|
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; ... |
11-516 |
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: 994.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 91 SNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEE 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 171 NRALFGTIDSWLIWSLTGGIHGGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKIshslk 250
Cdd:cd07792 160 GRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIAS----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 251 aGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYYALEGSVAI 330
Cdd:cd07792 235 -GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 331 AGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQT 410
Cdd:cd07792 314 AGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 411 REILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLSAVTM 490
Cdd:cd07792 394 REILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGR 473
|
490 500
....*....|....*....|....*.
gi 659066190 491 ERFEPQINAEESEIRYSTWKKAVMKS 516
Cdd:cd07792 474 TVFEPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
11-519 |
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: 828.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 11 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 91 SNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNnnFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEE 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYGE--FIREKTGLPLDPYFSATKLRWLLDNVPGVREAAER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 171 NRALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLk 250
Cdd:TIGR01311 155 GELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGLLG- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 251 agalEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYyALEGSVAI 330
Cdd:TIGR01311 231 ----AEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPVY-ALEGSVFV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 331 AGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQT 410
Cdd:TIGR01311 306 AGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 411 REILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLSAVTm 490
Cdd:TIGR01311 386 RDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVE- 464
|
490 500
....*....|....*....|....*....
gi 659066190 491 ERFEPQINAEESEIRYSTWKKAVMKSIGW 519
Cdd:TIGR01311 465 KTFEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
13-513 |
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: 762.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAG---ISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 93 QRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENR 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAK--GLEERIREKTGLPLDPYFSATKIKWILDNVPGARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 173 ALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmkisHSLKAG 252
Cdd:cd07769 156 LLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFG-----YTDPEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 253 ALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLgrDKPVYYALEGSVAIAG 332
Cdd:cd07769 228 LGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQI--GGKVTYALEGSIFIAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 333 AVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTRE 412
Cdd:cd07769 306 AAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 413 ILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgVWSLEPEDLSAVTMER 492
Cdd:cd07769 386 VLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalgaayl--aglavgFWKDLDELASLWQVDK 463
|
490 500
....*....|....*....|..
gi 659066190 493 -FEPQINAEESEIRYSTWKKAV 513
Cdd:cd07769 464 rFEPSMDEEERERLYRGWKKAV 485
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
13-520 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 754.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 93 QRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENR 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKAD--GLEDLIREKTGLVLDPYFSATKIKWILDNVPGARERAEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 173 ALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmkisHSLKAG 252
Cdd:COG0554 159 LLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFG-----ETDPDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 253 ALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGrDKPVYyALEGSVAIAG 332
Cdd:COG0554 231 FGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLG-GKVTY-ALEGSIFVAG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 333 AVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTRE 412
Cdd:COG0554 309 AAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 413 ILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgVWSlEPEDLSAV--TM 490
Cdd:COG0554 389 VLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalgaayl--aglavgFWK-SLEELAALwkVD 465
|
490 500 510
....*....|....*....|....*....|
gi 659066190 491 ERFEPQINAEESEIRYSTWKKAVMKSIGWV 520
Cdd:COG0554 466 RRFEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-520 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 726.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 11 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISnIKAIGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 91 SNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKsKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEE 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQK-ITGLPISTYFSAFKIRWMLENVPAVKDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 171 NRALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKishSLK 250
Cdd:PTZ00294 159 GTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTIS---GEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 251 AGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYYALEGSVAI 330
Cdd:PTZ00294 233 VPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 331 AGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQT 410
Cdd:PTZ00294 313 AGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 411 REILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVW-SLEP-EDLSAV 488
Cdd:PTZ00294 393 NDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT--ALGAALLAGLAVGVWkSLEEvKKLIRR 470
|
490 500 510
....*....|....*....|....*....|..
gi 659066190 489 TMERFEPQINAEESEIRYSTWKKAVMKSIGWV 520
Cdd:PTZ00294 471 SNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-520 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 711.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQ--LNIDiSNIKAIG 89
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAkgHNVD-SGLKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 90 VSNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVE 169
Cdd:PLN02295 79 ITNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 170 ENRALFGTIDSWLIWSLTGGIHGGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmKISHSl 249
Cdd:PLN02295 159 SGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG--TIAKG- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 250 kaGALEGVPISGCLGDQSAALVGQMCfQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYYALEGSVA 329
Cdd:PLN02295 236 --WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 330 IAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQ 409
Cdd:PLN02295 313 IAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 410 TREILDAMNRDCGIPLSH-----LQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVWSlePED 484
Cdd:PLN02295 393 VKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETT--ALGAAYAAGLAVGLWT--EEE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 659066190 485 LSAVTMER----FEPQINAEESEIRYSTWKKAVMKSIGWV 520
Cdd:PLN02295 469 IFASEKWKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-520 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 701.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 13 VGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 93 QRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENR 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRD--GYEDYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 173 ALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAG 252
Cdd:PRK00047 161 LLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 253 alegVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGrDKPVYyALEGSVAIAG 332
Cdd:PRK00047 238 ----VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGID-GKVVY-ALEGSIFVAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 333 AVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTRE 412
Cdd:PRK00047 312 SAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 413 ILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaagaaegvgvwSL------------ 480
Cdd:PRK00047 392 VLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT-----------------ALgaaylaglavgf 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 659066190 481 --EPEDLSAVTME--RFEPQINAEESEIRYSTWKKAVMKSIGWV 520
Cdd:PRK00047 455 wkDLDELKEQWKIdrRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
15-513 |
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: 694.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07786 4 AIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 95 ETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENRAL 174
Cdd:cd07786 80 ETTVVWDRETGKPVYNAIVWQDRRTADICEELKAE--GHEEMIREKTGLVLDPYFSATKIRWILDNVPGARERAERGELA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 175 FGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmkisHSLKAGAL 254
Cdd:cd07786 158 FGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFG-----YTDPDLLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 255 EGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGrdKPVYYALEGSVAIAGAV 334
Cdd:cd07786 230 AEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLG--GKVTYALEGSIFIAGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 335 IRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREIL 414
Cdd:cd07786 308 VQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 415 DAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL--------GAAMAAGAAEGVGVWSLEpedls 486
Cdd:cd07786 388 EAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALgaaylaglAVGLWKSLDELAKLWQVD----- 462
|
490 500
....*....|....*....|....*..
gi 659066190 487 avtmERFEPQINAEESEIRYSTWKKAV 513
Cdd:cd07786 463 ----RRFEPSMSEEEREALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
15-513 |
3.91e-151 |
|
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: 3.91e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07793 4 AVDVGTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAG---LTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 95 ETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSK---------------RIPGNNNFVKSKTgLPLSTYFSAVKLRWLLD 159
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFITWQDLRAAELCESWNRslllkalrggskflhFLTRNKRFLAASV-LKFSTAHVSIRLLWILQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 160 NVKKVQEAVEENRALFGTIDSWLIWSLTGGihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEI 239
Cdd:cd07793 159 NNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 240 YGLMKISHSLKAgalegVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGrDKP 319
Cdd:cd07793 236 FGSTDPSIFGAE-----IPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIG-GEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 320 VYyALEGSVAIAGAVIRWLRDNLGIiKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA 399
Cdd:cd07793 310 TY-LAEGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 400 FAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGAAMAAGAAEGVGVWS 479
Cdd:cd07793 388 RAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMS--ALGAAFLAGLASGIWK 465
|
490 500 510
....*....|....*....|....*....|....*.
gi 659066190 480 lEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAV 513
Cdd:cd07793 466 -SKEELKKLrkIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-272 |
2.23e-113 |
|
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: 337.00 E-value: 2.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVS 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLS---QLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 92 NQRETTVVWDKVTgEPLYNAVVWLDLRTQSTVENLSKriPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEen 171
Cdd:pfam00370 77 NQGHGTVLLDKND-KPLYNAILWKDRRTAEIVENLKE--EGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 172 raLFGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKA 251
Cdd:pfam00370 152 --KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMW 224
|
250 260
....*....|....*....|.
gi 659066190 252 GALEGVPISGCLGDQSAALVG 272
Cdd:pfam00370 225 GLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-461 |
8.27e-97 |
|
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: 303.29 E-value: 8.27e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 6 KAVLGplvgaVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNI 85
Cdd:COG1070 1 KYVLG-----IDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAG---VDPEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 86 KAIGVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNvkkvQ 165
Cdd:COG1070 72 AAIGVSGQMHGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREELGEEALY--EITGNPLHPGFTAPKLLWLKEN----E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 166 EAVEENRALFGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKI 245
Cdd:COG1070 145 PEIFARIAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 246 SHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKcVFSEHGLLTTVAYKL-GRdkpvyYAL 324
Cdd:COG1070 220 EAAAETGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKP-LPDPEGRVHTFCHAVpGR-----WLP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 325 EGSVAIAGAVIRWLRDNLGIIKSS--EEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFA 401
Cdd:COG1070 294 MGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARA 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 402 ALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:COG1070 374 VLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGG 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
15-461 |
8.75e-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: 8.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAG---IDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 95 ETTVVWDKvTGEPLYNAVVWLDlrtqstvenlskripgnnnfvksktglplstyfsavklrwlldnvkkvqeaveeNRAL 174
Cdd:cd00366 80 PGVVLVDA-DGNPLRPAIIWLD------------------------------------------------------RRAK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 175 FGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmKISH--SLKAG 252
Cdd:cd00366 105 FLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVG--RVTPeaAEETG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 253 ALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGhKCVFSEHGLLTTVAYKLGRdkpvyYALEGSVAIAG 332
Cdd:cd00366 178 LPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDPRLLNRCHVVPGL-----WLLEGAINTGG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 333 AVIRWLRDNLGIIKSSEE----IEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVC 407
Cdd:cd00366 252 ASLRWFRDEFGEEEDSDAeyegLDELAAEVPPgSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVA 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 659066190 408 FQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd00366 332 YALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
15-461 |
2.18e-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: 292.50 E-value: 2.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07779 4 GIDVGTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 95 ETTVVWDKvTGEPLYNAVVWLDLRTqstvenlskripgnnnfvksktglplstyfsavklrwlldnvkkvqeaveenrAL 174
Cdd:cd07779 80 STFVPVDE-DGRPLRPAISWQDKRT-----------------------------------------------------AK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 175 FGTIDSWLIWSLTggihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmKISH--SLKAG 252
Cdd:cd07779 106 FLTVQDYLLYRLT-----GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIG--TLTKeaAEETG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 253 ALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTgHKCVFSEHGLLTTVAYKLgrdkPVYYALEGSVAIAG 332
Cdd:cd07779 179 LPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAV----PGKWVLEGSINTGG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 333 AVIRWLRDNLG--------IIKSSEE-IEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAA 402
Cdd:cd07779 254 SAVRWFRDEFGqdevaekeLGVSPYElLNEEAAKSPPgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAI 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 659066190 403 LEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07779 334 LEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEAT 391
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-461 |
3.93e-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: 268.69 E-value: 3.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 12 LVGaVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQlnidiSNIKAIGVS 91
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 92 NQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVeen 171
Cdd:cd07773 75 SQGESGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERIGAEELY--RITGLPPSPMYSLAKLLWLREHEPEIFAKA--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 172 rALFGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKA 251
Cdd:cd07773 149 -AKWLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 252 GALEGVPIsgCLG--DQSAALVGQMCFQDGQAKNTYGTG-CFLLC-NTGHKCVFSEHGLLTTVAYKLGRdkpvYYALEGS 327
Cdd:cd07773 223 GLPAGTPV--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLDEMLAEGGLSYGHHVPGG----YYYLAGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 328 VAiAGAVIRWLRDNLGI--IKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEA 405
Cdd:cd07773 297 LP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEG 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 659066190 406 VCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07773 376 LAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEAT 430
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-461 |
8.13e-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: 261.32 E-value: 8.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 8 VLGplvgaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07808 2 LLG-----IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 88 IGVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPgnnNFVKSKTGLPLSTYFSAVKLRWLL----DNVKK 163
Cdd:cd07808 73 IGLTGQMHGLVLLDK-NGRPLRPAILWNDQRSAAECEELEARLG---DEILIITGNPPLPGFTLPKLLWLKenepEIFAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 164 VqeaveenRALFGTIDsWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlm 243
Cdd:cd07808 149 I-------RKILLPKD-YLRYRLTG-----ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVG-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 244 KISHSLkAGAL---EGVP-ISGClGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTgHKCVFSEHGLLTTVAYKLGrdkP 319
Cdd:cd07808 214 TLTPEA-AEELglpEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPHAVP---G 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 320 VYYALeGSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCH 397
Cdd:cd07808 288 KWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAH 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 659066190 398 IAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07808 367 LARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGS 429
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
15-461 |
3.95e-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: 251.32 E-value: 3.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDisnikAIGVSNQR 94
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVD-----AIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 95 ETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNnfVKSKTGLPLSTYFSAVKLRWLldnvKKVQEAVEENRAL 174
Cdd:cd07770 78 HSLLGVDE-DGEPLTPVITWADTRAAEEAERLRKEGDGSE--LYRRTGCPIHPMYPLAKLLWL----KEERPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 175 FGTIDSWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAGAL 254
Cdd:cd07770 151 FVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 255 EGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTgcfllcnTGHKCVFSEHGLLT----TVAYKLGRDKPVyyaLEGSVAI 330
Cdd:cd07770 226 AGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPVLDppgrLWCYRLDENRWL---VGGAINN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 331 AGAVIRWLRDNLGIIKSS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCF 408
Cdd:cd07770 296 GGNVLDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAF 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 659066190 409 QTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07770 376 NLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEAS 427
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-456 |
1.20e-70 |
|
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: 233.57 E-value: 1.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 12 LVGaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAG---ISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 92 NQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLLDNvkkvQEAVEEN 171
Cdd:cd07804 77 GLVPALVPVDE-NGKPLRPAILYGDRRATEEIEWLNENIGEDRIF--EITGNPLDSQSVGPKLLWIKRN----EPEVFKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 172 RALFGTIDSWLIWSLTGgihggVHCTDVTNASRTM-LFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmKISH--S 248
Cdd:cd07804 150 TRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVG--EVTKeaA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 249 LKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCFLLCntgHKCVFSEHGLLTTVAyklgrDKPVYYALEGS 327
Cdd:cd07804 223 EETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVV---TDKLPTDPRLWLDYH-----DIPGTYVLNGG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 328 VAIAGAVIRWLRDNLGIIKSSEE----------IEKLAKEVG-TSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKC 396
Cdd:cd07804 295 MATSGSLLRWFRDEFAGEEVEAEksggdsaydlLDEEAEKIPpGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRA 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 397 HIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPS 456
Cdd:cd07804 375 HLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVK 433
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
15-459 |
7.57e-68 |
|
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: 227.40 E-value: 7.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTrflvfnsKTA------ELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECiekTCEKLGQLNIDISNIKAI 88
Cdd:cd07805 4 AIDLGTSGV-------KAAlvdldgELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 89 GVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNnFVKSKTGLPLSTYFSAVKLRWLLDNVKkvqEAV 168
Cdd:cd07805 74 AFSGQMQGVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIAGGLGGIE-GYRLGGGNPPSGKDPLAKILWLKENEP---EIY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 169 EENRALFGTIDsWLIWSLTGgihggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYG--LMKIS 246
Cdd:cd07805 149 AKTHKFLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGelTPEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 247 HSLkaGALEGVPISGCLGDQSAALVGQMCFQDGQAkNTY-GTGCFLLCNTGHKCVFSEHGlLTTVAYKLgrdkPVYYALE 325
Cdd:cd07805 223 AEL--GLPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPKPKTDPDHG-IFTLASAD----PGRYLLA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 326 GSVAIAGAVIRWLRDNLGIIKSS-----EEIEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA 399
Cdd:cd07805 295 AEQETAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLA 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 400 FAALEAVCFQTREILDAMNRDCGiPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 459
Cdd:cd07805 375 RAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQ 433
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-464 |
2.77e-48 |
|
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: 173.89 E-value: 2.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 12 LVGaVDQGTSSTRFLVFNSKTAELLSHHqVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSG---VDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 92 NQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVeen 171
Cdd:cd07802 77 GHGNGLYLVDK-DGKPVRNAILSNDSRAADIVDRWEED--GTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRI--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 172 RALFGTIDsWLIWSLTGgihggVHCTDVTNASrTMLFNIHSLEWDKELCEFFGIP--MEILPNVRSSSEIYGLMKISHSL 249
Cdd:cd07802 151 RTVLFCKD-WIRYRLTG-----EISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 250 KAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCfllCNTG--HKCVFSEHGLLTTvaykLGRDKPVYYALEGS 327
Cdd:cd07802 224 LTGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEPVVPDSVGSNS----LHADPGLYLIVEAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 328 VAIAGaVIRWLRDNLG------IIKSSEEIEKLAKEVG-TSYGCYFVPaFsgLYAPYWEPSARGIICGLTQFTNKCHIAF 400
Cdd:cd07802 297 PTSAS-NLDWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLR 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 659066190 401 AALEAVCFQTREILDAMNRDCgiPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 464
Cdd:cd07802 373 AVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALG 434
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
15-460 |
1.85e-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: 171.25 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLgqlniDISNIKAIGVSNQR 94
Cdd:cd07783 4 GIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 95 ETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPgnnnFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVeenrAL 174
Cdd:cd07783 78 GTLVLVDR-EGEPLRPAIMYNDARAVAEAEELAEAAG----AVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKT----AK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 175 FGTIDSWLIWSLTGGihggVHCTDVTNASRTmLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYG--LMKISHSLkaG 252
Cdd:cd07783 149 FLHQADWLAGRLTGD----RGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGtlTAEAAEEL--G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 253 ALEGVPIsgCLG--DQSAALVGQMCFQDGQAKNTYGTgcfllcntghkcvfsehglltTVAYKLGRDKPV---------- 320
Cdd:cd07783 222 LPAGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGT---------------------TLVLKLLSDKRVpdpgggvysh 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 321 -----YYALEGSVAIAGAVIRWLrdnlgiiKSSEEIEKLAKEVGTSY--GCYFVP-AFSGLYAPYWEPSARGIICGLTqf 392
Cdd:cd07783 279 rhgdgYWLVGGASNTGGAVLRWF-------FSDDELAELSAQADPPGpsGLIYYPlPLRGERFPFWDPDARGFLLPRP-- 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 659066190 393 TNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 460
Cdd:cd07783 350 HDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
281-464 |
3.22e-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: 3.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 281 AKNTYGTGCFLLCNTGHKCVFsEHGLLTTVAyklGRDKPVYYALEGSVAIAGAVIRWLRDNLGI---------IKSSEEI 351
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLS-VHGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 352 EKLAKEVGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVD 431
Cdd:pfam02782 77 AALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190
....*....|....*....|....*....|...
gi 659066190 432 GGMTSNKILMQLQADILYIPVVKPSMPETTALG 464
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
15-461 |
6.21e-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: 167.40 E-value: 6.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGW-VEQDPKEILQSVYECIEKTcekLGQLNIDISNIKAIGVSNQ 93
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDaKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 94 RETTVVWDKvTGEPLYnAVVWLDLRTQSTVENLSKRIPgnnNFVKSKTGLPLSTYFSAVKLRWLldnvKKVQEAVEENRA 173
Cdd:cd07798 81 REGIVFLDK-DGRELY-AGPNIDARGVEEAAEIDDEFG---EEIYTTTGHWPTELFPAARLLWF----KENRPEIFERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 174 LFGTIDSWLIWSLTGGIHggvhcTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmKISHSLKA-- 251
Cdd:cd07798 152 TVLSISDWIGYRLTGELV-----SEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLG--TVSEEAARel 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 252 GALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGhKCVFSEHGLLTTVAYkLGRDKpvyYALEGSVAIA 331
Cdd:cd07798 225 GLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTD-EPIIDPERRLWTGCH-LVPGK---WVLESNAGVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 332 GAVIRWLRDNL--GIIKSSEEIEKLAKEVG-TSYGCYfvpAFSGLYAPYwePSARGIICGLTQFT--------NKCHIAF 400
Cdd:cd07798 300 GLNYQWLKELLygDPEDSYEVLEEEASEIPpGANGVL---AFLGPQIFD--ARLSGLKNGGFLFPtplsaselTRGDFAR 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659066190 401 AALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07798 375 AILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREAS 435
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
8-464 |
7.03e-38 |
|
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: 145.00 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07809 2 VLG-----IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 88 IGVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNnfvKSKTGLPLSTYFSAVKLRWLLDN----VKK 163
Cdd:cd07809 74 IGISGQMHGLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGKK---CLLVGLNIPARFTASKLLWLKENepehYAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 164 VqeaveenrALFGTIDSWLIWSLTGGihggvHCTDVTNASRTMLFNIHSLEWDKELCEFF---GIPMEILPNVRSSSEIY 240
Cdd:cd07809 150 I--------AKILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 241 GLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCflLCNTGHKCVFSEHGLLTTVAyklgrDKP 319
Cdd:cd07809 217 GRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT--AYGVSDKPVSDPHGRVATFC-----DST 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 320 VYYALegSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEV-GTSYGCYFVPAFSGLYAPYWePSARGIICGLTQF-TNKC 396
Cdd:cd07809 290 GGMLP--LINTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPFLNGERTPNL-PHGRASLVGLTLSnFTRA 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 659066190 397 HIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALG 464
Cdd:cd07809 367 NLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALG 433
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-460 |
2.00e-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: 132.75 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 12 LVGaVDQGTSSTRFLVFNSKTAELlSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNidiSNIKAIGVS 91
Cdd:cd24121 2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 92 NQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRipGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKkvqEAVEEN 171
Cdd:cd24121 77 GQGDGTWLVDE-DGRPVRDAILWLDGRAADIVERWQAD--GIAEAVFEITGTGLFPGSQAAQLAWLKENEP---ERLERA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 172 RALFGTIDsWLIWSLTGGIhggvhCTDVTNASRTMlFNIHSLEWDKELCEFFGIP--MEILPNVRSSSEIYGLMKISHSL 249
Cdd:cd24121 151 RTALHCKD-WLFYKLTGEI-----ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 250 KAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFllcntghkcvfseHGLLTTVAYkLGRDKP---VYYALEG 326
Cdd:cd24121 224 ATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV-------------HEVVVDEPD-LEPEGVgytICLGVPG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 327 SV-----AIAG-AVIRWLRDNLGIIKSSE----------EIEKLAKEV-----GTSYGCYFVPAfsGLYAPYWEPSARGI 385
Cdd:cd24121 290 RWlramaNMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppgaeGVLYHPYLSPA--GERAPFVNPNARAQ 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659066190 386 ICGLTQFTNKCHIAFAALEAVCFQTREILDAMnrdcGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 460
Cdd:cd24121 368 FTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEF 438
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-461 |
1.06e-32 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 130.03 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNSKTAELLS----HHQVEIKQEFPreGWVEQDPKEILQSVYECIEKTCEKLGqlnidiSNIKAIGV 90
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILEsvsrPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 91 SNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNnnfVKSKTGLPLSTYFSAVKLRWLLdnvkkVQEAVEE 170
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLITWQDQRCSEEFLGGLSTYGEE---LLPKSGMRLKPGYGLATLFWLL-----RNGPLPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 171 NRALFGTIDSWLIWSLTGGIHggvHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGlmkishSLK 250
Cdd:cd07777 147 KADRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVG------TLS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 251 AGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTG---CFLLC-NTGHKCV----FSEHGLLTTVAyKL--GRdkpV 320
Cdd:cd07777 218 SALPKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGaqlSFLTPkFELSGSVeirpFFDGRYLLVAA-SLpgGR---A 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 321 YYALEGSVAiagaviRWLRDnLGIIKSSEEI-EKLAKEVGTSYGC--YFVPAFSGlyaPYWEPSARGIICGLTQ--FTNK 395
Cdd:cd07777 294 LAVLVDFLR------EWLRE-LGGSLSDDEIwEKLDELAESEESSdlSVDPTFFG---ERHDPEGRGSITNIGEsnFTLG 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 659066190 396 cHIAFAALEAVCfqtREILDAMNRDC--GIPLSHLQVDGGM-TSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07777 364 -NLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRIIEKRFGLPVVLSEGSEEA 428
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
8-461 |
6.41e-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: 123.03 E-value: 6.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEF--PREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNI 85
Cdd:cd07781 2 VIG-----IDFGTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAG---VDPEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 86 KAIGVSNQRETTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLS--TYFSavKLRWLLDNVKK 163
Cdd:cd07781 74 VGIGVDTTSSTVVPVDE-DGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYGGVYSseWMWP--KALWLKRNAPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 164 VQEA----VEEnralfgtIDsWLIWSLTGGIHGGVhCtdvtNASRTMLFNIHSLEWDKELCEFFGIPM----EILP-NVR 234
Cdd:cd07781 151 VYDAaytiVEA-------CD-WINARLTGRWVRSR-C----AAGHKWMYNEWGGGPPREFLAALDPGLlklrEKLPgEVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 235 SSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCFLLcnTGHKCVFSEhGLLTTVayk 313
Cdd:cd07781 218 PVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTsTCHLM--VSPKPVDIP-GICGPV--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 314 lgrDKPV---YYALEGSVAIAGAVIRWLRDNLGI------IKSSEEIEKLAKEVGTsyGCyfvpafSGLYA--------- 375
Cdd:cd07781 292 ---PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEAAKLPP--GE------SGLVAldwfngnrt 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 376 PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTS-NKILMQLQADILYIPVVK 454
Cdd:cd07781 361 PLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAEkNPLWMQIYADVLGRPIKV 439
|
....*..
gi 659066190 455 PSMPETT 461
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; ... |
15-461 |
2.82e-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: 118.20 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNsKTAELLSHHQVE-IKQEFPR-EGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVSN 92
Cdd:cd07775 4 ALDAGTGSGRAVIFD-LEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALK---KAGIAPKSIAAISTTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 93 QRETTVVWDKvTGEPLYnAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLStyFSAV-KLRWLLDNVKKVQEAVeen 171
Cdd:cd07775 80 MREGIVLYDN-EGEEIW-ACANVDARAAEEVSELKELYNTLEEEVYRISGQTFA--LGAIpRLLWLKNNRPEIYRKA--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 172 rALFGTIDSWLIWSLTGGIhggvhCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKA 251
Cdd:cd07775 153 -AKITMLSDWIAYKLSGEL-----AVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 252 GALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKcVFSEHGLLTTVAYKLgrdkPVYYALEGSVAIA 331
Cdd:cd07775 227 GLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAP-VTDPAMNIRVNCHVI----PDMWQAEGISFFP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 332 GAVIRWLRDNLGI----------IKSSEEIEKLAKEVGTsyGCY-FVPAFSGL--YApYWEPSARGIIcGLTQFTNKCHI 398
Cdd:cd07775 302 GLVMRWFRDAFCAeekeiaerlgIDAYDLLEEMAKDVPP--GSYgIMPIFSDVmnYK-NWRHAAPSFL-NLDIDPEKCNK 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659066190 399 A--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 461
Cdd:cd07775 378 AtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEAT 443
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-462 |
6.62e-26 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 110.89 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 17 DQGTSSTRFLVFNSKTAELLSHHQ---VEIKQEFPRegWVEQDPKEILQSVYECIEKTCEKLGQlnidiSNIKAIGVsnq 93
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTpnaSDIAAENSD--WHQWSLDAILQRFADCCRQINSELTE-----CHIRGITV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 94 reTT-----VVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTG-LPLSTYFsavKLRWLldnvkkvqea 167
Cdd:PRK10331 78 --TTfgvdgALVDK-QGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGaFSFNTLY---KLVWL---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 168 vEENRA-LFGTIDSWL-IWSLTGGIHGGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKI 245
Cdd:PRK10331 142 -KENHPqLLEQAHAWLfISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 246 SHSLKAGALEGVPISGCLGDQSAALVGQMCFQDgQAKNTYGTGCFLLCNTGH---KCVFSEHGLLTTVAYKLGRDKPvyy 322
Cdd:PRK10331 221 SAAALLGLPVGIPVISAGHDTQFALFGSGAGQN-QPVLSSGTWEILMVRSAQvdtSLLSQYAGSTCELDSQSGLYNP--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 323 aleGSVAIAGAVIRWLRDNLGiikSSEE-----IEKlAKEVGT-SYGCYFVPAFSGlyapywepSARGIICGLTQFTNKC 396
Cdd:PRK10331 297 ---GMQWLASGVLEWVRKLFW---TAETpyqtmIEE-ARAIPPgADGVKMQCDLLA--------CQNAGWQGVTLNTTRG 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659066190 397 HIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 462
Cdd:PRK10331 362 HFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTV 427
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
16-447 |
8.07e-22 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 98.50 E-value: 8.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 16 VDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVyeciEKTCEKLGQLNiDISNIKAIGVSNQRE 95
Cdd:PRK15027 5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQWWQAT----DRAMKALGDQH-SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 96 TTVVWDKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNnnfvKSKTGLPLSTYFSAVKLRWlldnVKKVQEAVEENRALF 175
Cdd:PRK15027 79 GATLLDA-QQRVLRPAILWNDGRCAQECALLEARVPQS----RVITGNLMMPGFTAPKLLW----VQRHEPEIFRQIDKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 176 GTIDSWLIWSLTggihgGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMkISHSLKAGALE 255
Cdd:PRK15027 150 LLPKDYLRLRMT-----GEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGAL-LPEVAKAWGMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 256 GVPISGCLGDQSAALVGQMCFQDGQAKNTYGTgcfllcnTGHKCVFSEhGLLT---TVAYKLGRDKPVYYALEGSVAIAG 332
Cdd:PRK15027 224 TVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE-GFLSkpeSAVHSFCHALPQRWHLMSVMLSAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 333 AVIRW------LRDNLGIIKSSEEIEKLAKEVgtsygcYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAV 406
Cdd:PRK15027 296 SCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 659066190 407 CFQTREILDAMNrDCGIPLSHLQVDGGMTSNKILMQLQADI 447
Cdd:PRK15027 370 GYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
16-460 |
2.57e-21 |
|
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: 97.31 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 16 VDQGTSSTRFLVFNSKTAELLSHHQVEIKQ-EFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKAIGVSN-- 92
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDAtc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 93 -----QRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLskripgnnNFVKSKTGLP-----LSTYFSAVKLRWLLDNVK 162
Cdd:cd07768 82 slaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWI--------NMQCPQQLLDylggkISPEMGVPKLKYFLDEYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 163 KVQEAVEEnraLFGTIDsWLIWSLTGGIHGGVhCTDVTNASrtmlFNIHSLEWDKELCEFFGIPME------ILPNVRSS 236
Cdd:cd07768 154 HLRDKHFH---IFDLHD-YIAYELTRLYEWNI-CGLLGKEN----LDGEESGWSSSFFKNIDPRLEhltttkNLPSNVPI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 237 SEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVgqmcfqdGQAKNTYGTGCFLLCNTGhkcvfSEHGLLTTVAYKL-G 315
Cdd:cd07768 225 GTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASWF-------AVASPHLETSLFMIAGTS-----SCHMYGTTISDRIpG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 316 RDKPVYYAL-------EGSVAIAGAVIRWL-------RDNLGIIKSSEEI--------EKLAKEVGTSYGCYFVPAFSGL 373
Cdd:cd07768 293 VWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleqtiRQIEKNNGLSIHILTLDMFFGN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 374 YAPYWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQADILYI 450
Cdd:cd07768 373 RSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNV 451
|
490
....*....|
gi 659066190 451 PVVKPSMPET 460
Cdd:cd07768 452 AIIKPKENMM 461
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
15-460 |
4.99e-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: 93.37 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVsnqr 94
Cdd:cd07782 4 GVDVGTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAG---VDPEQVKGIGF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 95 ETT---VVWDK--------VTGEPLYNAVVWLDLRTQSTVEnlskRIpgnnnfvkSKTGLPLSTYFSAV--------KLR 155
Cdd:cd07782 76 DATcslVVLDAegkpvsvsPSGDDERNVILWMDHRAVEEAE----RI--------NATGHEVLKYVGGKispemeppKLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 156 WLldnvKKVQEAVEENRALFGTIDSWLIWSLTGgihggvhctdvtNASR---------TMLFNIHSLE-WDKELCEFFG- 224
Cdd:cd07782 144 WL----KENLPETWAKAGHFFDLPDFLTWKATG------------SLTRslcslvckwTYLAHEGSEGgWDDDFFKEIGl 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 225 ----------IPMEILPNVRSSSEiyGLmkishSLKA----GALEGVPIS--------GCLGDQSAALVGQMC-FQDGQA 281
Cdd:cd07782 208 edlvednfakIGSVVLPPGEPVGG--GL-----TAEAakelGLPEGTPVGvslidahaGGLGTLGADVGGLPCeADPLTR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 282 KntygtgCFLLCNTG--HkCVFSEHGLLttVA-----YKlGRDKPVYYALEGSVAIAGAVIRWlrdnlgIIKS---SEEI 351
Cdd:cd07782 281 R------LALICGTSscH-MAVSPEPVF--VPgvwgpYY-SAMLPGLWLNEGGQSATGALLDH------IIEThpaYPEL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 352 EKLAKEVGTSY------------------------GCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIA---FAALE 404
Cdd:cd07782 345 KEEAKAAGKSIyeylnerleqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLAllyLATLQ 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 659066190 405 AVCFQTREILDAMNRdCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 460
Cdd:cd07782 425 ALAYGTRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
15-453 |
1.76e-17 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 85.27 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLV--FNSKTAELL-----SHHQVEIKQefpREGWveqDPKEILQSVYECIEKTCEKLGQlnidisnIKA 87
Cdd:cd07771 4 AVDLGASSGRVILgsLDGGKLELEeihrfPNRPVEING---HLYW---DIDRLFDEIKEGLKKAAEQGGD-------IDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 88 IGVsnqreTTvvW-------DKvTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLldn 160
Cdd:cd07771 71 IGI-----DT--WgvdfgllDK-NGELLGNPVHYRDPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 161 vkkvqeaVEENRALFGTIDSWLI------WSLTGGIhggvhCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVR 234
Cdd:cd07771 138 -------KKEGPELLERADKLLMlpdllnYLLTGEK-----VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 235 SSSEIYGLMKISHSlKAGALEGVP-ISGCLGDQSAALVGQMCFQDGQAkntygtgcFLLCNT----GhkcVFSEHGLLTT 309
Cdd:cd07771 206 PPGTVLGTLKPEVA-EELGLKGIPvIAVASHDTASAVAAVPAEDEDAA--------FISSGTwsliG---VELDEPVITE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 310 VAYKLGrdkpvyYALEGSVA--------IAGaviRWL----RDNL---GIIKSSEEIEKLAKEVgTSYGCYFVPAFSGLY 374
Cdd:cd07771 274 EAFEAG------FTNEGGADgtirllknITG---LWLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 375 APywePSARGIICGLTQFTN------KCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADIL 448
Cdd:cd07771 344 NP---GDMPEAIRAYCRETGqpvpesPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADAT 420
|
....*
gi 659066190 449 YIPVV 453
Cdd:cd07771 421 GLPVI 425
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-464 |
9.03e-16 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 80.16 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 5 KKAVLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQ------EFPREGWVEQDPKEILQSVYECIektCEKLGQL 78
Cdd:COG1069 1 EKYVIG-----VDFGTDSVRAVVVDAADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAV---REALAQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 79 NIDISNIKAIGVSNQRETTVVWDKvTGEPL-----------YNAVVWLDLRTQSTVEnlskRIpgnnNFVKSKTGLPLST 147
Cdd:COG1069 73 GVDPADVVGIGVDATGCTPVPVDA-DGTPLallpefaenphAMVILWKDHTAQEEAE----RI----NELAKARGEDYLR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 148 Y---------FSAvKLRWLLdnvkkvqeavEENRALFGTIDS------WLIWSLTGGIHGGVhCTdvtnASRTMLFNIHS 212
Cdd:COG1069 144 YvggiissewFWP-KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRSR-CT----AGHKALWHAHE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 213 LEWDKElcEFF---GIPMEILPNvRSSSEIYGLmkishSLKAGAL-----------EGVPISGCLGDQSAALVGQMCFQD 278
Cdd:COG1069 208 GGYPSE--EFFaalDPLLDGLAD-RLGTEIYPL-----GEPAGTLtaewaarlglpPGTAVAVGAIDAHAGAVGAGGVEP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 279 GQ-AKNtYGT-GCFLLCNTGHKC-------VFSehGLLttvayklgrdkPVYYALEGSVAIAGAVIRWLRDNLGiikSSE 349
Cdd:COG1069 280 GTlVKV-MGTsTCHMLVSPEERFvpgicgqVDG--SIV-----------PGMWGYEAGQSAVGDIFAWFVRLLV---PPL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 350 EIEKLAKEVGTS----------------YGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREI 413
Cdd:COG1069 343 EYEKEAEERGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAI 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 659066190 414 LDAMNrDCGIPLSHLQVDGG-MTSNKILMQLQADILYIPVVKPSMPETTALG 464
Cdd:COG1069 423 IERFE-EEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALG 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-264 |
3.30e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 68.88 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPR-EGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSNQ 93
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 94 RETTVVWDKvTGEPLYnAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLStyFSAV-KLRWLldnvKKVQEAVEENR 172
Cdd:PRK10939 84 REGIVLYDR-NGTEIW-ACANVDARASREVSELKELHNNFEEEVYRCSGQTLA--LGALpRLLWL----AHHRPDIYRQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 173 ALFGTIDSWLIWSLTGGIhggvhCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAG 252
Cdd:PRK10939 156 HTITMISDWIAYMLSGEL-----AVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETG 230
|
250 260
....*....|....*....|
gi 659066190 253 ALEGVPI--------SGCLG 264
Cdd:PRK10939 231 LRAGTPVvmgggdvqLGCLG 250
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
16-454 |
2.30e-08 |
|
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: 56.64 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 16 VDQGTSSTRFLVFNSKTaELLSHHQVEI-KQEFPREGW-VEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKA---IGV 90
Cdd:cd07778 5 IDVGSTSVRIGIFDYHG-TLLATSERPIsYKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSAtcsMVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 91 SNQRETTVVWDKVTGEPLY-----NAVVWLDLRTQSTVENLskripgNNNFVKSKTGLPLSTYF---SAVKLRWLLDNVK 162
Cdd:cd07778 84 MQRDSDTSYLVPYNVIHEKsnpdqDIIFWMDHRASEETQWL------NNILPDDILDYLGGGFIpemAIPKLKYLIDLIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 163 kvqEAVEENRALFGTIDsWLIWSL-TGGIHGGVhcTDVTNASRTMLFNIHSLE-WDKELCEFFGIPMEILPNVRSSSEIY 240
Cdd:cd07778 158 ---EDTFKKLEVFDLHD-WISYMLaTNLGHSNI--VPVNAPPSIGIGIDGSLKgWSKDFYSKLKISTKVCNVGNTFKEAP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 241 GLM----KISH-SLKAGALEGVPIS-----GCLgDQSAALVGQMC---FQDGQAKNTYGTG-CFLLcntGHKCV------ 300
Cdd:cd07778 232 PLPyagiPIGKvNVILASYLGIDKStvvghGCI-DCYAGWFSTFAaakTLDTTLFMVAGTStCFLY---ATSSSqvgpip 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 301 -----FSEhgllttvaykLGRDKPVYyalEGSVAIAG-----------AVIRWLRDNLGIIKSSEE-IEKLAKEVGTS-- 361
Cdd:cd07778 308 giwgpFDQ----------LLKNYSVY---EGGQSATGklieklfnshpAIIELLKSDANFFETVEEkIDKYERLLGQSih 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 362 --YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTNKCHIAF---AALEAVCFQTREILDAMNRDCgIPLSHLQVDG 432
Cdd:cd07778 375 ylTRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQTKLIIDNFQKEK-IIIQKVVISG 450
|
490 500
....*....|....*....|..
gi 659066190 433 GMTSNKILMQLQADILYIPVVK 454
Cdd:cd07778 451 SQAKNARLLQLLSTVLSKIHII 472
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
383-464 |
1.89e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 44.07 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659066190 383 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGM-TSNKILMQLQADILYIPV-VKPSmPET 460
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475
|
....
gi 659066190 461 TALG 464
Cdd:PRK04123 476 PALG 479
|
|
| |
