|
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; ... |
11-544 |
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: 976.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 91 SNQRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFVKSKTG 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAI----------------------------VWLDTRTSDTVEELSAKTPGGKDHFRKKTG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 171 LPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEF 250
Cdd:cd07792 132 LPISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 251 FGIPMEILPNVRSSSEIYGLMKIshsvkaGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:cd07792 212 FGIPMSILPEIRSSSEVYGKIAS------GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 331 DHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:cd07792 286 KHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:cd07792 366 RGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTA 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 768032244 491 LGAAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKS 544
Cdd:cd07792 446 LGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
11-547 |
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: 815.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 11 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 91 SNQRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNnnFVKSKTG 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAI----------------------------VWQDRRTASICEELKAEGYGE--FIREKTG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 171 LPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEF 250
Cdd:TIGR01311 127 LPLDPYFSATKLRWLLDNVPGVREAAERGELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLEL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 251 FGIPMEILPNVRSSSEIYGlmkisHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:TIGR01311 204 FGIPREILPEVRSSSEVYG-----YTDPGLLGAEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVIS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 331 DHGLLTTVAYKLGRDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:TIGR01311 279 KHGLLTTVAYQLGGKKPVY-ALEGSVFVAGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:TIGR01311 358 RGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTA 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 768032244 491 LGAAMAAGAAEGVGVWSLEPEDLSAVTmERFEPQINAEESEIRYSTWKKAVMKSMGW 547
Cdd:TIGR01311 438 LGAAYAAGLAVGYWKSLEEIEALWRVE-KTFEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
13-541 |
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: 740.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAG---ISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 93 QRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGLP 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAI----------------------------VWQDRRTADICEELKAK--GLEERIREKTGLP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 173 LSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFG 252
Cdd:cd07769 128 LDPYFSATKIKWILDNVPGARERAERGELLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 253 IPMEILPNVRSSSEIYGlmkisHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDH 332
Cdd:cd07769 205 IPRSMLPEVRPSSEVFG-----YTDPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 333 GLLTTVAYKLgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:cd07769 280 GLLTTIAWQI--GGKVTYALEGSIFIAGAAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:cd07769 358 AIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalg 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 768032244 493 aamaagaaegvgVWSLEPEDLSAVTMER-FEPQINAEESEIRYSTWKKAV 541
Cdd:cd07769 438 aayl--aglavgFWKDLDELASLWQVDKrFEPSMDEEERERLYRGWKKAV 485
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
13-548 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 734.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 93 QRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGLP 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAI----------------------------VWQDRRTADICEELKAD--GLEDLIREKTGLV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 173 LSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFG 252
Cdd:COG0554 131 LDPYFSATKIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 253 IPMEILPNVRSSSEIYGlmkisHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDH 332
Cdd:COG0554 208 IPRSMLPEVRPSSEVFG-----ETDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 333 GLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:COG0554 283 GLLTTIAWGLG-GKVTY-ALEGSIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:COG0554 361 AIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalg 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 768032244 493 aamaagaaegvgVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAVMKSMGWV 548
Cdd:COG0554 441 aayl--aglavgFWK-SLEELAALwkVDRRFEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-548 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 707.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 11 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDISnIKAIGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 91 SNQRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFVKsKTG 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAI----------------------------VWLDTRTYDIVNELTKKYGGSNFFQK-ITG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 171 LPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEF 250
Cdd:PTZ00294 131 LPISTYFSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 251 FGIPMEILPNVRSSSEIYGLMKishSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:PTZ00294 208 FGIPKETLPEIKSSSENFGTIS---GEAVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 331 DHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:PTZ00294 285 KHGLLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTa 490
Cdd:PTZ00294 365 RGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT- 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 491 lGAAMAAGAAEGVGVW-SLEP-EDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSMGWV 548
Cdd:PTZ00294 444 -ALGAALLAGLAVGVWkSLEEvKKLIRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-548 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 693.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQ--LNIDiSNIKAIG 89
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAkgHNVD-SGLKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 90 VSNQRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFVKSKT 169
Cdd:PLN02295 79 ITNQRETTVAWSKSTGRPLYNAI----------------------------VWMDSRTSSICRRLEKELSGGRKHFVETC 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 170 GLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCE 249
Cdd:PLN02295 131 GLPISTYFSATKLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 250 FFGIPMEILPNVRSSSEIYGlmKISHSvkaGALEGVPISGCLGDQSAALVGQMCfQIGQAKNTYGTGCFLLCNTGHKCVF 329
Cdd:PLN02295 211 ALGIPAEILPKIVSNSEVIG--TIAKG---WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 330 SDHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPS 409
Cdd:PLN02295 285 SKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 410 ARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSH-----LQVDGGMTSNKILMQLQADILYIPVVKPS 484
Cdd:PLN02295 365 ARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPA 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032244 485 MPETTalGAAMAAGAAEGVGVWSlePEDLSAVTMER----FEPQINAEESEIRYSTWKKAVMKSMGWV 548
Cdd:PLN02295 445 DIETT--ALGAAYAAGLAVGLWT--EEEIFASEKWKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-548 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 681.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 13 VGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 93 QRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGLP 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAI----------------------------VWQDRRTADICEELKRD--GYEDYIREKTGLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 173 LSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFG 252
Cdd:PRK00047 133 IDPYFSGTKIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 253 IPMEILPNVRSSSEIYGLMKISHsvkaGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDH 332
Cdd:PRK00047 210 IPRSMLPEVRPSSEVYGKTNPYG----FFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSEN 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 333 GLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:PRK00047 286 GLLTTIAWGID-GKVVY-ALEGSIFVAGSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:PRK00047 364 AIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT--- 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032244 493 aamaagaaegvgvwSL--------------EPEDLSAVTME--RFEPQINAEESEIRYSTWKKAVMKSMGWV 548
Cdd:PRK00047 441 --------------ALgaaylaglavgfwkDLDELKEQWKIdrRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
15-541 |
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: 673.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07786 4 AIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 95 ETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLS 174
Cdd:cd07786 80 ETTVVWDRETGKPVYNAI----------------------------VWQDRRTADICEELKAE--GHEEMIREKTGLVLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 175 TYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd07786 130 PYFSATKIRWILDNVPGARERAERGELAFGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 255 MEILPNVRSSSEIYGlmkisHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGL 334
Cdd:cd07786 207 ASMLPEVKPSSEVFG-----YTDPDLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 335 LTTVAYKLGrdKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGII 414
Cdd:cd07786 282 LTTIAWQLG--GKVTYALEGSIFIAGAAVQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 415 CGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL--- 491
Cdd:cd07786 360 FGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALgaa 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 768032244 492 -----GAAMAAGAAEGVGVWSLEpedlsavtmERFEPQINAEESEIRYSTWKKAV 541
Cdd:cd07786 440 ylaglAVGLWKSLDELAKLWQVD---------RRFEPSMSEEEREALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
15-541 |
3.93e-145 |
|
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: 427.75 E-value: 3.93e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07793 4 AVDVGTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAG---LTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 95 ETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSK---------------RIP 159
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFI----------------------------TWQDLRAAELCESWNRslllkalrggskflhFLT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 160 GNNNFVKSKTgLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIH 239
Cdd:cd07793 132 RNKRFLAASV-LKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 240 SLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSVKAgalegVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFL 319
Cdd:cd07793 208 TLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGAE-----IPITAVVADQQAALFGECCFDKGDVKITMGTGTFI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 320 LCNTGHKCVFSDHGLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIiKTSEEIEKLAKEVGTSYGCYFVPAFS 399
Cdd:cd07793 283 DINTGSKPHASVKGLYPLVGWKIG-GEITY-LAEGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 400 GLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIP 479
Cdd:cd07793 360 GLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKP 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032244 480 VVKPSMPETTalGAAMAAGAAEGVGVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAV 541
Cdd:cd07793 440 VERPKNTEMS--ALGAAFLAGLASGIWK-SKEELKKLrkIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-300 |
4.17e-108 |
|
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: 323.52 E-value: 4.17e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEklgQLNIDISNIKAIGVS 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLS---QLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 92 NQRETTVVWDKITgEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKriPGNNNFVKSKTGL 171
Cdd:pfam00370 77 NQGHGTVLLDKND-KPLYNAI----------------------------LWKDRRTAEIVENLKE--EGNNQKLYEITGL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 172 PLSTYFSAVKLRWLLDNVRKVQKAVEekraLFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFF 251
Cdd:pfam00370 126 PIWPGFTLSKLRWIKENEPEVFEKIH----KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAAL 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 768032244 252 GIPMEILPNVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVG 300
Cdd:pfam00370 197 GIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-489 |
1.26e-89 |
|
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: 284.42 E-value: 1.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 6 KAVLGplvgaVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNI 85
Cdd:COG1070 1 KYVLG-----IDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAG---VDPEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 86 KAIGVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFv 165
Cdd:COG1070 72 AAIGVSGQMHGLVLLDA-DGEPLRPAI----------------------------LWNDTRAAAEAAELREELGEEALY- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 166 kSKTGLPLSTYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDK 245
Cdd:COG1070 122 -EITGNPLHPGFTAPKLLWLKEN----EPEIFARIAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 246 QLCEFFGIPMEILPNVRSSSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNT 323
Cdd:COG1070 192 ELLEALGIDRELLPELVPPGEVAG--TLTAEAAAetGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 324 GHKcVFSDHGLLTTVAYKL-GRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKTS--EEIEKLAKEVGT-SYGCYFVPAFS 399
Cdd:COG1070 270 DKP-LPDPEGRVHTFCHAVpGR-----WLPMGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 400 GLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIP 479
Cdd:COG1070 344 GERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRP 422
|
490
....*....|
gi 768032244 480 VVKPSMPETT 489
Cdd:COG1070 423 VEVPEAEEGG 432
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
15-489 |
4.33e-86 |
|
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: 273.24 E-value: 4.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07779 4 GIDVGTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 95 ETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTqstveslskripgnnnfvksktglpls 174
Cdd:cd07779 80 STFVPVDE-DGRPLRPAI----------------------------SWQDKRT--------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 175 tyfsavklrwlldnvrkvqkaveekrALFGTIDSWLIWSLTggvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd07779 104 --------------------------AKFLTVQDYLLYRLT-----GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGID 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 255 MEILPNVRSSSEIYGlmKISHSV--KAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTgHKCVFSDH 332
Cdd:cd07779 153 RDKLPELVPPGTVIG--TLTKEAaeETGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 333 GLLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLG---------IIKTSEEIEKLAKEVGT-SYGCYFVPAFSGLY 402
Cdd:cd07779 230 RRIPCNPSAV----PGKWVLEGSINTGGSAVRWFRDEFGqdevaekelGVSPYELLNEEAAKSPPgSDGLLFLPYLAGAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 403 APYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVK 482
Cdd:cd07779 306 TPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVER 384
|
....*..
gi 768032244 483 PSMPETT 489
Cdd:cd07779 385 PETSEAT 391
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
15-489 |
9.54e-86 |
|
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: 271.36 E-value: 9.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAG---IDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 95 ETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDlrtqstveslskripgnnnfvksktglpls 174
Cdd:cd00366 80 PGVVLVDA-DGNPLRPAI----------------------------IWLD------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 175 tyfsavklrwlldnvrkvqkaveeKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd00366 101 ------------------------RRAKFLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIP 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 255 MEILPNVRSSSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGhKCVFSDH 332
Cdd:cd00366 152 REKLPPIVESGEVVG--RVTPEAAEetGLPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDP 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 333 GLLTTVAYKLGRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKTSEE----IEKLAKEVGT-SYGCYFVPAFSGLYAPYWE 407
Cdd:cd00366 229 RLLNRCHVVPGL-----WLLEGAINTGGASLRWFRDEFGEEEDSDAeyegLDELAAEVPPgSDGLIFLPYLSGERSPIWD 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 408 PSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 487
Cdd:cd00366 304 PAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAE 382
|
..
gi 768032244 488 TT 489
Cdd:cd00366 383 GA 384
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-489 |
1.88e-77 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 251.35 E-value: 1.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 12 LVGaVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQlnidiSNIKAIGVS 91
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 92 NQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFvkSKTGL 171
Cdd:cd07773 75 SQGESGVPVDR-DGEPLGPAI----------------------------VWFDPRGKEEAEELAERIGAEELY--RITGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 172 PLSTYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFF 251
Cdd:cd07773 124 PPSPMYSLAKLLWLREH----EPEIFAKAAKWLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 252 GIPMEILPNVRSSSEIYGLMKISHSVKAGALEGVPIsgCLG--DQSAALVGQMCFQIGQAKNTYGTG-CFLLC-NTGHKC 327
Cdd:cd07773 195 GIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPV--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 328 VFSDHGLLTTVAYKLGRdkpvYYALEGSVAiAGAVIRWLRDNLGI--IKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPY 405
Cdd:cd07773 273 EMLAEGGLSYGHHVPGG----YYYLAGSLP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 406 WEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSM 485
Cdd:cd07773 348 FDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426
|
....
gi 768032244 486 PETT 489
Cdd:cd07773 427 PEAT 430
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-489 |
7.04e-75 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 245.53 E-value: 7.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 8 VLGplvgaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07808 2 LLG-----IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 88 IGVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPgnnNFVKS 167
Cdd:cd07808 73 IGLTGQMHGLVLLDK-NGRPLRPAI----------------------------LWNDQRSAAECEELEARLG---DEILI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 168 KTGLPLSTYFSAVKLRWLL----DNVRKVQKAVEEKralfgtiDsWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEW 243
Cdd:cd07808 121 ITGNPPLPGFTLPKLLWLKenepEIFARIRKILLPK-------D-YLRYRLTG-----ELATDPSDASGTLLFDVEKREW 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 244 DKQLCEFFGIPMEILPNVRSSSEIYGlmKISHSVkAGAL---EGVP-ISGClGDQSAALVGQMCFQIGQAKNTYGTGCFL 319
Cdd:cd07808 188 SEELLEALGLDPSILPPIVESTEIVG--TLTPEA-AEELglpEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 320 LCNTgHKCVFSDHGLLTTVAYKLGrdkPVYYALeGSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEVG-TSYGCYFVPA 397
Cdd:cd07808 264 FAPT-DKPVPDPKGRLHTFPHAVP---GKWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 398 FSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILY 477
Cdd:cd07808 339 LSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLG 417
|
490
....*....|..
gi 768032244 478 IPVVKPSMPETT 489
Cdd:cd07808 418 VPVVVPAEEEGS 429
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
15-489 |
4.60e-69 |
|
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: 230.14 E-value: 4.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDisnikAIGVSNQR 94
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVD-----AIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 95 ETTVVWDKiTGEPLynavaAPVSPgpsvpvavvpsgssvpapgtssvWLDLRTQSTVESLSKRIPGNNnfVKSKTGLPLS 174
Cdd:cd07770 78 HSLLGVDE-DGEPL-----TPVIT-----------------------WADTRAAEEAERLRKEGDGSE--LYRRTGCPIH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 175 TYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd07770 127 PMYPLAKLLWLKEE----RPELFAKAAKFVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGID 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 255 MEILPNVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTgcfllcnTGHKCVFSDHGL 334
Cdd:cd07770 198 EEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 335 LT----TVAYKLGRDKPVyyaLEGSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEP 408
Cdd:cd07770 271 LDppgrLWCYRLDENRWL---VGGAINNGGNVLDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 409 SARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07770 348 DARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEA 426
|
.
gi 768032244 489 T 489
Cdd:cd07770 427 S 427
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-484 |
2.65e-65 |
|
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: 219.70 E-value: 2.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 12 LVGaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAG---ISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 92 NQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFvkSKTGL 171
Cdd:cd07804 77 GLVPALVPVDE-NGKPLRPAI----------------------------LYGDRRATEEIEWLNENIGEDRIF--EITGN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 172 PLSTYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTM-LFNIHSLEWDKQLCEF 250
Cdd:cd07804 126 PLDSQSVGPKLLWIKRN----EPEVFKKTRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 251 FGIPMEILPNVRSSSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALV-------GQMCFQIGqakntyGTGCFLLC 321
Cdd:cd07804 197 LGIDPDLLPELVPSTEIVG--EVTKEAAEetGLAEGTPVVAGTVDAAASALsagvvepGDLLLMLG------TAGDIGVV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 322 ntgHKCVFSDHGLLTTVAyklgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEE----------IEKLAKEVG-TSY 390
Cdd:cd07804 269 ---TDKLPTDPRLWLDYH-----DIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEksggdsaydlLDEEAEKIPpGSD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 391 GCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQ 470
Cdd:cd07804 341 GLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQ 419
|
490
....*....|....
gi 768032244 471 LQADILYIPVVKPS 484
Cdd:cd07804 420 IVADVTGVPQEYVK 433
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
15-487 |
1.83e-59 |
|
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: 205.06 E-value: 1.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTrflvfnsKTA------ELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECiekTCEKLGQLNIDISNIKAI 88
Cdd:cd07805 4 AIDLGTSGV-------KAAlvdldgELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 89 GVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNnFVKSK 168
Cdd:cd07805 74 AFSGQMQGVVPVDK-DGNPLRNAI----------------------------IWSDTRAAEEAEEIAGGLGGIE-GYRLG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 169 TGLPLSTYFSAVKLRWLLDN----VRKVQKaveekraLFGTIDsWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWD 244
Cdd:cd07805 124 GGNPPSGKDPLAKILWLKENepeiYAKTHK-------FLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 245 KQLCEFFGIPMEILPNVRSSSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAkNTY-GTGCFLLC 321
Cdd:cd07805 191 EELLRAAGIDPDKLPELVPSTEVVG--ELTPEAAAelGLPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 322 NTGHKCVFSDHGlLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLGIIKTS-----EEIEKLAKEVGT-SYGCYFV 395
Cdd:cd07805 268 HVPKPKTDPDHG-IFTLASAD----PGRYLLAAEQETAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 396 PAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGiPLSHLQVDGGMTSNKILMQLQADI 475
Cdd:cd07805 343 PWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADV 421
|
490
....*....|..
gi 768032244 476 LYIPVVKPSMPE 487
Cdd:cd07805 422 LGRPVEVPENPQ 433
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
309-492 |
2.05e-45 |
|
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: 158.64 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 309 AKNTYGTGCFLLCNTGHKCVFSdHGLLTTVAyklGRDKPVYYALEGSVAIAGAVIRWLRDNLGI---------IKTSEEI 379
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSV-HGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 380 EKLAKEVGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVD 459
Cdd:pfam02782 77 AALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190
....*....|....*....|....*....|...
gi 768032244 460 GGMTSNKILMQLQADILYIPVVKPSMPETTALG 492
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-489 |
1.00e-43 |
|
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: 161.18 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 12 LVGaVDQGTSSTRFLVFNSKTAELLSHHqVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSG---VDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 92 NQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGL 171
Cdd:cd07802 77 GHGNGLYLVDK-DGKPVRNAI----------------------------LSNDSRAADIVDRWEED--GTLEKVYPLTGQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 172 PLSTYFSAVKLRWLLDN----VRKVQKAVEEKralfgtiDsWLIWSLTggvngGVHCTDVTNASrTMLFNIHSLEWDKQL 247
Cdd:cd07802 126 PLWPGQPVALLRWLKENeperYDRIRTVLFCK-------D-WIRYRLT-----GEISTDYTDAG-SSLLDLDTGEYDDEL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 248 CEFFGIP--MEILPNVRSSSEIYGlmKISHSVKA--GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCfllCNT 323
Cdd:cd07802 192 LDLLGIEelKDKLPPLVPSTEIAG--RVTAEAAAltGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 324 G--HKCVFSDHGLLTTvaykLGRDKPVYYALEGSVAIAGaVIRWLRDNLG------IIKTSEEIEKLAKEVG-TSYGCYF 394
Cdd:cd07802 267 VvtDEPVVPDSVGSNS----LHADPGLYLIVEASPTSAS-NLDWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 395 VPaFsgLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCgiPLSHLQVDGGMTSNKILMQLQAD 474
Cdd:cd07802 342 LP-Y--LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFAD 416
|
490
....*....|....*
gi 768032244 475 ILYIPVVKPSMPETT 489
Cdd:cd07802 417 VLGLPVEVPDGEELG 431
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
15-488 |
1.07e-42 |
|
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: 158.15 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLgqlniDISNIKAIGVSNQR 94
Cdd:cd07783 4 GIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 95 ETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPgnnnFVKSKTGLPLS 174
Cdd:cd07783 78 GTLVLVDR-EGEPLRPAI----------------------------MYNDARAVAEAEELAEAAG----AVAPRTGLAVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 175 TYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGGVNggvhCTDVTNASRTmLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd07783 125 PSSSLAKLLWLKRH----EPEVLAKTAKFLHQADWLAGRLTGDRG----VTDYNNALKL-GYDPETGRWPSWLLALLGIP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 255 MEILPNVRSSSEIYGLMKISHSVKAGALEGVPIsgCLG--DQSAALVGQMCFQIGQAKNTYGTG-CF-LLCntgHKCVFS 330
Cdd:cd07783 196 PDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLkLLS---DKRVPD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 331 DHGLLTTvaYKLGRDkpvYYALEGSVAIAGAVIRWL--RDNLgiiktsEEIEKLAKEVGTSyGCYFVP-AFSGLYAPYWE 407
Cdd:cd07783 271 PGGGVYS--HRHGDG---YWLVGGASNTGGAVLRWFfsDDEL------AELSAQADPPGPS-GLIYYPlPLRGERFPFWD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 408 PSARGIICGLTqfTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 487
Cdd:cd07783 339 PDARGFLLPRP--HDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE 416
|
.
gi 768032244 488 T 488
Cdd:cd07783 417 A 417
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
15-489 |
1.23e-40 |
|
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: 152.76 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGW-VEQDPKEILHSVYECIEKTcekLGQLNIDISNIKAIGVSNQ 93
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDaKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 94 RETTVVWDKiTGEPLYNavaapvspGPSVpvavvpsgssvpapgtssvwlDLRTQSTVESLSKRIPgnnNFVKSKTGLPL 173
Cdd:cd07798 81 REGIVFLDK-DGRELYA--------GPNI---------------------DARGVEEAAEIDDEFG---EEIYTTTGHWP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 174 STYFSAVKLRWLldnvRKVQKAVEEKRALFGTIDSWLIWSLTGGVnggvhCTDVTNASRTMLFNIHSLEWDKQLCEFFGI 253
Cdd:cd07798 128 TELFPAARLLWF----KENRPEIFERIATVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 254 PMEILPNVRSSSEIYGlmKISHSVKA--GALEGVPISGCLGD-QSAALvgqmcfqigqakntyGTGCFllcNTGHKCVFS 330
Cdd:cd07798 199 PPEILPEIVPSGTVLG--TVSEEAARelGLPEGTPVVVGGADtQCALL---------------GSGAI---EPGDIGIVA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 331 dhGllTTVAYKLGRDKPVY----------------YALEGSVAIAGAVIRWLRDNL--GIIKTSEEIEKLAKEVG-TSYG 391
Cdd:cd07798 259 --G--TTTPVQMVTDEPIIdperrlwtgchlvpgkWVLESNAGVTGLNYQWLKELLygDPEDSYEVLEEEASEIPpGANG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 392 CYfvpAFSGLYAPYwePSARGIICGLTQFT--------NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMT 463
Cdd:cd07798 335 VL---AFLGPQIFD--ARLSGLKNGGFLFPtplsaselTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGS 409
|
490 500
....*....|....*....|....*.
gi 768032244 464 SNKILMQLQADILYIPVVKPSMPETT 489
Cdd:cd07798 410 RSALLCQILADVLGKPVLVPEGREAS 435
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
8-488 |
5.50e-32 |
|
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: 128.44 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07809 2 VLG-----IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 88 IGVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNnfvKS 167
Cdd:cd07809 74 IGISGQMHGLVALDA-DGKVLRPAK----------------------------LWCDTRTAPEAEELTEALGGKK---CL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 168 KTGLPLSTYFSAVKLRWLLDN----VRKVQKaveekralFGTIDSWLIWSLTGGvnggvHCTDVTNASRTMLFNIHSLEW 243
Cdd:cd07809 122 LVGLNIPARFTASKLLWLKENepehYARIAK--------ILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDY 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 244 DKQLCEFF---GIPMEILPNVRSSSEIYGlmkisHSVKAGALE-----GVPISGCLGDQSAALVGQMCFQIGQAKNTYGT 315
Cdd:cd07809 189 DAELLAAIdpsRDLRDLLPEVLPAGEVAG-----RLTPEGAEElglpaGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 316 -GCflLCNTGHKCVFSDHGLLTTVAyklgrDKPVYYALegSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEV-GTSYGC 392
Cdd:cd07809 264 sGT--AYGVSDKPVSDPHGRVATFC-----DSTGGMLP--LINTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 393 YFVPAFSGLYAPYWePSARGIICGLTQF-TNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQL 471
Cdd:cd07809 335 LLLPFLNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQI 412
|
490
....*....|....*..
gi 768032244 472 QADILYIPVVKPSMPET 488
Cdd:cd07809 413 LADVFGVPVVVPETGEG 429
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-489 |
1.66e-25 |
|
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: 109.23 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNSKTAELLS----HHQVEIKQEFPreGWVEQDPKEILHSVYECIEKTCEKLGqlnidiSNIKAIGV 90
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILEsvsrPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 91 SNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgTssvWLDLRtqSTVESLSKRIPGNNNFvKSKTG 170
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLI-------------------------T---WQDQR--CSEEFLGGLSTYGEEL-LPKSG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 171 LPLSTYFSAVKLRWLLdnvrkVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEF 250
Cdd:cd07777 124 MRLKPGYGLATLFWLL-----RNGPLPSKADRAGTIGDYIVARLTGL---PKPVMHPTNAASWGLFDLETGTWNKDLLEA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 251 FGIPMEILPNVRSSSEIYGlmKISHSVKAgaleGVPISGCLGDQSAALVGqmCFQIGqaKNT----YGTG---CFLLC-N 322
Cdd:cd07777 196 LGLPVILLPEIVPSGEIVG--TLSSALPK----GIPVYVALGDNQASVLG--SGLNE--ENDavlnIGTGaqlSFLTPkF 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 323 TGHKCV----FSDHGLLTTVAyKL--GRdkpVYYALEGSVAiagaviRWLRDnLGIIKTSEEI-EKLAKEVGTSYGC--Y 393
Cdd:cd07777 266 ELSGSVeirpFFDGRYLLVAA-SLpgGR---ALAVLVDFLR------EWLRE-LGGSLSDDEIwEKLDELAESEESSdlS 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 394 FVPAFSGlyaPYWEPSARGIICGLTQ--FTNKcHIAFAALEAVCfqtREILDAMNRDC--GIPLSHLQVDGGM-TSNKIL 468
Cdd:cd07777 335 VDPTFFG---ERHDPEGRGSITNIGEsnFTLG-NLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVL 407
|
490 500
....*....|....*....|.
gi 768032244 469 MQLQADILYIPVVKPSMPETT 489
Cdd:cd07777 408 RRIIEKRFGLPVVLSEGSEEA 428
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-488 |
3.29e-24 |
|
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: 105.40 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 12 LVGaVDQGTSSTRFLVFNSKTAELlSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNidiSNIKAIGVS 91
Cdd:cd24121 2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 92 NQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGL 171
Cdd:cd24121 77 GQGDGTWLVDE-DGRPVRDAI----------------------------LWLDGRAADIVERWQAD--GIAEAVFEITGT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 172 PLSTYFSAVKLRWLLDNvrkVQKAVEEKRALFGTIDsWLIWSLTggvngGVHCTDVTNASRTMlFNIHSLEWDKQLCEFF 251
Cdd:cd24121 126 GLFPGSQAAQLAWLKEN---EPERLERARTALHCKD-WLFYKLT-----GEIATDPSDASLTF-LDFRTRQYDDEVLDLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 252 GIP--MEILPNVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFllcntghkcvf 329
Cdd:cd24121 196 GLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV----------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 330 sdHGLLTTVAYkLGRDKP---VYYALEGSV-----AIAG-AVIRWLRDNLGIIKTSE----------EIEKLAKEV---- 386
Cdd:cd24121 265 --HEVVVDEPD-LEPEGVgytICLGVPGRWlramaNMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppga 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 387 -GTSYGCYFVPAfsGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnrdcGIPLSHLQVDGGMTSN 465
Cdd:cd24121 342 eGVLYHPYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARS 415
|
490 500
....*....|....*....|...
gi 768032244 466 KILMQLQADILYIPVVKPSMPET 488
Cdd:cd24121 416 DTWCQILADALGVPVRVPAGEEF 438
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
15-489 |
1.79e-23 |
|
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: 103.57 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNsKTAELLSHHQVE-IKQEFPR-EGWVEQDPKEILHSVYECIEKTCEklgQLNIDISNIKAIGVSN 92
Cdd:cd07775 4 ALDAGTGSGRAVIFD-LEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALK---KAGIAPKSIAAISTTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 93 QRETTVVWDKiTGEPLYnAVAApvspgpsvpvavvpsgssvpapgtssvwLDLRTQSTVESLSKRIPGNNNFVKSKTGLP 172
Cdd:cd07775 80 MREGIVLYDN-EGEEIW-ACAN----------------------------VDARAAEEVSELKELYNTLEEEVYRISGQT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 173 LStyFSAV-KLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFF 251
Cdd:cd07775 130 FA--LGAIpRLLWLKNN----RPEIYRKAAKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 252 GIPMEILPNVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSD 331
Cdd:cd07775 199 GLKADILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 332 HGLLTTVAYklgrDKPVYYAlEGSVAIAGAVIRWLRDNLGI----------IKTSEEIEKLAKEVGTsyGCY-FVPAFSG 400
Cdd:cd07775 279 MNIRVNCHV----IPDMWQA-EGISFFPGLVMRWFRDAFCAeekeiaerlgIDAYDLLEEMAKDVPP--GSYgIMPIFSD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 401 L--YApYWEPSARGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADI 475
Cdd:cd07775 352 VmnYK-NWRHAAPSFL-NLDIDPEKCNKAtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADV 429
|
490
....*....|....
gi 768032244 476 LYIPVVKPSMPETT 489
Cdd:cd07775 430 LGLPVKVPVVKEAT 443
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
8-489 |
8.17e-22 |
|
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: 98.76 E-value: 8.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEF--PREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNI 85
Cdd:cd07781 2 VIG-----IDFGTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAG---VDPEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 86 KAIGVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFV 165
Cdd:cd07781 74 VGIGVDTTSSTVVPVDE-DGNPLAPAI----------------------------LWMDHRAQEEAAEINETAHPALEYY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 166 KSKTGLPLS--TYFSavKLRWLLDNVRKVQKA----VEEkralfgtIDsWLIWSLTGGVNGGVhCtdvtNASRTMLFNIH 239
Cdd:cd07781 125 LAYYGGVYSseWMWP--KALWLKRNAPEVYDAaytiVEA-------CD-WINARLTGRWVRSR-C----AAGHKWMYNEW 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 240 SLEWDKQLCEFFGIPM----EILP-NVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYG 314
Cdd:cd07781 190 GGGPPREFLAALDPGLlklrEKLPgEVVPVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 315 T-GCFLLcnTGHKCVFSDhGLLTTVayklgrDKPV---YYALEGSVAIAGAVIRWLRDNLGI------IKTSEEIEKLAK 384
Cdd:cd07781 270 TsTCHLM--VSPKPVDIP-GICGPV------PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEAA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 385 EVGTsyGCyfvpafSGLYA---------PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSH 455
Cdd:cd07781 341 KLPP--GE------SGLVAldwfngnrtPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNR 411
|
490 500 510
....*....|....*....|....*....|....*
gi 768032244 456 LQVDGGMTS-NKILMQLQADILYIPVVKPSMPETT 489
Cdd:cd07781 412 VVACGGIAEkNPLWMQIYADVLGRPIKVPKSDQAP 446
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-489 |
5.36e-20 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 92.78 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 17 DQGTSSTRFLVFNSKTAELLSHHQ---VEIKQEFPRegWVEQDPKEILHSVYECIEKTCEKLGQlnidiSNIKAIGVsnq 93
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTpnaSDIAAENSD--WHQWSLDAILQRFADCCRQINSELTE-----CHIRGITV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 94 reTT-----VVWDKiTGEPLYnavaapvspgpsvpvavvpsgssvpaPGTSsvWLDLRTQSTVESLSKRIPGNNNFVKSK 168
Cdd:PRK10331 78 --TTfgvdgALVDK-QGNLLY--------------------------PIIS--WKCPRTAAVMENIERYISAQQLQQISG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 169 TG-LPLSTYFsavKLRWLLDNvrkvqkaveeKRALFGTIDSWL-IWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQ 246
Cdd:PRK10331 127 VGaFSFNTLY---KLVWLKEN----------HPQLLEQAHAWLfISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 247 LCEFFGIPMEILPNVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALVGQmcfqiGQAKN----TYGTGCFLLCN 322
Cdd:PRK10331 194 ILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISAGHDTQFALFGS-----GAGQNqpvlSSGTWEILMVR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 323 TGH---KCVFSDHGLLTTVAYKLGRDKPvyyaleGSVAIAGAVIRWLRDNLGiikTSEE-----IEKlAKEVGT-SYGCY 393
Cdd:PRK10331 269 SAQvdtSLLSQYAGSTCELDSQSGLYNP------GMQWLASGVLEWVRKLFW---TAETpyqtmIEE-ARAIPPgADGVK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 394 FVPAFSGlyapywepSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQA 473
Cdd:PRK10331 339 MQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKA 410
|
490
....*....|....*.
gi 768032244 474 DILYIPVVKPSMPETT 489
Cdd:PRK10331 411 NMLDIPIKVLDDAETT 426
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
16-475 |
6.43e-18 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 86.56 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 16 VDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEIlhsvYECIEKTCEKLGQLNiDISNIKAIGVSNQRE 95
Cdd:PRK15027 5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQW----WQATDRAMKALGDQH-SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 96 TTVVWDKitgeplYNAVAAPvspgpsvpvavvpsgssvpapgtSSVWLDLRTQSTVESLSKRIPGNnnfvKSKTGLPLST 175
Cdd:PRK15027 79 GATLLDA------QQRVLRP-----------------------AILWNDGRCAQECALLEARVPQS----RVITGNLMMP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 176 YFSAVKLRWLL----DNVRKVQKAVEEKralfgtidSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFF 251
Cdd:PRK15027 126 GFTAPKLLWVQrhepEIFRQIDKVLLPK--------DYLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQAC 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 252 GIPMEILPNVRSSSEIYGLMkISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTgcfllcnTGHKCVFSD 331
Cdd:PRK15027 193 HLSRDQMPALYEGSEITGAL-LPEVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 332 hGLLT---TVAYKLGRDKPVYYALEGSVAIAGAVIRW------LRDNLGIIKTSEEIEKLAKEVgtsygcYFVPAFSGLY 402
Cdd:PRK15027 265 -GFLSkpeSAVHSFCHALPQRWHLMSVMLSAASCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGER 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032244 403 APYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGGMTSNKILMQLQADI 475
Cdd:PRK15027 338 TPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
16-488 |
3.13e-17 |
|
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: 84.60 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 16 VDQGTSSTRFLVFNSKTAELLSHHQVEIKQ-EFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDATC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 95 eTTVVWDKiTGEPLYnavaapvspgpsvpvavvpsgSSVPAPGTSSV--WLDLRTQSTVESLskripgnnNFVKSKTGLP 172
Cdd:cd07768 82 -SLAIFDR-EGTPLM---------------------ALIPYPNEDNVifWMDHSAVNEAQWI--------NMQCPQQLLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 173 -----LSTYFSAVKLRWLLDNVRKVQKAVEEkraLFGTIDsWLIWSLTGgvnggvhctDVTNASRTMLF--NIHSLE--W 243
Cdd:cd07768 131 ylggkISPEMGVPKLKYFLDEYSHLRDKHFH---IFDLHD-YIAYELTR---------LYEWNICGLLGkeNLDGEEsgW 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 244 DKQLCEFFGIPME------ILPNVRSSSEIYGLMKISHSVKAGALEGVPISGCLGDQSAALvgqmcfqIGQAKNTYGTGC 317
Cdd:cd07768 198 SSSFFKNIDPRLEhltttkNLPSNVPIGTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASW-------FAVASPHLETSL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 318 FLLCNTGhkcvfSDHGLLTTVAYKL-GRDKPVYYAL-------EGSVAIAGAVIRWL-------RDNLGIIKTSEEI--- 379
Cdd:cd07768 271 FMIAGTS-----SCHMYGTTISDRIpGVWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqv 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 380 -----EKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREILDAMNRDcGI 451
Cdd:cd07768 346 leqtiRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GI 424
|
490 500 510
....*....|....*....|....*....|....*..
gi 768032244 452 PLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07768 425 HIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
15-488 |
7.04e-17 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 83.74 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVsnqr 94
Cdd:cd07782 4 GVDVGTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAG---VDPEQVKGIGF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 95 ETT---VVWDKiTGEPlynavaapvspgpsvpVAVVPSGSS----VpapgtssVWLDLRTQSTVEslskRIpgnnnfvkS 167
Cdd:cd07782 76 DATcslVVLDA-EGKP----------------VSVSPSGDDernvI-------LWMDHRAVEEAE----RI--------N 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 168 KTGLPLSTYFSAV--------KLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGGVNGGVhCTDVtnASRTMLFNIH 239
Cdd:cd07782 120 ATGHEVLKYVGGKispemeppKLLWLKEN----LPETWAKAGHFFDLPDFLTWKATGSLTRSL-CSLV--CKWTYLAHEG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 240 SLE-WDKQLCEFFGIPmEILPNVRSsseiyglmKISHSVKAGaleGVPISGCLGDQSAAlvgqmcfQIGQAKNT------ 312
Cdd:cd07782 193 SEGgWDDDFFKEIGLE-DLVEDNFA--------KIGSVVLPP---GEPVGGGLTAEAAK-------ELGLPEGTpvgvsl 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 313 ---Y--GTGCflLCNTGHKCVFSDHGLLTTVAYKLG--------RDKPV--------YY-AL-------EGSVAIAGAVI 363
Cdd:cd07782 254 idaHagGLGT--LGADVGGLPCEADPLTRRLALICGtsschmavSPEPVfvpgvwgpYYsAMlpglwlnEGGQSATGALL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 364 RWlrdnlgIIKT---SEEIEKLAKEVGTSY------------------------GCYFVPAFSGLYAPYWEPSARGIICG 416
Cdd:cd07782 332 DH------IIEThpaYPELKEEAKAAGKSIyeylnerleqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISG 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032244 417 LTQFTNKCHIA---FAALEAVCFQTREILDAMNRdCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07782 406 LTLDTSLDDLAllyLATLQALAYGTRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
144-481 |
1.18e-13 |
|
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: 73.33 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 144 DLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLldnvrkvqkaVEEKRALFGTIDSWLI------WSLTGg 217
Cdd:cd07771 98 DPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL----------KKEGPELLERADKLLMlpdllnYLLTG- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 218 vnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKISHSvKAGALEGVP-ISGCLGDQSA 296
Cdd:cd07771 165 ----EKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVA-EELGLKGIPvIAVASHDTAS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 297 ALVGqmcfqI-GQAKNTYgtgcFLLCNT----GhkcVFSDHGLLTTVAYKLGrdkpvyYALEGSVA--------IAGavi 363
Cdd:cd07771 240 AVAA-----VpAEDEDAA----FISSGTwsliG---VELDEPVITEEAFEAG------FTNEGGADgtirllknITG--- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 364 RWL----RDNL---GIIKTSEEIEKLAKEVgTSYGCYFVPAFSGLYAPywePSARGIICGLTQFTN------KCHIAFAA 430
Cdd:cd07771 299 LWLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFLNP---GDMPEAIRAYCRETGqpvpesPGEIARCI 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 768032244 431 LEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 481
Cdd:cd07771 375 YESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVI 425
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-492 |
2.13e-12 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 69.37 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 5 KKAVLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQ------EFPREGWVEQDPKEILHSVYECIektCEKLGQL 78
Cdd:COG1069 1 EKYVIG-----VDFGTDSVRAVVVDAADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAV---REALAQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 79 NIDISNIKAIGVSNQRETTVVWDKiTGEPLynavaaPVSPGPS-VPVA-VVpsgssvpapgtssVWLDLRTQSTVEslsk 156
Cdd:COG1069 73 GVDPADVVGIGVDATGCTPVPVDA-DGTPL------ALLPEFAeNPHAmVI-------------LWKDHTAQEEAE---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 157 RIpgnnNFVKSKTGLPLSTY---------FSAvKLRWLLdnvrkvqkavEEKRALFGTIDS------WLIWSLTGGVNGG 221
Cdd:COG1069 129 RI----NELAKARGEDYLRYvggiissewFWP-KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 222 VhCTdvtnASRTMLFNIHSLEW-DKqlcEFF---GIPMEILPNvRSSSEIYGLmkishSVKAGAL-----------EGVP 286
Cdd:COG1069 194 R-CT----AGHKALWHAHEGGYpSE---EFFaalDPLLDGLAD-RLGTEIYPL-----GEPAGTLtaewaarlglpPGTA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 287 ISGCLGDQSAALVGqmcfqIGQAKNTY-----GT-GCFLLCNTGHKCVFS-----DHGLLttvayklgrdkPVYYALEGS 355
Cdd:COG1069 260 VAVGAIDAHAGAVG-----AGGVEPGTlvkvmGTsTCHMLVSPEERFVPGicgqvDGSIV-----------PGMWGYEAG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 356 VAIAGAVIRWLRDNLGiikTSEEIEKLAKEVGTS----------------YGCYFVPAFSGLYAPYWEPSARGIICGLTQ 419
Cdd:COG1069 324 QSAVGDIFAWFVRLLV---PPLEYEKEAEERGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTL 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032244 420 FTNKCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGG-MTSNKILMQLQADILYIPVVKPSMPETTALG 492
Cdd:COG1069 401 GTDAEDIYRALVEATAFGTRAIIERFE-EEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALG 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-489 |
4.27e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 55.78 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPR-EGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSNQ 93
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 94 RETTVVWDKiTGEPLYnAVAApvspgpsvpvavvpsgssvpapgtssvwLDLRTQSTVESLSKRIPGNNNFVKSKTGLPL 173
Cdd:PRK10939 84 REGIVLYDR-NGTEIW-ACAN----------------------------VDARASREVSELKELHNNFEEEVYRCSGQTL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 174 StyFSAV-KLRWLldnvRKVQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFG 252
Cdd:PRK10939 134 A--LGALpRLLWL----AHHRPDIYRQAHTITMISDWIAYMLSG-----ELAVDPSNAGTTGLLDLVTRDWDPALLEMAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 253 IPMEILPNVRSSSEIYGLMKISHSVKAGALEGVPI--------SGCLG------DQSAALVGQMCFQIgqakntygtgcf 318
Cdd:PRK10939 203 LRADILPPVKETGTVLGHVTAKAAAETGLRAGTPVvmgggdvqLGCLGlgvvrpGQTAVLGGTFWQQV------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 319 llCNTGHKCVFSDHGLlttvayklgRDKPvyYALEGSV---AIA---GAVIRWLRD-----------NLGiIKTSEEIEK 381
Cdd:PRK10939 271 --VNLPAPVTDPNMNI---------RINP--HVIPGMVqaeSISfftGLTMRWFRDafcaeekllaeRLG-IDAYSLLEE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 382 LAKEVGT-SYGcyFVPAFSG-LYAPYWEPSARGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHL 456
Cdd:PRK10939 337 MASRVPVgSHG--IIPIFSDvMRFKSWYHAAPSFI-NLSIDPEKCNKAtlFRALeENAAIVSACNLQQIAAFSGVFPSSL 413
|
490 500 510
....*....|....*....|....*....|...
gi 768032244 457 QVDGGMTSNKILMQLQADILYIPVVKPSMPETT 489
Cdd:PRK10939 414 VFAGGGSKGKLWSQILADVTGLPVKVPVVKEAT 446
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
16-482 |
7.13e-06 |
|
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: 48.94 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 16 VDQGTSSTRFLVFNSKTaELLSHHQVEI-KQEFPREGW-VEQDPKEILHSVYECIEKTCEKLgqlniDISNIKAIGVSnq 93
Cdd:cd07778 5 IDVGSTSVRIGIFDYHG-TLLATSERPIsYKQDPKDLWfVTQSSTEIWKAIKTALKELIEEL-----SDYIVSGIGVS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 94 reTT---VVWDKITGEPLYnavaapvspgpsVPVAVVPSGSSvpaPGTSSV-WLDLRTQSTVESLskripgNNNFVKSKT 169
Cdd:cd07778 77 --ATcsmVVMQRDSDTSYL------------VPYNVIHEKSN---PDQDIIfWMDHRASEETQWL------NNILPDDIL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 170 GLPLSTYF---SAVKLRWLLDNVrkvqKAVEEKRALFGTIDSWLIWSLTGGVNGG--VHCTDVTNASRTM---LFNihsl 241
Cdd:cd07778 134 DYLGGGFIpemAIPKLKYLIDLI----KEDTFKKLEVFDLHDWISYMLATNLGHSniVPVNAPPSIGIGIdgsLKG---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 242 eWDKQLCEFFGIPMEILPNVRSSSEIYGLM----KISH-SVKAGALEGVPIS-----GCLgDQSAALVGQMCfQIGQAKN 311
Cdd:cd07778 206 -WSKDFYSKLKISTKVCNVGNTFKEAPPLPyagiPIGKvNVILASYLGIDKStvvghGCI-DCYAGWFSTFA-AAKTLDT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 312 TY----GTG-CFLLcntGHKCVFSDH-----GLLTTvaykLGRDKPVYyalEGSVAIAG-----------AVIRWLRDNL 370
Cdd:cd07778 283 TLfmvaGTStCFLY---ATSSSQVGPipgiwGPFDQ----LLKNYSVY---EGGQSATGklieklfnshpAIIELLKSDA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 371 GIIKTSEE-IEKLAKEVGTS----YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTNKCHIAF---AALEAVCFQT 438
Cdd:cd07778 353 NFFETVEEkIDKYERLLGQSihylTRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQT 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 768032244 439 REILDAMNRDCgIPLSHLQVDGGMTSNKILMQLQADILYIPVVK 482
Cdd:cd07778 430 KLIIDNFQKEK-IIIQKVVISGSQAKNARLLQLLSTVLSKIHII 472
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
411-492 |
2.20e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 44.07 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032244 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGM-TSNKILMQLQADILYIPV-VKPSmPET 488
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475
|
....
gi 768032244 489 TALG 492
Cdd:PRK04123 476 PALG 479
|
|
| |
