07783 150 LHQAD-WLAGRLT----GDRGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAeaaeelGLP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 249 EGVPIsgCLG--DQSAALVGQLCLQDGQAKSTYGTG-CF-LLcnTGQKCVNSEHGLLTtvaYQLGRQepvYYALEGSVAI 324
Cdd:cd07783 224 AGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLkLL--SDKRVPDPGGGVYS---HRHGDG---YWLVGGASNT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 325 AGAVVSWIKNNLQIiqssSEIEKLAEVAGTSyGCYFVP-AFSGLYAPYWDPSARGIICGLTqfTNKFHIAFAALEAVCFQ 403
Cdd:cd07783 294 GGAVLRWFFSDDEL----AELSAQADPPGPS-GLIYYPlPLRGERFPFWDPDARGFLLPRP--HDRAEFLRALLEGIAFI 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49355801 404 TREILDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPfMPETTALGVAMAAGAA 466
Cdd:cd07783 367 ERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIA-EEEEAALGAALLAAAG 428
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
15-468 |
2.39e-46 |
|
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: 168.56 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNPQTAELLCHHQ---------VEIAQEFpkegwveqDPKAILQSVYECIEKACEKLGqqsIDISNI 85
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYReweyytdddYPDAKEF--------DPEELWEKICEAIREALKKAG---ISPEDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 86 KAIGVTNQRETTIVWDKFtGEPLYnAVVWLDLRTQSTVENLSKSISVSnnfVKNKTGLPISTYFSAVKLHWLienvRKVQ 165
Cdd:cd07798 73 SAVSSTSQREGIVFLDKD-GRELY-AGPNIDARGVEEAAEIDDEFGEE---IYTTTGHWPTELFPAARLLWF----KENR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 166 KAIEDGRAIFGTVDSWLIWCMTGGInggvhCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS 245
Cdd:cd07798 144 PEIFERIATVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 246 ------GVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTtvayqlGRQ-EPVYYAL 318
Cdd:cd07798 219 eaarelGLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWT------GCHlVPGKWVL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 319 EGSVAIAGAVVSWIKNNLQIIQSSS--EIEKLA-EVAGTSYGCYfvpAFSGLYAPywDPSARGIICGLTQFT-------- 387
Cdd:cd07798 293 ESNAGVTGLNYQWLKELLYGDPEDSyeVLEEEAsEIPPGANGVL---AFLGPQIF--DARLSGLKNGGFLFPtplsasel 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 388 NKFHIAFAALEAVCFQTREILDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAE 467
Cdd:cd07798 368 TRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGA 447
|
.
gi 49355801 468 G 468
Cdd:cd07798 448 G 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
8-466 |
1.09e-42 |
|
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: 158.10 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 8 VLGplvgaVDQGTSSTRFLVFNPQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKAcekLGQQSIDISNIKA 87
Cdd:cd07809 2 VLG-----IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 88 IGVTNQRETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNnfvKNKTGLPISTYFSAVKLHWLIEN----VRK 163
Cdd:cd07809 74 IGISGQMHGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGKK---CLLVGLNIPARFTASKLLWLKENepehYAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 164 VQKaiedgraiFGTVDSWLIWCMTGGinggvHCTDVSNASRTMLFNIHSLQWDEELCDFF---GIPMTILPRIRSSSEIY 240
Cdd:cd07809 150 IAK--------ILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 241 GLV------KSGVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGT-GCflLCNTGQKCVNSEHGLLTTVAYQLGRQEP 313
Cdd:cd07809 217 GRLtpegaeELGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFCDSTGGMLP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 314 vyyalegSVAIAGAVVSWIKNNLQIIQSS-SEIEKLA-EVAGTSYGCYFVPAFSGLYAPYWdPSARGIICGLTQF-TNKF 390
Cdd:cd07809 295 -------LINTTNCLTAWTELFRELLGVSyEELDELAaQAPPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRA 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49355801 391 HIAFAALEAVCFQTREILDAMnSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAA 466
Cdd:cd07809 367 NLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWG 441
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-468 |
6.89e-36 |
|
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: 139.30 E-value: 6.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 12 LVGaVDQGTSSTRFLVFNPQTAELlCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGQQSidiSNIKAIGVT 91
Cdd:cd24121 2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 92 NQRETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFvkNKTGLPISTYFSAVKLHWLIENvrkVQKAIEDG 171
Cdd:cd24121 77 GQGDGTWLVDE-DGRPVRDAILWLDGRAADIVERWQADGIAEAVF--EITGTGLFPGSQAAQLAWLKEN---EPERLERA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 172 RAIFGTVDsWLIWCMTGGInggvhCTDVSNASRTMlFNIHSLQWDEELCDFFGIP--MTILPRIRSSSEIYGLVKS---- 245
Cdd:cd24121 151 RTALHCKD-WLFYKLTGEI-----ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPeaaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 246 --GVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFllcntgqkcvnseHGLLTTVAYQLGRQEP--VYYALEGS 321
Cdd:cd24121 224 atGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV-------------HEVVVDEPDLEPEGVGytICLGVPGR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 322 VA--------------IAGAVVSWIKNNLQIIQSSS--EIE-KLAEVAGTSYGCYFVPAFS--GLYAPYWDPSARGIICG 382
Cdd:cd24121 291 WLramanmagtpnldwFLRELGEVLKEGAEPAGSDLfqDLEeLAASSPPGAEGVLYHPYLSpaGERAPFVNPNARAQFTG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 383 LTQFTNKFHIAFAALEAVCFQTREILDAMnsdcGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMA 462
Cdd:cd24121 371 LSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMN 446
|
....*.
gi 49355801 463 AGAAEG 468
Cdd:cd24121 447 AAVALG 452
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-463 |
3.23e-35 |
|
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: 137.35 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNPQTAELL----CHHQVEIAQEFPkeGWVEQDPKAILQSVYECIEKACEKLGqqsidiSNIKAIGV 90
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILesvsRPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 91 TNQRETTIVWDKfTGEPLYNAVVWLDLRtqSTVENLSKSISVSNNFvKNKTGLPISTYFSAVKLHWLIENvrkvqKAIED 170
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLITWQDQR--CSEEFLGGLSTYGEEL-LPKSGMRLKPGYGLATLFWLLRN-----GPLPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 171 GRAIFGTVDSWLIWCMTGGINggvHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSGVLEG 250
Cdd:cd07777 147 KADRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 251 VPISGCLGDQSAALVGQLCLQDGQAKSTYGTGcfllcntGQKCVNSEHGLLTTvAYQL-----------------GRqep 313
Cdd:cd07777 224 IPVYVALGDNQASVLGSGLNEENDAVLNIGTG-------AQLSFLTPKFELSG-SVEIrpffdgryllvaaslpgGR--- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 314 vyyALEgsvAIAGAVVSWIKnNLQIIQSSSEI-EKLAEVAGTSYGC--YFVPAFSGlyaPYWDPSARGIICGLTQftNKF 390
Cdd:cd07777 293 ---ALA---VLVDFLREWLR-ELGGSLSDDEIwEKLDELAESEESSdlSVDPTFFG---ERHDPEGRGSITNIGE--SNF 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49355801 391 ---HIAFAALEAVCfqtREILDAMNSDC--GIPLTHLQVDGGM-TANRVLMQLQADILCIPVMKPFMPETTALGVAMAA 463
Cdd:cd07777 361 tlgNLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
8-506 |
6.30e-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: 137.67 E-value: 6.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 8 VLGplvgaVDQGTSSTRFLVFNPQTAELL--CHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNI 85
Cdd:cd07781 2 VIG-----IDFGTQSVRAGLVDLADGEELasAVVPYPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAG---VDPEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 86 KAIGVTNQRETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFVKNKTGLPIS--TYFSavKLHWLIENVRK 163
Cdd:cd07781 74 VGIGVDTTSSTVVPVDE-DGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSseWMWP--KALWLKRNAPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 164 VQKAIedgRAIFGTVDsWLIWCMTGGINGGVhctdvSNASRTMLFNIHSLQWDEELC-----DFFGIPMTILPRIRSSSE 238
Cdd:cd07781 151 VYDAA---YTIVEACD-WINARLTGRWVRSR-----CAAGHKWMYNEWGGGPPREFLaaldpGLLKLREKLPGEVVPVGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 239 IYGLVKS------GVLEGVPISGCLGDQSAALVGQLCLQDGQ-AKSTyGT-GCFLLCNTGQKCVnseHGLLTTVayqlgr 310
Cdd:cd07781 222 PAGTLTAeaaerlGLPAGIPVAQGGIDAHMGAIGAGVVEPGTlALIM-GTsTCHLMVSPKPVDI---PGICGPV------ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 311 QEPV---YYALEGSVAIAGAVVSWIKNNLQIIQSSSE-------IEKLAEVAGTSYGCYFVPAFSGLYAPYWDPSARGII 380
Cdd:cd07781 292 PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPPAEERGdsiyallSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 381 CGLTQFTNKFHIAFAALEAVCFQTREILDAMnSDCGIPLTHLQVDGGMTA-NRVLMQLQADILCIPVMKPFMPETTALGV 459
Cdd:cd07781 372 VGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAEkNPLWMQIYADVLGRPIKVPKSDQAPALGA 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 49355801 460 AMAAGAAEGVSvwsldpKDLSS-----VQMEK-FEP-QINVEESEGRYATWKKA 506
Cdd:cd07781 451 AILAAVAAGVY------ADIEEaadamVRVDRvYEPdPENHAVYEELYALYKEL 498
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-469 |
1.80e-32 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 130.15 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 17 DQGTSSTRFLVFNPQTAELLCHHQ---VEIAQEFPKegWVEQDPKAILQSVYECIEKACEKLGQQsidisNIKAIGVTNQ 93
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTpnaSDIAAENSD--WHQWSLDAILQRFADCCRQINSELTEC-----HIRGITVTTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 94 RETTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFVKNKTG-LPISTYFsavKLHWLIENvrKVQkaiedgr 172
Cdd:PRK10331 81 GVDGALVDK-QGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGaFSFNTLY---KLVWLKEN--HPQ------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 173 aIFGTVDSWLIwcMTGGIN---GGVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKS---- 245
Cdd:PRK10331 148 -LLEQAHAWLF--ISSLINhrlTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPsaaa 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 246 --GVLEGVPISGCLGDQSAALVGQLCLQDgQAKSTYGTGCFLLCNTGQkcVNS-----EHGLLTTVAYQLGRQEPvyyal 318
Cdd:PRK10331 225 llGLPVGIPVISAGHDTQFALFGSGAGQN-QPVLSSGTWEILMVRSAQ--VDTsllsqYAGSTCELDSQSGLYNP----- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 319 eGSVAIAGAVVSWIKnnlQIIQSSSE-----IEKLAEVAGTSYGCYFVPAFSGlyapywdpSARGIICGLTQFTNKFHIA 393
Cdd:PRK10331 297 -GMQWLASGVLEWVR---KLFWTAETpyqtmIEEARAIPPGADGVKMQCDLLA--------CQNAGWQGVTLNTTRGHFY 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49355801 394 FAALEAVCFQTREILDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGV 469
Cdd:PRK10331 365 RAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGE 440
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
15-469 |
1.06e-29 |
|
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: 122.44 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNpqtaelLCHHQVEIAQ------EFPK-EGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKA 87
Cdd:cd07775 4 ALDAGTGSGRAVIFD------LEGNQIAVAQrewrhkEVPDvPGSMDFDTEKNWKLICECIREALKKAG---IAPKSIAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 88 IGVTNQRETTIVWDKfTGEPLYnAVVWLDLRTQSTVENLSKSISVSNNFVKNKTGlpiSTY-FSAV-KLHWLIENVRKVQ 165
Cdd:cd07775 75 ISTTSMREGIVLYDN-EGEEIW-ACANVDARAAEEVSELKELYNTLEEEVYRISG---QTFaLGAIpRLLWLKNNRPEIY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 166 KAIedgrAIFGTVDSWLIWCMTGGInggvhCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVK- 244
Cdd:cd07775 150 RKA----AKITMLSDWIAYKLSGEL-----AVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTk 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 245 -----SGVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTGCFLLCNTGQKCVNSEHGLLTTVAYQlgrqePVYYALE 319
Cdd:cd07775 221 eaaeeTGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVI-----PDMWQAE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 320 GSVAIAGAVVSWIKNNLqiiqsSSEIEKLAEVAGTS-Y------------GCY-FVPAFSGL--YApYWDPSARGIIcGL 383
Cdd:cd07775 296 GISFFPGLVMRWFRDAF-----CAEEKEIAERLGIDaYdlleemakdvppGSYgIMPIFSDVmnYK-NWRHAAPSFL-NL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 384 TQFTNKFHIA--FAAL-EAVCFQTREILDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVA 460
Cdd:cd07775 369 DIDPEKCNKAtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAA 448
|
....*....
gi 49355801 461 MAAGAAEGV 469
Cdd:cd07775 449 IAAGVGAGI 457
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
15-473 |
3.12e-24 |
|
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: 106.47 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNpQTAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNIKAIG----- 89
Cdd:cd07782 4 GVDVGTGSARAGLFD-LDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAG---VDPEQVKGIGfdatc 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 90 ----VTNQRETTIVWDkfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFVKNKtglpISTYFSAVKLHWLIENVRKVQ 165
Cdd:cd07782 80 slvvLDAEGKPVSVSP--SGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGK----ISPEMEPPKLLWLKENLPETW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 166 KAIedGRAiFGTVDsWLIWCMTGGINGGVhCTDVSNasrtMLFNIHSL---QWDEEL----------CDFFG-IPMTILP 231
Cdd:cd07782 154 AKA--GHF-FDLPD-FLTWKATGSLTRSL-CSLVCK----WTYLAHEGsegGWDDDFfkeigledlvEDNFAkIGSVVLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 232 RIRSSSEiyGLVKS-----GVLEGVPISGCLGDQSAALVGQLCLQDGQAKSTYGTG---CFLLCNTGqkcvnSEHGLLTt 303
Cdd:cd07782 225 PGEPVGG--GLTAEaakelGLPEGTPVGVSLIDAHAGGLGTLGADVGGLPCEADPLtrrLALICGTS-----SCHMAVS- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 304 vayqlgrQEPV--------YY-AL-------EGSVAIAGAVVSWIknnlqiIQS---SSEIEKLAEVAGTSY-------- 356
Cdd:cd07782 297 -------PEPVfvpgvwgpYYsAMlpglwlnEGGQSATGALLDHI------IEThpaYPELKEEAKAAGKSIyeylnerl 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 357 ----------------GCYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIA---FAALEAVCFQTREILDAMNSdCGI 417
Cdd:cd07782 364 eqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLAllyLATLQALAYGTRHIIEAMNA-AGH 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 49355801 418 PLTHLQVDGGMTANRVLMQLQADILCIPVMKPFMPETTALGVAMAAGAAEGV--SVWS 473
Cdd:cd07782 443 KIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDfpSLWD 500
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
16-441 |
6.05e-23 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 101.97 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 16 VDQGTSSTRFLVFNPQtAELLCHHQVEIAQEFPKEGWVEQDPKAILQSVyeciEKACEKLGQQSiDISNIKAIGVTNQRE 95
Cdd:PRK15027 5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQWWQAT----DRAMKALGDQH-SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 96 TTIVWDKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSnnfvKNKTGLPISTYFSAVKLHWlienvrkVQKAIEDgraIF 175
Cdd:PRK15027 79 GATLLDA-QQRVLRPAILWNDGRCAQECALLEARVPQS----RVITGNLMMPGFTAPKLLW-------VQRHEPE---IF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 176 GTVDS------WLIWCMTGginggVHCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSGVLE 249
Cdd:PRK15027 144 RQIDKvllpkdYLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 250 -----GVPISGCLGDQSAALVGQLCLQDGQAKSTYGT-GCFLLCNTG-----QKCVNSE-HGLlttvayqlgrqePVYYA 317
Cdd:PRK15027 219 awgmaTVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSFcHAL------------PQRWH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 318 LEGSVAIAGAVVSWIKnNLQIIQSSSEIEKLAEVAGTSYG-CYFVPAFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAA 396
Cdd:PRK15027 287 LMSVMLSAASCLDWAA-KLTGLSNVPALIAAAQQADESAEpVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAV 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 49355801 397 LEAVCFQTREILDAMNsDCGIPLTHLQVDGGMTANRVLMQLQADI 441
Cdd:PRK15027 366 LEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
16-492 |
2.32e-22 |
|
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: 100.39 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 16 VDQGTSSTRFLVFNPQTAELLCHHQVEIAQ-EFPKEGWVEQDPKAILQSVYECIEKAcekLGQQSIDISNIKAIGVTN-- 92
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDAtc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 93 -----QRETTIVWDKFTGEPLYNAVVWLDLRTQSTVENLsksisvsnNFVKNKTGLP-----ISTYFSAVKLHWLIENVR 162
Cdd:cd07768 82 slaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWI--------NMQCPQQLLDylggkISPEMGVPKLKYFLDEYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 163 KVQKAIEDgraIFGTVDsWLIWCMTGGINGGVhCTDVSNASrtmlFNIHSLQWDEE------LCDFFGIPMTILPRIRSS 236
Cdd:cd07768 154 HLRDKHFH---IFDLHD-YIAYELTRLYEWNI-CGLLGKEN----LDGEESGWSSSffknidPRLEHLTTTKNLPSNVPI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 237 SEIYGLV------KSGVLEGVPISGCLGDQSAALVGQlclqdgqAKSTYGTGCFLLCNTgqkcvNSEHGLLTTVAYQL-G 309
Cdd:cd07768 225 GTTSGVAlpemaeKMGLHPGTAVVVSCIDAHASWFAV-------ASPHLETSLFMIAGT-----SSCHMYGTTISDRIpG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 310 RQEPVYYAL-------EGSVAIAGAVVSWI-------KNNLQIIQSSSEI-----EKLAEVAGT---SYGCYFVPAFSGL 367
Cdd:cd07768 293 VWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleQTIRQIEKNnglSIHILTLDMFFGN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 368 YAPYWDPSARGIICGLTQFTNKFHIAF---AALEAVCFQTREILDAMNSDcGIPLTHLQVDGGMTANRVLMQLQADILCI 444
Cdd:cd07768 373 RSEFADPRLKGSFIGESLDTSMLNLTYkyiAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 49355801 445 PVMKPFMPETTALGVAMAAGAAEGVSVW--SLDPKDLS-SVQMEKFEPQIN 492
Cdd:cd07768 452 AIIKPKENMMGILGAAVLAKVAAGKKQLadSITEADISnDRKSETFEPLAY 502
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
15-462 |
1.16e-17 |
|
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: 85.66 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLV--FNPQTAELlchhqVEIAQeFPKEGwVEQDPK------AILQSVYECIEKACEKLGQqsidisnIK 86
Cdd:cd07771 4 AVDLGASSGRVILgsLDGGKLEL-----EEIHR-FPNRP-VEINGHlywdidRLFDEIKEGLKKAAEQGGD-------ID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 87 AIGVTnqretTivW-------DKfTGEPLYNAVVWLDLRTQSTVENLSKSISVSNNFvkNKTGLPISTYFSAVKLHWLIE 159
Cdd:cd07771 70 SIGID-----T--WgvdfgllDK-NGELLGNPVHYRDPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYALKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 160 NvrkvqkaiedGRAIFGTVDSWLI------WCMTGGInggvhCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRI 233
Cdd:cd07771 140 E----------GPELLERADKLLMlpdllnYLLTGEK-----VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 234 RSSSEIYGLVKSGVLE-----GVP-ISGCLGDQSAALVGQLCLQDGQAkstygtgcFLLCNT----GqkcVNSEHGLLTT 303
Cdd:cd07771 205 VPPGTVLGTLKPEVAEelglkGIPvIAVASHDTASAVAAVPAEDEDAA--------FISSGTwsliG---VELDEPVITE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 304 VAYQLGrqepvyYALEGSVA--------IAGavvswiknnLQIIQ-------------SSSEIEKLAEVAgTSYGCYFVP 362
Cdd:cd07771 274 EAFEAG------FTNEGGADgtirllknITG---------LWLLQecrreweeegkdySYDELVALAEEA-PPFGAFIDP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 363 AFSGLYAPywdPSARGIICGLTQFTNKF------HIAFAALEAVCFQTREILDAMNSDCGIPLTHLQVDGGMTANRVLMQ 436
Cdd:cd07771 338 DDPRFLNP---GDMPEAIRAYCRETGQPvpespgEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQ 414
|
490 500
....*....|....*....|....*.
gi 49355801 437 LQADILCIPVMKpFMPETTALGVAMA 462
Cdd:cd07771 415 LTADATGLPVIA-GPVEATAIGNLLV 439
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-518 |
5.79e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 68.11 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 15 AVDQGTSSTRFLVFNPQTAellchhQVEIAQE---------FPkeGWVEQDPKAILQSVYECIEKACEKLGqqsIDISNI 85
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGN------QIAVGQAewrhlavpdVP--GSMEFDLEKNWQLACQCIRQALQKAG---IPASDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 86 KAIGVTNQRETTIVWDKfTGEPLYnAVVWLDLRTQSTVENLSKSISVSNNFVKNKTGlpiSTY-FSAV-KLHWLIENVRK 163
Cdd:PRK10939 76 AAVSATSMREGIVLYDR-NGTEIW-ACANVDARASREVSELKELHNNFEEEVYRCSG---QTLaLGALpRLLWLAHHRPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 164 VQKAIedgrAIFGTVDSWLIWCMTGGInggvhCTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLV 243
Cdd:PRK10939 151 IYRQA----HTITMISDWIAYMLSGEL-----AVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 244 ------KSGVLEGVPISGCLGD-QSAALvGQLCLQDGQAKSTYGTgcFLlcntgQKCVNSEHGllTTVAYQLGRQEPvyY 316
Cdd:PRK10939 222 takaaaETGLRAGTPVVMGGGDvQLGCL-GLGVVRPGQTAVLGGT--FW-----QQVVNLPAP--VTDPNMNIRINP--H 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 317 ALEGSV---AIA---GAVVSWIKN----NLQIIQSSSEI-------EKLAEVAGTSYGcyFVPAFSGLY--------APY 371
Cdd:PRK10939 290 VIPGMVqaeSISfftGLTMRWFRDafcaEEKLLAERLGIdayslleEMASRVPVGSHG--IIPIFSDVMrfkswyhaAPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 372 W-----DPSargiICgltqftNKFHIAFAALEAVCFQTREILDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPV 446
Cdd:PRK10939 368 FinlsiDPE----KC------NKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49355801 447 MKPFMPETTALGVAMAAGAaeGVSVW-SLDPKDLSSVQMEK-FEPQI-NVEESEGRYATWKKAVLKSMGWV---LTQS 518
Cdd:PRK10939 438 KVPVVKEATALGCAIAAGV--GAGIYsSLAETGERLVRWERtFEPNPeNHELYQEAKEKWQAVYADQLGLVdhgLTTS 513
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
364-469 |
8.58e-11 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 64.48 E-value: 8.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 364 FSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDAMNsDCGIPLTHLQVDGGM-TANRVLMQLQADIL 442
Cdd:PRK04123 385 FNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFE-DQGVPVEEVIAAGGIaRKNPVLMQIYADVL 463
|
90 100
....*....|....*....|....*..
gi 49355801 443 CIPVMKPFMPETTALGVAMAAGAAEGV 469
Cdd:PRK04123 464 NRPIQVVASDQCPALGAAIFAAVAAGA 490
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
16-453 |
7.71e-05 |
|
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: 45.47 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 16 VDQGTSSTRFLVFNPQTaELLCHHQVEIA-QEFPKEGW-VEQDPKAILQSVYECIEKACEKLGQQSIDISNIKA---IGV 90
Cdd:cd07778 5 IDVGSTSVRIGIFDYHG-TLLATSERPISyKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSAtcsMVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 91 TNQRETTIVWDKFTGEPLY-----NAVVWLDLRTQSTVENLsksisvsNNFVKNKTGLPISTYF----SAVKLHWLIENV 161
Cdd:cd07778 84 MQRDSDTSYLVPYNVIHEKsnpdqDIIFWMDHRASEETQWL-------NNILPDDILDYLGGGFipemAIPKLKYLIDLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 162 RKVQkaiEDGRAIFGTVD--SWLIWCMTG---------------GINGGVHCTDVSNASRTMLFNIHSLQWDEELCD--- 221
Cdd:cd07778 157 KEDT---FKKLEVFDLHDwiSYMLATNLGhsnivpvnappsigiGIDGSLKGWSKDFYSKLKISTKVCNVGNTFKEAppl 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 222 -FFGIPM-TILPRIRSSSEIYGlvksgvlEGVPISGCLgDQSAALVGQLC---LQDGQAKSTYGTG-CFLLCNTgqkcvN 295
Cdd:cd07778 234 pYAGIPIgKVNVILASYLGIDK-------STVVGHGCI-DCYAGWFSTFAaakTLDTTLFMVAGTStCFLYATS-----S 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 296 SEHGLLTTV---AYQLGRQEPVYyalEGSVAIAG-----------AVVSWIKNNLQIIQS-SSEIEKLAEVAGTS----Y 356
Cdd:cd07778 301 SQVGPIPGIwgpFDQLLKNYSVY---EGGQSATGklieklfnshpAIIELLKSDANFFETvEEKIDKYERLLGQSihylT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 357 GCYFvpaFSGLYA----PYWDPSARGIICGLTQFTNKFHIAF---AALEAVCFQTREILDAMNSDCgIPLTHLQVDGGMT 429
Cdd:cd07778 378 RHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKEK-IIIQKVVISGSQA 453
|
490 500
....*....|....*....|....
gi 49355801 430 ANRVLMQLQADILCIPVMKPFMPE 453
Cdd:cd07778 454 KNARLLQLLSTVLSKIHIIVPLSD 477
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
363-463 |
3.51e-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: 43.02 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 363 AFSGLYAPYWDPSARGIICGLTQFTNKFHIAFAALEAVCFQTREILDAMNSDCGipltHLQVDGGMTANRVLMQLQADIL 442
Cdd:cd07772 327 ALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYALDLLGSGVG----RIIVEGGFAKNPVFLRLLAALR 402
|
90 100
....*....|....*....|..
gi 49355801 443 -CIPVMKPFMPETTALGVAMAA 463
Cdd:cd07772 403 pDQPVYLSDDSEGTALGAALLA 424
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
186-447 |
1.54e-03 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 41.24 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 186 MTGGINggvhcTDVSNASRTMLFNIHSLQWDEELCDFFGIPMTILPRIRSSSEIYGLVKSGVLEGVP------------- 252
Cdd:PRK10640 150 LTGKMN-----WEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQGNEIPvvavashdtasav 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 253 ISGCLGDQSAALV--GQLCLQDGQAKSTYGTGCFLLCNtgqkcVNSEHGLlttvayqlgrqEPVYYALEGsvaIAGAvvs 330
Cdd:PRK10640 225 IASPLNDSDAAYLssGTWSLMGFESQTPFTNDTALAAN-----ITNEGGA-----------EGRYRVLKN---IMGL--- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 331 WIKNNLQIIQSSSEIEKLAEVAGTSYGCYFVpafsglyapywdpsargIICGLTQFTNKFHIAfAALEAVCFQT------ 404
Cdd:PRK10640 283 WLLQRVLQERQITDLPALIAATAALPACRFL-----------------INPNDDRFINPPSMC-SEIQAACRETaqpvpe 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49355801 405 -----------------REILDAMNSDCGIPLTHLQVDGGMTANRVLMQLQADILCIPVM 447
Cdd:PRK10640 345 sdaelarcifdslallyADVLHELAQLRGEPFSQLHIVGGGCQNALLNQLCADACGIRVI 404
|
|
| |
