|
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: 998.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 91 SNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEE 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 171 NRALFGTIDSWLIWSLTGGIHGGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGALEG 250
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASGPLAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 251 VPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIR 330
Cdd:cd07792 240 VPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 331 WLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDA 410
Cdd:cd07792 320 WLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 411 MNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQ 490
Cdd:cd07792 400 MNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQ 479
|
490 500
....*....|....*....|
gi 6680139 491 INAEESEIRYSTWKKAVMKS 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: 830.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 11 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 91 SNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNnnFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEE 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGE--FIREKTGLPLDPYFSATKLRWLLDNVPGVREAAER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 171 NRALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGAL-E 249
Cdd:TIGR01311 155 GELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLgA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 250 GVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYyALEGSVAIAGAVI 329
Cdd:TIGR01311 232 EIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPVY-ALEGSVFVAGAAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 330 RWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILD 409
Cdd:TIGR01311 311 QWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 410 AMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLSAVTmERFEP 489
Cdd:TIGR01311 391 AMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVE-KTFEP 469
|
490 500
....*....|....*....|....
gi 6680139 490 QINAEESEIRYSTWKKAVMKSIGW 513
Cdd:TIGR01311 470 EMDEEEREARYAGWKEAVKRSLGW 493
|
|
| 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: 759.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAG---ISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 93 QRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENR 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK--GLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 173 ALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGAL-EGV 251
Cdd:cd07769 156 LLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLgAGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 252 PISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLgrDKPVYYALEGSVAIAGAVIRW 331
Cdd:cd07769 233 PIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQI--GGKVTYALEGSIFIAGAAIQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 332 LRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAM 411
Cdd:cd07769 311 LRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 412 NRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgVWSLEPEDLSAVTMER-FEPQ 490
Cdd:cd07769 391 EKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalgaayl--aglavgFWKDLDELASLWQVDKrFEPS 468
|
490
....*....|....*..
gi 6680139 491 INAEESEIRYSTWKKAV 507
Cdd:cd07769 469 MDEEERERLYRGWKKAV 485
|
|
| 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: 757.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 93 QRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENR 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKAD--GLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 173 ALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGAL-EGV 251
Cdd:COG0554 159 LLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGETDPDLFgAEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 252 PISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRW 331
Cdd:COG0554 236 PIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLG-GKVTY-ALEGSIFVAGAAVQW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 332 LRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAM 411
Cdd:COG0554 314 LRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 412 NRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgVWSlEPEDLSAV--TMERFEP 489
Cdd:COG0554 394 EADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalgaayl--aglavgFWK-SLEELAALwkVDRRFEP 470
|
490 500
....*....|....*....|....*
gi 6680139 490 QINAEESEIRYSTWKKAVMKSIGWV 514
Cdd:COG0554 471 QMDEEERERLYAGWKKAVERTLGWA 495
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-514 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 724.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 11 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISnIKAIGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 91 SNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKsKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEE 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQK-ITGLPISTYFSAFKIRWMLENVPAVKDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 171 NRALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMK---AGA 247
Cdd:PTZ00294 159 GTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISgeaVPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 248 LEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYYALEGSVAIAGA 327
Cdd:PTZ00294 236 LEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAVAGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 328 VIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREI 407
Cdd:PTZ00294 316 GVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 408 LDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVW-SLEP-EDLSAVTME 485
Cdd:PTZ00294 396 IESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT--ALGAALLAGLAVGVWkSLEEvKKLIRRSNS 473
|
490 500
....*....|....*....|....*....
gi 6680139 486 RFEPQINAEESEIRYSTWKKAVMKSIGWV 514
Cdd:PTZ00294 474 TFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-514 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 713.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQ--LNIDiSNIKAIG 89
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAkgHNVD-SGLKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 90 VSNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVE 169
Cdd:PLN02295 79 ITNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 170 ENRALFGTIDSWLIWSLTGGIHGGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAG-AL 248
Cdd:PLN02295 159 SGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGwPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 249 EGVPISGCLGDQSAALVGQMCfQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYYALEGSVAIAGAV 328
Cdd:PLN02295 239 AGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 329 IRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIL 408
Cdd:PLN02295 318 VQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 409 DAMNRDCGIPLSH-----LQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVWSlePEDLSAVT 483
Cdd:PLN02295 398 DAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETT--ALGAAYAAGLAVGLWT--EEEIFASE 473
|
490 500 510
....*....|....*....|....*....|....*
gi 6680139 484 MER----FEPQINAEESEIRYSTWKKAVMKSIGWV 514
Cdd:PLN02295 474 KWKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-514 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 698.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 13 VGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 93 QRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENR 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRD--GYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 173 ALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAG--ALEG 250
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYgfFGGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 251 VPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGrDKPVYyALEGSVAIAGAVIR 330
Cdd:PRK00047 238 VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGID-GKVVY-ALEGSIFVAGSAIQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 331 WLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDA 410
Cdd:PRK00047 316 WLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 411 MNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgvwSL--------------EP 476
Cdd:PRK00047 396 MQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT-----------------ALgaaylaglavgfwkDL 458
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 6680139 477 EDLSAVTME--RFEPQINAEESEIRYSTWKKAVMKSIGWV 514
Cdd:PRK00047 459 DELKEQWKIdrRFEPQMDEEEREKLYAGWKKAVKRTLAWA 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: 693.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07786 4 AIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 95 ETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENRAL 174
Cdd:cd07786 80 ETTVVWDRETGKPVYNAIVWQDRRTADICEELKAE--GHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 175 FGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGAL-EGVPI 253
Cdd:cd07786 158 FGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLgAEIPI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 254 SGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGrdKPVYYALEGSVAIAGAVIRWLR 333
Cdd:cd07786 235 AGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLG--GKVTYALEGSIFIAGAAVQWLR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 334 DNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNR 413
Cdd:cd07786 313 DGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 414 DCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL--------GAAMAAGAAEGVGVWSLEpedlsavtmE 485
Cdd:cd07786 393 DSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALgaaylaglAVGLWKSLDELAKLWQVD---------R 463
|
490 500
....*....|....*....|..
gi 6680139 486 RFEPQINAEESEIRYSTWKKAV 507
Cdd:cd07786 464 RFEPSMSEEEREALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
15-507 |
9.33e-152 |
|
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: 443.16 E-value: 9.33e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07793 4 AVDVGTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAG---LTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 95 ETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSK---------------RIPGNNNFVKSKTgLPLSTYFSAVKLRWLLD 159
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFITWQDLRAAELCESWNRslllkalrggskflhFLTRNKRFLAASV-LKFSTAHVSIRLLWILQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 160 NVKKVQEAVEENRALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEI 239
Cdd:cd07793 159 NNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 240 YGLMKAGAL-EGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGrDKPVYyAL 318
Cdd:cd07793 236 FGSTDPSIFgAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIG-GEITY-LA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 319 EGSVAIAGAVIRWLRDNLGIiKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALE 398
Cdd:cd07793 314 EGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAILE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 399 AVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVWSlEPED 478
Cdd:cd07793 393 SIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMS--ALGAAFLAGLASGIWK-SKEE 469
|
490 500 510
....*....|....*....|....*....|.
gi 6680139 479 LSAV--TMERFEPQINAEESEIRYSTWKKAV 507
Cdd:cd07793 470 LKKLrkIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-266 |
1.34e-109 |
|
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: 326.22 E-value: 1.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVS 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLS---QLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 92 NQRETTVVWDKVTgEPLYNAVVWLDLRTQSTVENLSKriPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEen 171
Cdd:pfam00370 77 NQGHGTVLLDKND-KPLYNAILWKDRRTAEIVENLKE--EGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 172 raLFGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKA------ 245
Cdd:pfam00370 152 --KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPelaamw 224
|
250 260
....*....|....*....|.
gi 6680139 246 GALEGVPISGCLGDQSAALVG 266
Cdd:pfam00370 225 GLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-455 |
3.03e-98 |
|
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: 305.99 E-value: 3.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 6 KAVLGplvgaVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNI 85
Cdd:COG1070 1 KYVLG-----IDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAG---VDPEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 86 KAIGVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNvkkvQ 165
Cdd:COG1070 72 AAIGVSGQMHGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALY--EITGNPLHPGFTAPKLLWLKEN----E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 166 EAVEENRALFGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKA 245
Cdd:COG1070 145 PEIFARIAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 246 ------GALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKcVFSEHGLLTTVAYKL-GRdkpvyYAL 318
Cdd:COG1070 220 eaaaetGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKP-LPDPEGRVHTFCHAVpGR-----WLP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 319 EGSVAIAGAVIRWLRDNLGIIKSS--EEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFA 395
Cdd:COG1070 294 MGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARA 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 396 ALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:COG1070 374 VLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGG 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
15-455 |
2.40e-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: 292.16 E-value: 2.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAG---IDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 95 ETTVVWDKvTGEPLYNAVVWLDlrtqstvenlskripgnnnfvksktglplstyfsavklrwlldnvkkvqeaveeNRAL 174
Cdd:cd00366 80 PGVVLVDA-DGNPLRPAIIWLD------------------------------------------------------RRAK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 175 FGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYG-LMKAGAL----- 248
Cdd:cd00366 105 FLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGrVTPEAAEetglp 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 249 EGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGhKCVFSEHGLLTTVAYKLGRdkpvyYALEGSVAIAGAV 328
Cdd:cd00366 180 AGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDPRLLNRCHVVPGL-----WLLEGAINTGGAS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 329 IRWLRDNLGIIKSSEE----IEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQ 403
Cdd:cd00366 254 LRWFRDEFGEEEDSDAeyegLDELAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYA 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6680139 404 TREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:cd00366 334 LRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
15-455 |
4.02e-93 |
|
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: 290.57 E-value: 4.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07779 4 GIDVGTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 95 ETTVVWDKvTGEPLYNAVVWLDLRTqstvenlskripgnnnfvksktglplstyfsavklrwlldnvkkvqeaveenrAL 174
Cdd:cd07779 80 STFVPVDE-DGRPLRPAISWQDKRT-----------------------------------------------------AK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 175 FGTIDSWLIWSLTggihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYG-LMKAGAL----- 248
Cdd:cd07779 106 FLTVQDYLLYRLT-----GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGtLTKEAAEetglp 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 249 EGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTgHKCVFSEHGLLTTVAYKLgrdkPVYYALEGSVAIAGAV 328
Cdd:cd07779 181 EGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAV----PGKWVLEGSINTGGSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 329 IRWLRDNLG--------IIKSSEE-IEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALE 398
Cdd:cd07779 256 VRWFRDEFGqdevaekeLGVSPYElLNEEAAKSPPgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILE 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 6680139 399 AVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:cd07779 336 GIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEAT 391
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-455 |
3.55e-84 |
|
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: 267.92 E-value: 3.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 12 LVGaVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQlnidiSNIKAIGVS 91
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 92 NQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVeen 171
Cdd:cd07773 75 SQGESGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELY--RITGLPPSPMYSLAKLLWLREHEPEIFAKA--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 172 rALFGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGALE-- 249
Cdd:cd07773 149 -AKWLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEel 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 250 ----GVPIsgCLG--DQSAALVGQMCFQDGQAKNTYGTG-CFLLC-NTGHKCVFSEHGLLTTVAYKLGRdkpvYYALEGS 321
Cdd:cd07773 223 glpaGTPV--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLDEMLAEGGLSYGHHVPGG----YYYLAGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 322 VAiAGAVIRWLRDNLGI--IKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEA 399
Cdd:cd07773 297 LP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 6680139 400 VCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:cd07773 376 LAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-455 |
1.93e-81 |
|
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: 261.70 E-value: 1.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 8 VLGplvgaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07808 2 LLG-----IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 88 IGVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPgnnNFVKSKTGLPLSTYFSAVKLRWLL----DNVKK 163
Cdd:cd07808 73 IGLTGQMHGLVLLDK-NGRPLRPAILWNDQRSAAECEELEARLG---DEILIITGNPPLPGFTLPKLLWLKenepEIFAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 164 VqeaveenRALFGTIDsWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLM 243
Cdd:cd07808 149 I-------RKILLPKD-YLRYRLTG-----ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 244 KAGA------LEGVP-ISGClGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTgHKCVFSEHGLLTTVAYKLGrdkPVYY 316
Cdd:cd07808 216 TPEAaeelglPEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVP---GKWY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 317 ALeGSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAF 394
Cdd:cd07808 291 AM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLAR 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680139 395 AALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:cd07808 370 AVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGS 429
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
15-455 |
3.16e-77 |
|
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: 250.55 E-value: 3.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDisnikAIGVSNQR 94
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVD-----AIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 95 ETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNnfVKSKTGLPLSTYFSAVKLRWLldnvKKVQEAVEENRAL 174
Cdd:cd07770 78 HSLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSE--LYRRTGCPIHPMYPLAKLLWL----KEERPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 175 FGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKA------GAL 248
Cdd:cd07770 151 FVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPefaerlGLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 249 EGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTgcfllcnTGHKCVFSEHGLLT----TVAYKLGRDKPVyyaLEGSVAI 324
Cdd:cd07770 226 AGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPVLDppgrLWCYRLDENRWL---VGGAINN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 325 AGAVIRWLRDNLGIIKSS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCF 402
Cdd:cd07770 296 GGNVLDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAF 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 6680139 403 QTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:cd07770 376 NLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEAS 427
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-450 |
1.75e-71 |
|
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: 234.73 E-value: 1.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 12 LVGaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAG---ISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 92 NQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNvkkvQEAVEEN 171
Cdd:cd07804 77 GLVPALVPVDE-NGKPLRPAILYGDRRATEEIEWLNENIGEDRIF--EITGNPLDSQSVGPKLLWIKRN----EPEVFKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 172 RALFGTIDSWLIWSLTGgihggVHCTDVTNASRTM-LFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGA--- 247
Cdd:cd07804 150 TRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAaee 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 248 ---LEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCFLLCntgHKCVFSEHGLLTTVAyklgrDKPVYYALEGSVA 323
Cdd:cd07804 225 tglAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVV---TDKLPTDPRLWLDYH-----DIPGTYVLNGGMA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 324 IAGAVIRWLRDNLGIIKSSEE----------IEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHI 392
Cdd:cd07804 297 TSGSLLRWFRDEFAGEEVEAEksggdsaydlLDEEAEKIPpGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHL 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 6680139 393 AFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPS 450
Cdd:cd07804 377 YRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVK 433
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
15-453 |
3.64e-69 |
|
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: 229.71 E-value: 3.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTrflvfnsKTA------ELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECiekTCEKLGQLNIDISNIKAI 88
Cdd:cd07805 4 AIDLGTSGV-------KAAlvdldgELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 89 GVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNnFVKSKTGLPLSTYFSAVKLRWLLDNVKkvqEAV 168
Cdd:cd07805 74 AFSGQMQGVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIAGGLGGIE-GYRLGGGNPPSGKDPLAKILWLKENEP---EIY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 169 EENRALFGTIDsWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYG--LMKA- 245
Cdd:cd07805 149 AKTHKFLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGelTPEAa 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 246 ---GALEGVPISGCLGDQSAALVGQMCFQDGQAkNTY-GTGCFLLCNTGHKCVFSEHGlLTTVAYKLgrdkPVYYALEGS 321
Cdd:cd07805 223 aelGLPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASAD----PGRYLLAAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 322 VAIAGAVIRWLRDNLGIIKSS-----EEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFA 395
Cdd:cd07805 297 QETAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARA 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 6680139 396 ALEAVCFQTREILDAMNRDCGiPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 453
Cdd:cd07805 377 VLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQ 433
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-458 |
3.32e-49 |
|
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: 175.43 E-value: 3.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 12 LVGaVDQGTSSTRFLVFNSKTAELLSHHqVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSG---VDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 92 NQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVeen 171
Cdd:cd07802 77 GHGNGLYLVDK-DGKPVRNAILSNDSRAADIVDRWEED--GTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRI--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 172 RALFGTIDsWLIWSLTGgihggVHCTDVTNASrTMLFNIHSLEWDKELCEFFGIP--MEILPNVRSSSEIYGLMKAGA-- 247
Cdd:cd07802 151 RTVLFCKD-WIRYRLTG-----EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 248 ----LEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCfllCNTG--HKCVFSEHGLLTTvaykLGRDKPVYYALEGS 321
Cdd:cd07802 224 ltglPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNS----LHADPGLYLIVEAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 322 VAIAGaVIRWLRDNLG------IIKSSEEIEKLAKEVG-TSYGCYFVPaFsgLYAPYWEPSARGIICGLTQFTNKCHIAF 394
Cdd:cd07802 297 PTSAS-NLDWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLR 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680139 395 AALEAVCFQTREILDAMNRDCgiPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 458
Cdd:cd07802 373 AVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALG 434
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
15-454 |
2.65e-47 |
|
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: 170.10 E-value: 2.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLgqlniDISNIKAIGVSNQR 94
Cdd:cd07783 4 GIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 95 ETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPgnnnFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVeenrAL 174
Cdd:cd07783 78 GTLVLVDR-EGEPLRPAIMYNDARAVAEAEELAEAAG----AVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKT----AK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 175 FGTIDSWLIWSLTGGihggVHCTDVTNASRTmLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKA------GAL 248
Cdd:cd07783 149 FLHQADWLAGRLTGD----RGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAeaaeelGLP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 249 EGVPIsgCLG--DQSAALVGQMCFQDGQAKNTYGTgcfllcntghkcvfsehglltTVAYKLGRDKPV------------ 314
Cdd:cd07783 224 AGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGT---------------------TLVLKLLSDKRVpdpgggvyshrh 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 315 ---YYALEGSVAIAGAVIRWLrdnlgiiKSSEEIEKLAKEVGTSY--GCYFVP-AFSGLYAPYWEPSARGIICGLTqfTN 388
Cdd:cd07783 281 gdgYWLVGGASNTGGAVLRWF-------FSDDELAELSAQADPPGpsGLIYYPlPLRGERFPFWDPDARGFLLPRP--HD 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6680139 389 KCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 454
Cdd:cd07783 352 RAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
15-455 |
1.65e-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: 168.17 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGW-VEQDPKEILQSVYECIEKTcekLGQLNIDISNIKAIGVSNQ 93
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDaKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 94 RETTVVWDKvTGEPLYnAVVWLDLRTQSTVENLSKRIPgnnNFVKSKTGLPLSTYFSAVKLRWLldnvKKVQEAVEENRA 173
Cdd:cd07798 81 REGIVFLDK-DGRELY-AGPNIDARGVEEAAEIDDEFG---EEIYTTTGHWPTELFPAARLLWF----KENRPEIFERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 174 LFGTIDSWLIWSLTGGIHggvhcTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGA------ 247
Cdd:cd07798 152 TVLSISDWIGYRLTGELV-----SEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAarelgl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 248 LEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGhKCVFSEHGLLTTVAYkLGRDKpvyYALEGSVAIAGA 327
Cdd:cd07798 227 PEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTD-EPIIDPERRLWTGCH-LVPGK---WVLESNAGVTGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 328 VIRWLRDNL--GIIKSSEEIEKLAKEVG-TSYGCYfvpAFSGLYAPYwePSARGIICGLTQFT--------NKCHIAFAA 396
Cdd:cd07798 302 NYQWLKELLygDPEDSYEVLEEEASEIPpGANGVL---AFLGPQIFD--ARLSGLKNGGFLFPtplsaselTRGDFARAI 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 6680139 397 LEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:cd07798 377 LENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREAS 435
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
275-458 |
1.88e-46 |
|
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: 160.95 E-value: 1.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 275 AKNTYGTGCFLLCNTGHKCVFsEHGLLTTVAyklGRDKPVYYALEGSVAIAGAVIRWLRDNLGI---------IKSSEEI 345
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLS-VHGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 346 EKLAKEVGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVD 425
Cdd:pfam02782 77 AALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190
....*....|....*....|....*....|...
gi 6680139 426 GGMTSNKILMQLQADILYIPVVKPSMPETTALG 458
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
8-458 |
5.91e-39 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 147.31 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07809 2 VLG-----IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 88 IGVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNnfvKSKTGLPLSTYFSAVKLRWLLDN----VKK 163
Cdd:cd07809 74 IGISGQMHGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGKK---CLLVGLNIPARFTASKLLWLKENepehYAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 164 VqeaveenrALFGTIDSWLIWSLTGGihggvHCTDVTNASRTMLFNIHSLEWDKELCEFF---GIPMEILPNVRSSSEIY 240
Cdd:cd07809 150 I--------AKILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 241 G-LMKAGALE-----GVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCflLCNTGHKCVFSEHGLLTTVAyklgrDKP 313
Cdd:cd07809 217 GrLTPEGAEElglpaGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFC-----DST 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 314 VYYALegSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEV-GTSYGCYFVPAFSGLYAPYWePSARGIICGLTQF-TNKC 390
Cdd:cd07809 290 GGMLP--LINTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRA 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6680139 391 HIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 458
Cdd:cd07809 367 NLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALG 433
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-455 |
2.92e-34 |
|
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: 134.27 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNSKTAELLS----HHQVEIKQEFPreGWVEQDPKEILQSVYECIEKTCEKLGqlnidiSNIKAIGV 90
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILEsvsrPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 91 SNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNnnfVKSKTGLPLSTYFSAVKLRWLLdnvkkVQEAVEE 170
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLITWQDQRCSEEFLGGLSTYGEE---LLPKSGMRLKPGYGLATLFWLL-----RNGPLPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 171 NRALFGTIDSWLIWSLTGGIHggvHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKAGALEG 250
Cdd:cd07777 147 KADRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 251 VPISGCLGDQSAALVGQMCFQDGQAKNTYGTG---CFLLC-NTGHKCV----FSEHGLLTTVAyKL--GRdkpVYYALEG 320
Cdd:cd07777 224 IPVYVALGDNQASVLGSGLNEENDAVLNIGTGaqlSFLTPkFELSGSVeirpFFDGRYLLVAA-SLpgGR---ALAVLVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 321 SVAiagaviRWLRDnLGIIKSSEEI-EKLAKEVGTSYGC--YFVPAFSGlyaPYWEPSARGIICGLTQ--FTNKcHIAFA 395
Cdd:cd07777 300 FLR------EWLRE-LGGSLSDDEIwEKLDELAESEESSdlSVDPTFFG---ERHDPEGRGSITNIGEsnFTLG-NLFRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6680139 396 ALEAVCfqtREILDAMNRDC--GIPLSHLQVDGGM-TSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:cd07777 369 LCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRIIEKRFGLPVVLSEGSEEA 428
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-454 |
9.22e-33 |
|
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: 130.05 E-value: 9.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 12 LVGaVDQGTSSTRFLVFNSKTAELlSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNidiSNIKAIGVS 91
Cdd:cd24121 2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 92 NQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKkvqEAVEEN 171
Cdd:cd24121 77 GQGDGTWLVDE-DGRPVRDAILWLDGRAADIVERWQAD--GIAEAVFEITGTGLFPGSQAAQLAWLKENEP---ERLERA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 172 RALFGTIDsWLIWSLTGGIhggvhCTDVTNASRTMlFNIHSLEWDKELCEFFGIP--MEILPNVRSSSEIYGLMKA---- 245
Cdd:cd24121 151 RTALHCKD-WLFYKLTGEI-----ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPeaaa 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 246 --GALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFllcntghkcvfseHGLLTTVAYkLGRDKP---VYYALEG 320
Cdd:cd24121 224 atGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV-------------HEVVVDEPD-LEPEGVgytICLGVPG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 321 SV-----AIAG-AVIRWLRDNLGIIKSSE----------EIEKLAKEV-----GTSYGCYFVPAfsGLYAPYWEPSARGI 379
Cdd:cd24121 290 RWlramaNMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppgaeGVLYHPYLSPA--GERAPFVNPNARAQ 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680139 380 ICGLTQFTNKCHIAFAALEAVCFQTREILDAMnrdcGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 454
Cdd:cd24121 368 FTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEF 438
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
8-455 |
1.79e-30 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 124.19 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEF--PREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNI 85
Cdd:cd07781 2 VIG-----IDFGTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAG---VDPEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 86 KAIGVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLS--TYFSavKLRWLLDNVKK 163
Cdd:cd07781 74 VGIGVDTTSSTVVPVDE-DGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSseWMWP--KALWLKRNAPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 164 VQEA----VEEnralfgtIDsWLIWSLTGGIHGGVhCtdvtNASRTMLFNIHSLEWDKELCEFFGIPM----EILP-NVR 234
Cdd:cd07781 151 VYDAaytiVEA-------CD-WINARLTGRWVRSR-C----AAGHKWMYNEWGGGPPREFLAALDPGLlklrEKLPgEVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 235 SSSEIYGLMKA------GALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCFLLcnTGHKCVFSEhGLLTTVayk 307
Cdd:cd07781 218 PVGEPAGTLTAeaaerlGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTsTCHLM--VSPKPVDIP-GICGPV--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 308 lgrDKPV---YYALEGSVAIAGAVIRWLRDNLGI------IKSSEEIEKLAKEVGTsyGCyfvpafSGLYA--------- 369
Cdd:cd07781 292 ---PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEAAKLPP--GE------SGLVAldwfngnrt 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 370 PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTS-NKILMQLQADILYIPVVK 448
Cdd:cd07781 361 PLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAEkNPLWMQIYADVLGRPIKV 439
|
....*..
gi 6680139 449 PSMPETT 455
Cdd:cd07781 440 PKSDQAP 446
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
15-455 |
3.04e-28 |
|
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: 117.82 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNsKTAELLSHHQVE-IKQEFPR-EGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVSN 92
Cdd:cd07775 4 ALDAGTGSGRAVIFD-LEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALK---KAGIAPKSIAAISTTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 93 QRETTVVWDKvTGEPLYnAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLStyFSAV-KLRWLLDNVKKVQEAVeen 171
Cdd:cd07775 80 MREGIVLYDN-EGEEIW-ACANVDARAAEEVSELKELYNTLEEEVYRISGQTFA--LGAIpRLLWLKNNRPEIYRKA--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 172 rALFGTIDSWLIWSLTGGIhggvhCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKA------ 245
Cdd:cd07775 153 -AKITMLSDWIAYKLSGEL-----AVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKeaaeet 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 246 GALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKcVFSEHGLLTTVAYKLgrdkPVYYALEGSVAIA 325
Cdd:cd07775 227 GLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAP-VTDPAMNIRVNCHVI----PDMWQAEGISFFP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 326 GAVIRWLRDNLGI----------IKSSEEIEKLAKEVGTsyGCY-FVPAFSGL--YApYWEPSARGIIcGLTQFTNKCHI 392
Cdd:cd07775 302 GLVMRWFRDAFCAeekeiaerlgIDAYDLLEEMAKDVPP--GSYgIMPIFSDVmnYK-NWRHAAPSFL-NLDIDPEKCNK 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6680139 393 A--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 455
Cdd:cd07775 378 AtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEAT 443
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-456 |
1.91e-25 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 109.35 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 17 DQGTSSTRFLVFNSKTAELLSHHQ---VEIKQEFPRegWVEQDPKEILQSVYECIEKTCEKLGQlnidiSNIKAIGVsnq 93
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTpnaSDIAAENSD--WHQWSLDAILQRFADCCRQINSELTE-----CHIRGITV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 94 reTT-----VVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTG-LPLSTYFsavKLRWLldnvkkvqea 167
Cdd:PRK10331 78 --TTfgvdgALVDK-QGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGaFSFNTLY---KLVWL---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 168 vEENRA-LFGTIDSWL-IWSLTGGIHGGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKA 245
Cdd:PRK10331 142 -KENHPqLLEQAHAWLfISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 246 GALE------GVPISGCLGDQSAALVGQMCFQDgQAKNTYGTGCFLLCNTGH---KCVFSEHGLLTTVAYKLGRDKPvyy 316
Cdd:PRK10331 221 SAAAllglpvGIPVISAGHDTQFALFGSGAGQN-QPVLSSGTWEILMVRSAQvdtSLLSQYAGSTCELDSQSGLYNP--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 317 aleGSVAIAGAVIRWLRDNLGiikSSEE-----IEKlAKEVGT-SYGCYFVPAFSGlyapywepSARGIICGLTQFTNKC 390
Cdd:PRK10331 297 ---GMQWLASGVLEWVRKLFW---TAETpyqtmIEE-ARAIPPgADGVKMQCDLLA--------CQNAGWQGVTLNTTRG 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6680139 391 HIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 456
Cdd:PRK10331 362 HFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTV 427
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
16-441 |
7.82e-22 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 98.50 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 16 VDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVyeciEKTCEKLGQLNiDISNIKAIGVSNQRE 95
Cdd:PRK15027 5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQWWQAT----DRAMKALGDQH-SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 96 TTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNnnfvKSKTGLPLSTYFSAVKLRWlldnVKKVQEAVEENRALF 175
Cdd:PRK15027 79 GATLLDA-QQRVLRPAILWNDGRCAQECALLEARVPQS----RVITGNLMMPGFTAPKLLW----VQRHEPEIFRQIDKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 176 GTIDSWLIWSLTggihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYG-----LMKAGALEG 250
Cdd:PRK15027 150 LLPKDYLRLRMT-----GEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGallpeVAKAWGMAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 251 VPISGCLGDQSAALVGQMCFQDGQAKNTYGTgcfllcnTGHKCVFSEhGLLT---TVAYKLGRDKPVYYALEGSVAIAGA 327
Cdd:PRK15027 225 VPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE-GFLSkpeSAVHSFCHALPQRWHLMSVMLSAAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 328 VIRW------LRDNLGIIKSSEEIEKLAKEVgtsygcYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVC 401
Cdd:PRK15027 297 CLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVG 370
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 6680139 402 FQTREILDAMNrDCGIPLSHLQVDGGMTSNKILMQLQADI 441
Cdd:PRK15027 371 YALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
15-454 |
1.89e-20 |
|
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: 94.52 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVsnqr 94
Cdd:cd07782 4 GVDVGTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAG---VDPEQVKGIGF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 95 ETT---VVWDK--------VTGEPLYNAVVWLDLRTQSTVEnlskRIpgnnnfvkSKTGLPLSTYFSAV--------KLR 155
Cdd:cd07782 76 DATcslVVLDAegkpvsvsPSGDDERNVILWMDHRAVEEAE----RI--------NATGHEVLKYVGGKispemeppKLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 156 WLldnvKKVQEAVEENRALFGTIDSWLIWSLTGgihggvhctdvtNASR---------TMLFNIHSLE-WDKELCEFFG- 224
Cdd:cd07782 144 WL----KENLPETWAKAGHFFDLPDFLTWKATG------------SLTRslcslvckwTYLAHEGSEGgWDDDFFKEIGl 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 225 ----------IPMEILPNVRSSSEiyGLMKAGA-----LEGVPIS--------GCLGDQSAALVGQMC-FQDGQAKntyg 280
Cdd:cd07782 208 edlvednfakIGSVVLPPGEPVGG--GLTAEAAkelglPEGTPVGvslidahaGGLGTLGADVGGLPCeADPLTRR---- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 281 tgCFLLCNTG--HkCVFSEHGLLttVA-----YKlGRDKPVYYALEGSVAIAGAVIRWlrdnlgIIKS---SEEIEKLAK 350
Cdd:cd07782 282 --LALICGTSscH-MAVSPEPVF--VPgvwgpYY-SAMLPGLWLNEGGQSATGALLDH------IIEThpaYPELKEEAK 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 351 EVGTSY------------------------GCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA---FAALEAVCFQ 403
Cdd:cd07782 350 AAGKSIyeylnerleqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLAllyLATLQALAYG 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 6680139 404 TREILDAMNRdCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 454
Cdd:cd07782 430 TRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
16-454 |
5.49e-20 |
|
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: 93.07 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 16 VDQGTSSTRFLVFNSKTAELLSHHQVEIKQ-EFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKAIGVSN-- 92
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDAtc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 93 -----QRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLskripgnnNFVKSKTGLP-----LSTYFSAVKLRWLLDNVK 162
Cdd:cd07768 82 slaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWI--------NMQCPQQLLDylggkISPEMGVPKLKYFLDEYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 163 KVQEAVEEnraLFGTIDsWLIWSLTGGIHGGVhCTDVTNASrtmlFNIHSLEWDKELCEFFGIPME------ILPNVRSS 236
Cdd:cd07768 154 HLRDKHFH---IFDLHD-YIAYELTRLYEWNI-CGLLGKEN----LDGEESGWSSSFFKNIDPRLEhltttkNLPSNVPI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 237 SEIYGLM------KAGALEGVPISGCLGDQSAALVGQmcfqdgqAKNTYGTGCFLLCNTGhkcvfSEHGLLTTVAYKL-G 309
Cdd:cd07768 225 GTTSGVAlpemaeKMGLHPGTAVVVSCIDAHASWFAV-------ASPHLETSLFMIAGTS-----SCHMYGTTISDRIpG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 310 RDKPVYYAL-------EGSVAIAGAVIRWL-------RDNLGIIKSSEEI--------EKLAKEVGTSYGCYFVPAFSGL 367
Cdd:cd07768 293 VWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleqtiRQIEKNNGLSIHILTLDMFFGN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 368 YAPYWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQADILYI 444
Cdd:cd07768 373 RSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNV 451
|
490
....*....|
gi 6680139 445 PVVKPSMPET 454
Cdd:cd07768 452 AIIKPKENMM 461
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
15-447 |
2.69e-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: 84.50 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLV--FNSKTAELL-----SHHQVEIKQefpREGWveqDPKEILQSVYECIEKTCEKLGQlnidisnIKA 87
Cdd:cd07771 4 AVDLGASSGRVILgsLDGGKLELEeihrfPNRPVEING---HLYW---DIDRLFDEIKEGLKKAAEQGGD-------IDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 88 IGVsnqreTTvvW-------DKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLldn 160
Cdd:cd07771 71 IGI-----DT--WgvdfgllDK-NGELLGNPVHYRDPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 161 vkkvqeaVEENRALFGTIDSWLI------WSLTGGIhggvhCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVR 234
Cdd:cd07771 138 -------KKEGPELLERADKLLMlpdllnYLLTGEK-----VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 235 SSSEIYG-----LMKAGALEGVP-ISGCLGDQSAALVGQMCFQDGQAkntygtgcFLLCNT----GhkcVFSEHGLLTTV 304
Cdd:cd07771 206 PPGTVLGtlkpeVAEELGLKGIPvIAVASHDTASAVAAVPAEDEDAA--------FISSGTwsliG---VELDEPVITEE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 305 AYKLGrdkpvyYALEGSVA--------IAGaviRWL----RDNL---GIIKSSEEIEKLAKEVgTSYGCYFVPAFSGLYA 369
Cdd:cd07771 275 AFEAG------FTNEGGADgtirllknITG---LWLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFLN 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 370 PywePSARGIICGLTQFTN------KCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILY 443
Cdd:cd07771 345 P---GDMPEAIRAYCRETGqpvpesPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATG 421
|
....
gi 6680139 444 IPVV 447
Cdd:cd07771 422 LPVI 425
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-458 |
1.26e-16 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 82.47 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 5 KKAVLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQ------EFPREGWVEQDPKEILQSVYECIektCEKLGQL 78
Cdd:COG1069 1 EKYVIG-----VDFGTDSVRAVVVDAADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAV---REALAQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 79 NIDISNIKAIGVSNQRETTVVWDKvTGEPL-----------YNAVVWLDLRTQSTVEnlskRIpgnnNFVKSKTGLPLST 147
Cdd:COG1069 73 GVDPADVVGIGVDATGCTPVPVDA-DGTPLallpefaenphAMVILWKDHTAQEEAE----RI----NELAKARGEDYLR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 148 Y---------FSAvKLRWLLdnvkkvqeavEENRALFGTIDS------WLIWSLTGGIHGGVhCTdvtnASRTMLFNIHS 212
Cdd:COG1069 144 YvggiissewFWP-KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRSR-CT----AGHKALWHAHE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 213 LEWDKElcEFF---GIPMEILPNvRSSSEIYGL-MKAGAL-----------EGVPISGCLGDQSAALVGQMCFQDGQ-AK 276
Cdd:COG1069 208 GGYPSE--EFFaalDPLLDGLAD-RLGTEIYPLgEPAGTLtaewaarlglpPGTAVAVGAIDAHAGAVGAGGVEPGTlVK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 277 NtYGT-GCFLLCNTGHKC-------VFSehGLLttvayklgrdkPVYYALEGSVAIAGAVIRWLRDNLGiikSSEEIEKL 348
Cdd:COG1069 285 V-MGTsTCHMLVSPEERFvpgicgqVDG--SIV-----------PGMWGYEAGQSAVGDIFAWFVRLLV---PPLEYEKE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 349 AKEVGTS----------------YGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMN 412
Cdd:COG1069 348 AEERGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFE 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 6680139 413 rDCGIPLSHLQVDGG-MTSNKILMQLQADILYIPVVKPSMPETTALG 458
Cdd:COG1069 428 -EEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALG 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-258 |
1.51e-11 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 66.57 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPR-EGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSNQ 93
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 94 RETTVVWDKvTGEPLYnAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLStyFSAV-KLRWLldnvKKVQEAVEENR 172
Cdd:PRK10939 84 REGIVLYDR-NGTEIW-ACANVDARASREVSELKELHNNFEEEVYRCSGQTLA--LGALpRLLWL----AHHRPDIYRQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 173 ALFGTIDSWLIWSLTGGIhggvhCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKA------G 246
Cdd:PRK10939 156 HTITMISDWIAYMLSGEL-----AVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAkaaaetG 230
|
250 260
....*....|....*....|
gi 6680139 247 ALEGVPI--------SGCLG 258
Cdd:PRK10939 231 LRAGTPVvmgggdvqLGCLG 250
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
16-448 |
7.57e-09 |
|
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: 58.18 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 16 VDQGTSSTRFLVFNSKTaELLSHHQVEI-KQEFPREGW-VEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKA---IGV 90
Cdd:cd07778 5 IDVGSTSVRIGIFDYHG-TLLATSERPIsYKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSAtcsMVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 91 SNQRETTVVWDKVTGEPLY-----NAVVWLDLRTQSTVENLskripgNNNFVKSKTGLPLSTYF---SAVKLRWLLDNVK 162
Cdd:cd07778 84 MQRDSDTSYLVPYNVIHEKsnpdqDIIFWMDHRASEETQWL------NNILPDDILDYLGGGFIpemAIPKLKYLIDLIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 163 kvqEAVEENRALFGTIDsWLIWSL-TGGIHGGVhcTDVTNASRTMLFNIHSLE-WDKELCEFFGIPMEILPNVRSSSEIY 240
Cdd:cd07778 158 ---EDTFKKLEVFDLHD-WISYMLaTNLGHSNI--VPVNAPPSIGIGIDGSLKgWSKDFYSKLKISTKVCNVGNTFKEAP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 241 GLMKAG-----------ALEGVPIS-----GCLgDQSAALVGQMC---FQDGQAKNTYGTG-CFLLcntGHKCV------ 294
Cdd:cd07778 232 PLPYAGipigkvnvilaSYLGIDKStvvghGCI-DCYAGWFSTFAaakTLDTTLFMVAGTStCFLY---ATSSSqvgpip 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 295 -----FSEhgllttvaykLGRDKPVYyalEGSVAIAG-----------AVIRWLRDNLGIIKSSEE-IEKLAKEVGTS-- 355
Cdd:cd07778 308 giwgpFDQ----------LLKNYSVY---EGGQSATGklieklfnshpAIIELLKSDANFFETVEEkIDKYERLLGQSih 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 356 --YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTNKCHIAF---AALEAVCFQTREILDAMNRDCgIPLSHLQVDG 426
Cdd:cd07778 375 ylTRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKEK-IIIQKVVISG 450
|
490 500
....*....|....*....|..
gi 6680139 427 GMTSNKILMQLQADILYIPVVK 448
Cdd:cd07778 451 SQAKNARLLQLLSTVLSKIHII 472
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
377-458 |
1.97e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 44.07 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680139 377 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGM-TSNKILMQLQADILYIPV-VKPSmPET 454
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475
|
....
gi 6680139 455 TALG 458
Cdd:PRK04123 476 PALG 479
|
|
| |
