|
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; ... |
11-538 |
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: 983.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 91 SNQRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFVKSKTG 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAI----------------------------VWLDTRTSDTVEELSAKTPGGKDHFRKKTG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 171 LPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEF 250
Cdd:cd07792 132 LPISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 251 FGIPMEILPNVRSSSEIYGLMKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLT 330
Cdd:cd07792 212 FGIPMSILPEIRSSSEVYGKIASGPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 331 TVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICG 410
Cdd:cd07792 292 TVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 411 LTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMA 490
Cdd:cd07792 372 LTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIA 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 578837869 491 AGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKS 538
Cdd:cd07792 452 AGLAVGVWKSLDELKSLNEGGRTVFEPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
11-541 |
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: 821.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 11 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 91 SNQRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNnnFVKSKTG 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAI----------------------------VWQDRRTASICEELKAEGYGE--FIREKTG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 171 LPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEF 250
Cdd:TIGR01311 127 LPLDPYFSATKLRWLLDNVPGVREAAERGELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLEL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 251 FGIPMEILPNVRSSSEIYGLMKAGAL-EGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLL 329
Cdd:TIGR01311 204 FGIPREILPEVRSSSEVYGYTDPGLLgAEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 330 TTVAYKLGRDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIIC 409
Cdd:TIGR01311 284 TTVAYQLGGKKPVY-ALEGSVFVAGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 410 GLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAM 489
Cdd:TIGR01311 363 GLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAY 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 578837869 490 AAGAAEGVGVWSLEPEDLSAVTmERFEPQINAEESEIRYSTWKKAVMKSMGW 541
Cdd:TIGR01311 443 AAGLAVGYWKSLEEIEALWRVE-KTFEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
13-535 |
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: 740.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAG---ISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 93 QRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGLP 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAI----------------------------VWQDRRTADICEELKAK--GLEERIREKTGLP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 173 LSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFG 252
Cdd:cd07769 128 LDPYFSATKIKWILDNVPGARERAERGELLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 253 IPMEILPNVRSSSEIYGLMKAGAL-EGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTT 331
Cdd:cd07769 205 IPRSMLPEVRPSSEVFGYTDPEGLgAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 332 VAYKLgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGL 411
Cdd:cd07769 285 IAWQI--GGKVTYALEGSIFIAGAAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 412 TQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaa 491
Cdd:cd07769 363 TRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalgaayl- 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 578837869 492 gaaegvgVWSLEPEDLSAVTMER-FEPQINAEESEIRYSTWKKAV 535
Cdd:cd07769 442 -aglavgFWKDLDELASLWQVDKrFEPSMDEEERERLYRGWKKAV 485
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
13-542 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 736.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 93 QRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGLP 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAI----------------------------VWQDRRTADICEELKAD--GLEDLIREKTGLV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 173 LSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFG 252
Cdd:COG0554 131 LDPYFSATKIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 253 IPMEILPNVRSSSEIYGLMKAGAL-EGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTT 331
Cdd:COG0554 208 IPRSMLPEVRPSSEVFGETDPDLFgAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 332 VAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGL 411
Cdd:COG0554 288 IAWGLG-GKVTY-ALEGSIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 412 TQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaamaa 491
Cdd:COG0554 366 TRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalgaayl- 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 578837869 492 gaaegvgVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAVMKSMGWV 542
Cdd:COG0554 445 -aglavgFWK-SLEELAALwkVDRRFEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-542 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 707.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 11 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDISnIKAIGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 91 SNQRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFVKsKTG 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAI----------------------------VWLDTRTYDIVNELTKKYGGSNFFQK-ITG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 171 LPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEF 250
Cdd:PTZ00294 131 LPISTYFSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 251 FGIPMEILPNVRSSSEIYGLMK---AGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHG 327
Cdd:PTZ00294 208 FGIPKETLPEIKSSSENFGTISgeaVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 328 LLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGI 407
Cdd:PTZ00294 288 LLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGT 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 408 ICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalGA 487
Cdd:PTZ00294 368 IVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT--AL 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 578837869 488 AMAAGAAEGVGVW-SLEP-EDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSMGWV 542
Cdd:PTZ00294 446 GAALLAGLAVGVWkSLEEvKKLIRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-542 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 695.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQ--LNIDiSNIKAIG 89
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAkgHNVD-SGLKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 90 VSNQRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFVKSKT 169
Cdd:PLN02295 79 ITNQRETTVAWSKSTGRPLYNAI----------------------------VWMDSRTSSICRRLEKELSGGRKHFVETC 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 170 GLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCE 249
Cdd:PLN02295 131 GLPISTYFSATKLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 250 FFGIPMEILPNVRSSSEIYGLMKAG-ALEGVPISGCLGDQSAALVGQMCfQIGQAKNTYGTGCFLLCNTGHKCVFSDHGL 328
Cdd:PLN02295 211 ALGIPAEILPKIVSNSEVIGTIAKGwPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 329 LTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGII 408
Cdd:PLN02295 290 LTTVAYKLGPDAPTNYALEGSVAIAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 409 CGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSH-----LQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 483
Cdd:PLN02295 370 VGITRFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETT 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578837869 484 alGAAMAAGAAEGVGVWSlePEDLSAVTMER----FEPQINAEESEIRYSTWKKAVMKSMGWV 542
Cdd:PLN02295 450 --ALGAAYAAGLAVGLWT--EEEIFASEKWKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-542 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 680.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 13 VGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 93 QRETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGLP 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAI----------------------------VWQDRRTADICEELKRD--GYEDYIREKTGLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 173 LSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFG 252
Cdd:PRK00047 133 IDPYFSGTKIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 253 IPMEILPNVRSSSEIYGLMKAG--ALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLT 330
Cdd:PRK00047 210 IPRSMLPEVRPSSEVYGKTNPYgfFGGEVPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 331 TVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICG 410
Cdd:PRK00047 290 TIAWGID-GKVVY-ALEGSIFVAGSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 411 LTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalgaama 490
Cdd:PRK00047 368 LTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT------- 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837869 491 agaaegvgvwSL--------------EPEDLSAVTME--RFEPQINAEESEIRYSTWKKAVMKSMGWV 542
Cdd:PRK00047 441 ----------ALgaaylaglavgfwkDLDELKEQWKIdrRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
15-535 |
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: 674.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07786 4 AIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 95 ETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGLPLS 174
Cdd:cd07786 80 ETTVVWDRETGKPVYNAI----------------------------VWQDRRTADICEELKAE--GHEEMIREKTGLVLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 175 TYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd07786 130 PYFSATKIRWILDNVPGARERAERGELAFGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 255 MEILPNVRSSSEIYGLMKAGAL-EGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGLLTTVA 333
Cdd:cd07786 207 ASMLPEVKPSSEVFGYTDPDLLgAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 334 YKLGrdKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQ 413
Cdd:cd07786 287 WQLG--GKVTYALEGSIFIAGAAVQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 414 FTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL-------- 485
Cdd:cd07786 365 GTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALgaaylagl 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 578837869 486 GAAMAAGAAEGVGVWSLEpedlsavtmERFEPQINAEESEIRYSTWKKAV 535
Cdd:cd07786 445 AVGLWKSLDELAKLWQVD---------RRFEPSMSEEEREALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
15-535 |
2.63e-144 |
|
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: 426.59 E-value: 2.63e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07793 4 AVDVGTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAG---LTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 95 ETTVVWDKITGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSK---------------RIP 159
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFI----------------------------TWQDLRAAELCESWNRslllkalrggskflhFLT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 160 GNNNFVKSKTgLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDSWLIWSLTGGvngGVHCTDVTNASRTMLFNIH 239
Cdd:cd07793 132 RNKRFLAASV-LKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 240 SLEWDKQLCEFFGIPMEILPNVRSSSEIYGLMKAGAL-EGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTG 318
Cdd:cd07793 208 TLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFgAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIDINTG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 319 HKCVFSDHGLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIiKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAP 398
Cdd:cd07793 288 SKPHASVKGLYPLVGWKIG-GEITY-LAEGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 399 YWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPS 478
Cdd:cd07793 365 YNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPK 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 578837869 479 MPETTalGAAMAAGAAEGVGVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAV 535
Cdd:cd07793 445 NTEMS--ALGAAFLAGLASGIWK-SKEELKKLrkIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-294 |
2.06e-103 |
|
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: 311.96 E-value: 2.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEklgQLNIDISNIKAIGVS 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLS---QLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 92 NQRETTVVWDKITgEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKriPGNNNFVKSKTGL 171
Cdd:pfam00370 77 NQGHGTVLLDKND-KPLYNAI----------------------------LWKDRRTAEIVENLKE--EGNNQKLYEITGL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 172 PLSTYFSAVKLRWLLDNVRKVQKAVEekraLFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFF 251
Cdd:pfam00370 126 PIWPGFTLSKLRWIKENEPEVFEKIH----KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAAL 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 578837869 252 GIPMEILPNVRSSSEIYGLMKA------GALEGVPISGCLGDQSAALVG 294
Cdd:pfam00370 197 GIPRDHLPPLVESSEIYGELNPelaamwGLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-483 |
3.21e-90 |
|
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: 286.73 E-value: 3.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 6 KAVLGplvgaVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNI 85
Cdd:COG1070 1 KYVLG-----IDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAG---VDPEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 86 KAIGVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFv 165
Cdd:COG1070 72 AAIGVSGQMHGLVLLDA-DGEPLRPAI----------------------------LWNDTRAAAEAAELREELGEEALY- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 166 kSKTGLPLSTYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDK 245
Cdd:COG1070 122 -EITGNPLHPGFTAPKLLWLKEN----EPEIFARIAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 246 QLCEFFGIPMEILPNVRSSSEIYGLMKA------GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGH 319
Cdd:COG1070 192 ELLEALGIDRELLPELVPPGEVAGTLTAeaaaetGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 320 KcVFSDHGLLTTVAYKL-GRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKTS--EEIEKLAKEVGT-SYGCYFVPAFSGL 395
Cdd:COG1070 272 P-LPDPEGRVHTFCHAVpGR-----WLPMGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 396 YAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 475
Cdd:COG1070 346 RTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVE 424
|
....*...
gi 578837869 476 KPSMPETT 483
Cdd:COG1070 425 VPEAEEGG 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
15-483 |
2.69e-85 |
|
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: 270.59 E-value: 2.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAG---IDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 95 ETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDlrtqstveslskripgnnnfvksktglpls 174
Cdd:cd00366 80 PGVVLVDA-DGNPLRPAI----------------------------IWLD------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 175 tyfsavklrwlldnvrkvqkaveeKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd00366 101 ------------------------RRAKFLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIP 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 255 MEILPNVRSSSEIYG-LMKAGAL-----EGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGhKCVFSDHGL 328
Cdd:cd00366 152 REKLPPIVESGEVVGrVTPEAAEetglpAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDPRL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 329 LTTVAYKLGRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKTSEE----IEKLAKEVGT-SYGCYFVPAFSGLYAPYWEPS 403
Cdd:cd00366 231 LNRCHVVPGL-----WLLEGAINTGGASLRWFRDEFGEEEDSDAeyegLDELAAEVPPgSDGLIFLPYLSGERSPIWDPA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 404 ARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETT 483
Cdd:cd00366 306 ARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGA 384
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
15-483 |
3.08e-84 |
|
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: 269.39 E-value: 3.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07779 4 GIDVGTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 95 ETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTqstveslskripgnnnfvksktglpls 174
Cdd:cd07779 80 STFVPVDE-DGRPLRPAI----------------------------SWQDKRT--------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 175 tyfsavklrwlldnvrkvqkaveekrALFGTIDSWLIWSLTggvngGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd07779 104 --------------------------AKFLTVQDYLLYRLT-----GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGID 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 255 MEILPNVRSSSEIYGLMKA------GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTgHKCVFSDHGL 328
Cdd:cd07779 153 RDKLPELVPPGTVIGTLTKeaaeetGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 329 LTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLG---------IIKTSEEIEKLAKEVGT-SYGCYFVPAFSGLYAP 398
Cdd:cd07779 232 IPCNPSAV----PGKWVLEGSINTGGSAVRWFRDEFGqdevaekelGVSPYELLNEEAAKSPPgSDGLLFLPYLAGAGTP 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 399 YWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPS 478
Cdd:cd07779 308 YWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPE 386
|
....*
gi 578837869 479 MPETT 483
Cdd:cd07779 387 TSEAT 391
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-483 |
1.72e-76 |
|
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: 249.43 E-value: 1.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 12 LVGaVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQlnidiSNIKAIGVS 91
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 92 NQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFvkSKTGL 171
Cdd:cd07773 75 SQGESGVPVDR-DGEPLGPAI----------------------------VWFDPRGKEEAEELAERIGAEELY--RITGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 172 PLSTYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFF 251
Cdd:cd07773 124 PPSPMYSLAKLLWLREH----EPEIFAKAAKWLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 252 GIPMEILPNVRSSSEIYGLMKAGALE------GVPIsgCLG--DQSAALVGQMCFQIGQAKNTYGTG-CFLLC-NTGHKC 321
Cdd:cd07773 195 GIDASLLPELVPSGTVIGTVTPEAAEelglpaGTPV--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 322 VFSDHGLLTTVAYKLGRdkpvYYALEGSVAiAGAVIRWLRDNLGI--IKTSEEIEKLAKEVGTSYGCYFVPAFSGLYAPY 399
Cdd:cd07773 273 EMLAEGGLSYGHHVPGG----YYYLAGSLP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 400 WEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSM 479
Cdd:cd07773 348 FDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426
|
....
gi 578837869 480 PETT 483
Cdd:cd07773 427 PEAT 430
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-483 |
2.41e-74 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 244.76 E-value: 2.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 8 VLGplvgaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07808 2 LLG-----IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 88 IGVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPgnnNFVKS 167
Cdd:cd07808 73 IGLTGQMHGLVLLDK-NGRPLRPAI----------------------------LWNDQRSAAECEELEARLG---DEILI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 168 KTGLPLSTYFSAVKLRWLL----DNVRKVQKAVEEKralfgtiDsWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEW 243
Cdd:cd07808 121 ITGNPPLPGFTLPKLLWLKenepEIFARIRKILLPK-------D-YLRYRLTG-----ELATDPSDASGTLLFDVEKREW 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 244 DKQLCEFFGIPMEILPNVRSSSEIYGLMKAGA------LEGVP-ISGClGDQSAALVGQMCFQIGQAKNTYGTGCFLLCN 316
Cdd:cd07808 188 SEELLEALGLDPSILPPIVESTEIVGTLTPEAaeelglPEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVVFAP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 317 TgHKCVFSDHGLLTTVAYKLGrdkPVYYALeGSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEVG-TSYGCYFVPAFSG 394
Cdd:cd07808 267 T-DKPVPDPKGRLHTFPHAVP---GKWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPYLSG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 395 LYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPV 474
Cdd:cd07808 342 ERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLGVPV 420
|
....*....
gi 578837869 475 VKPSMPETT 483
Cdd:cd07808 421 VVPAEEEGS 429
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
15-483 |
7.09e-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: 230.52 E-value: 7.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNIDisnikAIGVSNQR 94
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVD-----AIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 95 ETTVVWDKiTGEPLynavaAPVSPgpsvpvavvpsgssvpapgtssvWLDLRTQSTVESLSKRIPGNNnfVKSKTGLPLS 174
Cdd:cd07770 78 HSLLGVDE-DGEPL-----TPVIT-----------------------WADTRAAEEAERLRKEGDGSE--LYRRTGCPIH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 175 TYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd07770 127 PMYPLAKLLWLKEE----RPELFAKAAKFVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGID 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 255 MEILPNVRSSSEIYGLMKA------GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTgcfllcnTGHKCVFSDHGL 328
Cdd:cd07770 198 EEQLPELVDPTEVLPGLKPefaerlGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 329 LT----TVAYKLGRDKPVyyaLEGSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEP 402
Cdd:cd07770 271 LDppgrLWCYRLDENRWL---VGGAINNGGNVLDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 403 SARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 482
Cdd:cd07770 348 DARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEA 426
|
.
gi 578837869 483 T 483
Cdd:cd07770 427 S 427
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-478 |
3.45e-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: 3.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 12 LVGaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAG---ISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 92 NQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFvkSKTGL 171
Cdd:cd07804 77 GLVPALVPVDE-NGKPLRPAI----------------------------LYGDRRATEEIEWLNENIGEDRIF--EITGN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 172 PLSTYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTM-LFNIHSLEWDKQLCEF 250
Cdd:cd07804 126 PLDSQSVGPKLLWIKRN----EPEVFKKTRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 251 FGIPMEILPNVRSSSEIYGLMKAGA------LEGVPISGCLGDQSAALV-------GQMCFQIGqakntyGTGCFLLCnt 317
Cdd:cd07804 197 LGIDPDLLPELVPSTEIVGEVTKEAaeetglAEGTPVVAGTVDAAASALsagvvepGDLLLMLG------TAGDIGVV-- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 318 gHKCVFSDHGLLTTVAyklgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEE----------IEKLAKEVG-TSYGC 386
Cdd:cd07804 269 -TDKLPTDPRLWLDYH-----DIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEksggdsaydlLDEEAEKIPpGSDGL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 387 YFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQ 466
Cdd:cd07804 343 IVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIV 421
|
490
....*....|..
gi 578837869 467 ADILYIPVVKPS 478
Cdd:cd07804 422 ADVTGVPQEYVK 433
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
15-481 |
4.95e-60 |
|
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: 206.99 E-value: 4.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTrflvfnsKTA------ELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECiekTCEKLGQLNIDISNIKAI 88
Cdd:cd07805 4 AIDLGTSGV-------KAAlvdldgELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 89 GVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNnFVKSK 168
Cdd:cd07805 74 AFSGQMQGVVPVDK-DGNPLRNAI----------------------------IWSDTRAAEEAEEIAGGLGGIE-GYRLG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 169 TGLPLSTYFSAVKLRWLLDN----VRKVQKaveekraLFGTIDsWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWD 244
Cdd:cd07805 124 GGNPPSGKDPLAKILWLKENepeiYAKTHK-------FLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 245 KQLCEFFGIPMEILPNVRSSSEIYG--LMKA----GALEGVPISGCLGDQSAALVGQMCFQIGQAkNTY-GTGCFLLCNT 317
Cdd:cd07805 191 EELLRAAGIDPDKLPELVPSTEVVGelTPEAaaelGLPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 318 GHKCVFSDHGlLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLGIIKTS-----EEIEKLAKEVGT-SYGCYFVPA 391
Cdd:cd07805 270 PKPKTDPDHG-IFTLASAD----PGRYLLAAEQETAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFLPW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 392 FSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGiPLSHLQVDGGMTSNKILMQLQADILY 471
Cdd:cd07805 345 LNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLG 423
|
490
....*....|
gi 578837869 472 IPVVKPSMPE 481
Cdd:cd07805 424 RPVEVPENPQ 433
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
303-486 |
6.27e-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: 157.87 E-value: 6.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 303 AKNTYGTGCFLLCNTGHKCVFSdHGLLTTVAyklGRDKPVYYALEGSVAIAGAVIRWLRDNLGI---------IKTSEEI 373
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSV-HGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 374 EKLAKEVGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVD 453
Cdd:pfam02782 77 AALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190
....*....|....*....|....*....|...
gi 578837869 454 GGMTSNKILMQLQADILYIPVVKPSMPETTALG 486
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 ... |
12-483 |
1.76e-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: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 12 LVGaVDQGTSSTRFLVFNSKTAELLSHHqVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSG---VDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 92 NQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGL 171
Cdd:cd07802 77 GHGNGLYLVDK-DGKPVRNAI----------------------------LSNDSRAADIVDRWEED--GTLEKVYPLTGQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 172 PLSTYFSAVKLRWLLDN----VRKVQKAVEEKralfgtiDsWLIWSLTggvngGVHCTDVTNASrTMLFNIHSLEWDKQL 247
Cdd:cd07802 126 PLWPGQPVALLRWLKENeperYDRIRTVLFCK-------D-WIRYRLT-----GEISTDYTDAG-SSLLDLDTGEYDDEL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 248 CEFFGIP--MEILPNVRSSSEIYGLMKAGA------LEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCfllCNTG- 318
Cdd:cd07802 192 LDLLGIEelKDKLPPLVPSTEIAGRVTAEAaaltglPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVv 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 319 -HKCVFSDHGLLTTvaykLGRDKPVYYALEGSVAIAGaVIRWLRDNLG------IIKTSEEIEKLAKEVG-TSYGCYFVP 390
Cdd:cd07802 269 tDEPVVPDSVGSNS----LHADPGLYLIVEASPTSAS-NLDWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIFLP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 391 aFsgLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCgiPLSHLQVDGGMTSNKILMQLQADIL 470
Cdd:cd07802 344 -Y--LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVL 418
|
490
....*....|...
gi 578837869 471 YIPVVKPSMPETT 483
Cdd:cd07802 419 GLPVEVPDGEELG 431
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
15-482 |
9.17e-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: 155.84 E-value: 9.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLgqlniDISNIKAIGVSNQR 94
Cdd:cd07783 4 GIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 95 ETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPgnnnFVKSKTGLPLS 174
Cdd:cd07783 78 GTLVLVDR-EGEPLRPAI----------------------------MYNDARAVAEAEELAEAAG----AVAPRTGLAVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 175 TYFSAVKLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGGVNggvhCTDVTNASRTmLFNIHSLEWDKQLCEFFGIP 254
Cdd:cd07783 125 PSSSLAKLLWLKRH----EPEVLAKTAKFLHQADWLAGRLTGDRG----VTDYNNALKL-GYDPETGRWPSWLLALLGIP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 255 MEILPNVRSSSEIYGLMKA------GALEGVPIsgCLG--DQSAALVGQMCFQIGQAKNTYGTG-CF-LLCntgHKCVFS 324
Cdd:cd07783 196 PDLLPRVVAPGTVIGTLTAeaaeelGLPAGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGTTlVLkLLS---DKRVPD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 325 DHGLLTTvaYKLGRDkpvYYALEGSVAIAGAVIRWL--RDNLgiiktsEEIEKLAKEVGTSyGCYFVP-AFSGLYAPYWE 401
Cdd:cd07783 271 PGGGVYS--HRHGDG---YWLVGGASNTGGAVLRWFfsDDEL------AELSAQADPPGPS-GLIYYPlPLRGERFPFWD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 402 PSARGIICGLTqfTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 481
Cdd:cd07783 339 PDARGFLLPRP--HDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE 416
|
.
gi 578837869 482 T 482
Cdd:cd07783 417 A 417
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
15-483 |
2.47e-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: 152.38 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGW-VEQDPKEILHSVYECIEKTcekLGQLNIDISNIKAIGVSNQ 93
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDaKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 94 RETTVVWDKiTGEPLYNavaapvspGPSVpvavvpsgssvpapgtssvwlDLRTQSTVESLSKRIPgnnNFVKSKTGLPL 173
Cdd:cd07798 81 REGIVFLDK-DGRELYA--------GPNI---------------------DARGVEEAAEIDDEFG---EEIYTTTGHWP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 174 STYFSAVKLRWLldnvRKVQKAVEEKRALFGTIDSWLIWSLTGGVnggvhCTDVTNASRTMLFNIHSLEWDKQLCEFFGI 253
Cdd:cd07798 128 TELFPAARLLWF----KENRPEIFERIATVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALGL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 254 PMEILPNVRSSSEIYGLMKAGA------LEGVPISGCLGD-QSAALvgqmcfqigqakntyGTGCFllcNTGHKCVFSdh 326
Cdd:cd07798 199 PPEILPEIVPSGTVLGTVSEEAarelglPEGTPVVVGGADtQCALL---------------GSGAI---EPGDIGIVA-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 327 GllTTVAYKLGRDKPVY----------------YALEGSVAIAGAVIRWLRDNL--GIIKTSEEIEKLAKEVG-TSYGCY 387
Cdd:cd07798 259 G--TTTPVQMVTDEPIIdperrlwtgchlvpgkWVLESNAGVTGLNYQWLKELLygDPEDSYEVLEEEASEIPpGANGVL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 388 fvpAFSGLYAPYwePSARGIICGLTQFT--------NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSN 459
Cdd:cd07798 337 ---AFLGPQIFD--ARLSGLKNGGFLFPtplsaselTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRS 411
|
490 500
....*....|....*....|....
gi 578837869 460 KILMQLQADILYIPVVKPSMPETT 483
Cdd:cd07798 412 ALLCQILADVLGKPVLVPEGREAS 435
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
8-482 |
9.73e-33 |
|
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: 130.75 E-value: 9.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07809 2 VLG-----IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 88 IGVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNnfvKS 167
Cdd:cd07809 74 IGISGQMHGLVALDA-DGKVLRPAK----------------------------LWCDTRTAPEAEELTEALGGKK---CL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 168 KTGLPLSTYFSAVKLRWLLDN----VRKVQKaveekralFGTIDSWLIWSLTGGvnggvHCTDVTNASRTMLFNIHSLEW 243
Cdd:cd07809 122 LVGLNIPARFTASKLLWLKENepehYARIAK--------ILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDY 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 244 DKQLCEFF---GIPMEILPNVRSSSEIYG-LMKAGALE-----GVPISGCLGDQSAALVGQMCFQIGQAKNTYGT-GCfl 313
Cdd:cd07809 189 DAELLAAIdpsRDLRDLLPEVLPAGEVAGrLTPEGAEElglpaGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 314 LCNTGHKCVFSDHGLLTTVAyklgrDKPVYYALegSVAIAGAVIRWLRDNLGIIKTS-EEIEKLAKEV-GTSYGCYFVPA 391
Cdd:cd07809 267 AYGVSDKPVSDPHGRVATFC-----DSTGGMLP--LINTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 392 FSGLYAPYWePSARGIICGLTQF-TNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADIL 470
Cdd:cd07809 340 LNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVF 417
|
490
....*....|..
gi 578837869 471 YIPVVKPSMPET 482
Cdd:cd07809 418 GVPVVVPETGEG 429
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-483 |
2.73e-26 |
|
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: 111.54 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNSKTAELLS----HHQVEIKQEFPreGWVEQDPKEILHSVYECIEKTCEKLGqlnidiSNIKAIGV 90
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILEsvsrPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 91 SNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgTssvWLDLRtqSTVESLSKRIPGNNNFvKSKTG 170
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLI-------------------------T---WQDQR--CSEEFLGGLSTYGEEL-LPKSG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 171 LPLSTYFSAVKLRWLLdnvrkVQKAVEEKRALFGTIDSWLIWSLTGGVNggvHCTDVTNASRTMLFNIHSLEWDKQLCEF 250
Cdd:cd07777 124 MRLKPGYGLATLFWLL-----RNGPLPSKADRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 251 FGIPMEILPNVRSSSEIYGLMKAGALEGVPISGCLGDQSAALVGqmCFQIGqaKNT----YGTG---CFLLC-NTGHKCV 322
Cdd:cd07777 196 LGLPVILLPEIVPSGEIVGTLSSALPKGIPVYVALGDNQASVLG--SGLNE--ENDavlnIGTGaqlSFLTPkFELSGSV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 323 ----FSDHGLLTTVAyKL--GRdkpVYYALEGSVAiagaviRWLRDnLGIIKTSEEI-EKLAKEVGTSYGC--YFVPAFS 393
Cdd:cd07777 272 eirpFFDGRYLLVAA-SLpgGR---ALAVLVDFLR------EWLRE-LGGSLSDDEIwEKLDELAESEESSdlSVDPTFF 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 394 GlyaPYWEPSARGIICGLTQ--FTNKcHIAFAALEAVCfqtREILDAMNRDC--GIPLSHLQVDGGM-TSNKILMQLQAD 468
Cdd:cd07777 341 G---ERHDPEGRGSITNIGEsnFTLG-NLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRIIEK 413
|
490
....*....|....*
gi 578837869 469 ILYIPVVKPSMPETT 483
Cdd:cd07777 414 RFGLPVVLSEGSEEA 428
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
15-483 |
2.78e-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: 103.18 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNsKTAELLSHHQVE-IKQEFPR-EGWVEQDPKEILHSVYECIEKTCEklgQLNIDISNIKAIGVSN 92
Cdd:cd07775 4 ALDAGTGSGRAVIFD-LEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALK---KAGIAPKSIAAISTTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 93 QRETTVVWDKiTGEPLYnAVAApvspgpsvpvavvpsgssvpapgtssvwLDLRTQSTVESLSKRIPGNNNFVKSKTGLP 172
Cdd:cd07775 80 MREGIVLYDN-EGEEIW-ACAN----------------------------VDARAAEEVSELKELYNTLEEEVYRISGQT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 173 LStyFSAV-KLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFF 251
Cdd:cd07775 130 FA--LGAIpRLLWLKNN----RPEIYRKAAKITMLSDWIAYKLSG-----ELAVEPSNGSTTGLFDLKTRDWDPEILEMA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 252 GIPMEILPNVRSSSEIYGLMKA------GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSD 325
Cdd:cd07775 199 GLKADILPPVVESGTVIGKVTKeaaeetGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 326 HGLLTTVAYklgrDKPVYYAlEGSVAIAGAVIRWLRDNLGI----------IKTSEEIEKLAKEVGTsyGCY-FVPAFSG 394
Cdd:cd07775 279 MNIRVNCHV----IPDMWQA-EGISFFPGLVMRWFRDAFCAeekeiaerlgIDAYDLLEEMAKDVPP--GSYgIMPIFSD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 395 L--YApYWEPSARGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADI 469
Cdd:cd07775 352 VmnYK-NWRHAAPSFL-NLDIDPEKCNKAtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADV 429
|
490
....*....|....
gi 578837869 470 LYIPVVKPSMPETT 483
Cdd:cd07775 430 LGLPVKVPVVKEAT 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-482 |
5.90e-23 |
|
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: 101.93 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 12 LVGaVDQGTSSTRFLVFNSKTAELlSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGQLNidiSNIKAIGVS 91
Cdd:cd24121 2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 92 NQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRipGNNNFVKSKTGL 171
Cdd:cd24121 77 GQGDGTWLVDE-DGRPVRDAI----------------------------LWLDGRAADIVERWQAD--GIAEAVFEITGT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 172 PLSTYFSAVKLRWLLDNvrkVQKAVEEKRALFGTIDsWLIWSLTggvngGVHCTDVTNASRTMlFNIHSLEWDKQLCEFF 251
Cdd:cd24121 126 GLFPGSQAAQLAWLKEN---EPERLERARTALHCKD-WLFYKLT-----GEIATDPSDASLTF-LDFRTRQYDDEVLDLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 252 GIP--MEILPNVRSSSEIYGLMKA------GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFllcntghkcvf 323
Cdd:cd24121 196 GLEelRHLLPPIRPGTEVIGPLTPeaaaatGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV----------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 324 sdHGLLTTVAYkLGRDKP---VYYALEGSV-----AIAG-AVIRWLRDNLGIIKTSE----------EIEKLAKEV---- 380
Cdd:cd24121 265 --HEVVVDEPD-LEPEGVgytICLGVPGRWlramaNMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppga 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 381 -GTSYGCYFVPAfsGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnrdcGIPLSHLQVDGGMTSN 459
Cdd:cd24121 342 eGVLYHPYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARS 415
|
490 500
....*....|....*....|...
gi 578837869 460 KILMQLQADILYIPVVKPSMPET 482
Cdd:cd24121 416 DTWCQILADALGVPVRVPAGEEF 438
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
8-483 |
2.57e-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: 100.30 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEF--PREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNI 85
Cdd:cd07781 2 VIG-----IDFGTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAG---VDPEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 86 KAIGVSNQRETTVVWDKiTGEPLYNAVaapvspgpsvpvavvpsgssvpapgtssVWLDLRTQSTVESLSKRIPGNNNFV 165
Cdd:cd07781 74 VGIGVDTTSSTVVPVDE-DGNPLAPAI----------------------------LWMDHRAQEEAAEINETAHPALEYY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 166 KSKTGLPLS--TYFSavKLRWLLDNVRKVQKA----VEEkralfgtIDsWLIWSLTGGVNGGVhCtdvtNASRTMLFNIH 239
Cdd:cd07781 125 LAYYGGVYSseWMWP--KALWLKRNAPEVYDAaytiVEA-------CD-WINARLTGRWVRSR-C----AAGHKWMYNEW 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 240 SLEWDKQLCEFFGIPM----EILP-NVRSSSEIYGLMKA------GALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYG 308
Cdd:cd07781 190 GGGPPREFLAALDPGLlklrEKLPgEVVPVGEPAGTLTAeaaerlGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 309 T-GCFLLcnTGHKCVFSDhGLLTTVayklgrDKPV---YYALEGSVAIAGAVIRWLRDNLGI------IKTSEEIEKLAK 378
Cdd:cd07781 270 TsTCHLM--VSPKPVDIP-GICGPV------PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEAA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 379 EVGTsyGCyfvpafSGLYA---------PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSH 449
Cdd:cd07781 341 KLPP--GE------SGLVAldwfngnrtPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVNR 411
|
490 500 510
....*....|....*....|....*....|....*
gi 578837869 450 LQVDGGMTS-NKILMQLQADILYIPVVKPSMPETT 483
Cdd:cd07781 412 VVACGGIAEkNPLWMQIYADVLGRPIKVPKSDQAP 446
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-483 |
2.48e-19 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 90.86 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 17 DQGTSSTRFLVFNSKTAELLSHHQ---VEIKQEFPRegWVEQDPKEILHSVYECIEKTCEKLGQlnidiSNIKAIGVsnq 93
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTpnaSDIAAENSD--WHQWSLDAILQRFADCCRQINSELTE-----CHIRGITV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 94 reTT-----VVWDKiTGEPLYnavaapvspgpsvpvavvpsgssvpaPGTSsvWLDLRTQSTVESLSKRIPGNNNFVKSK 168
Cdd:PRK10331 78 --TTfgvdgALVDK-QGNLLY--------------------------PIIS--WKCPRTAAVMENIERYISAQQLQQISG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 169 TG-LPLSTYFsavKLRWLLDNvrkvqkaveeKRALFGTIDSWL-IWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQ 246
Cdd:PRK10331 127 VGaFSFNTLY---KLVWLKEN----------HPQLLEQAHAWLfISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 247 LCEFFGIPMEILPNVRSSSEIYGLMKAGALE------GVPISGCLGDQSAALVGQmcfqiGQAKN----TYGTGCFLLCN 316
Cdd:PRK10331 194 ILQATGLSRRLFPRLVEAGEQIGTLQPSAAAllglpvGIPVISAGHDTQFALFGS-----GAGQNqpvlSSGTWEILMVR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 317 TGH---KCVFSDHGLLTTVAYKLGRDKPvyyaleGSVAIAGAVIRWLRDNLGiikTSEE-----IEKlAKEVGT-SYGCY 387
Cdd:PRK10331 269 SAQvdtSLLSQYAGSTCELDSQSGLYNP------GMQWLASGVLEWVRKLFW---TAETpyqtmIEE-ARAIPPgADGVK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 388 FVPAFSGlyapywepSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQA 467
Cdd:PRK10331 339 MQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKA 410
|
490
....*....|....*.
gi 578837869 468 DILYIPVVKPSMPETT 483
Cdd:PRK10331 411 NMLDIPIKVLDDAETT 426
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
16-469 |
1.25e-17 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 85.79 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 16 VDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEIlhsvYECIEKTCEKLGQLNiDISNIKAIGVSNQRE 95
Cdd:PRK15027 5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQW----WQATDRAMKALGDQH-SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 96 TTVVWDKitgeplYNAVAAPvspgpsvpvavvpsgssvpapgtSSVWLDLRTQSTVESLSKRIPGNnnfvKSKTGLPLST 175
Cdd:PRK15027 79 GATLLDA------QQRVLRP-----------------------AILWNDGRCAQECALLEARVPQS----RVITGNLMMP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 176 YFSAVKLRWLL----DNVRKVQKAVEEKralfgtidSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFF 251
Cdd:PRK15027 126 GFTAPKLLWVQrhepEIFRQIDKVLLPK--------DYLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQAC 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 252 GIPMEILPNVRSSSEIYG-----LMKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTgcfllcnTGHKCVFSDh 326
Cdd:PRK15027 193 HLSRDQMPALYEGSEITGallpeVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 327 GLLT---TVAYKLGRDKPVYYALEGSVAIAGAVIRW------LRDNLGIIKTSEEIEKLAKEVgtsygcYFVPAFSGLYA 397
Cdd:PRK15027 265 GFLSkpeSAVHSFCHALPQRWHLMSVMLSAASCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERT 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578837869 398 PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGGMTSNKILMQLQADI 469
Cdd:PRK15027 339 PHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
15-482 |
3.14e-16 |
|
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: 81.81 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILHSVYECIEKTCEKLGqlnIDISNIKAIGVsnqr 94
Cdd:cd07782 4 GVDVGTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAG---VDPEQVKGIGF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 95 ETT---VVWDKiTGEPlynavaapvspgpsvpVAVVPSGSS----VpapgtssVWLDLRTQSTVEslskRIpgnnnfvkS 167
Cdd:cd07782 76 DATcslVVLDA-EGKP----------------VSVSPSGDDernvI-------LWMDHRAVEEAE----RI--------N 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 168 KTGLPLSTYFSAV--------KLRWLLDNvrkvQKAVEEKRALFGTIDSWLIWSLTGGVNGGVhCTDVtnASRTMLFNIH 239
Cdd:cd07782 120 ATGHEVLKYVGGKispemeppKLLWLKEN----LPETWAKAGHFFDLPDFLTWKATGSLTRSL-CSLV--CKWTYLAHEG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 240 SLE-WDKqlcEFF-GIPMEILpnvrsSSEIYGLMKAGALE-GVPISGCLGDQSAAlvgqmcfQIGQAKNT---------Y 307
Cdd:cd07782 193 SEGgWDD---DFFkEIGLEDL-----VEDNFAKIGSVVLPpGEPVGGGLTAEAAK-------ELGLPEGTpvgvslidaH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 308 --GTGCflLCNTGHKCVFSDHGLLTTVAYKLG--------RDKPV--------YY-AL-------EGSVAIAGAVIRWlr 361
Cdd:cd07782 258 agGLGT--LGADVGGLPCEADPLTRRLALICGtsschmavSPEPVfvpgvwgpYYsAMlpglwlnEGGQSATGALLDH-- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 362 dnlgIIKT---SEEIEKLAKEVGTSY------------------------GCYFVPAFSGLYAPYWEPSARGIICGLTQF 414
Cdd:cd07782 334 ----IIEThpaYPELKEEAKAAGKSIyeylnerleqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLD 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578837869 415 TNKCHIA---FAALEAVCFQTREILDAMNRdCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 482
Cdd:cd07782 410 TSLDDLAllyLATLQALAYGTRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
16-482 |
4.71e-16 |
|
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: 81.13 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 16 VDQGTSSTRFLVFNSKTAELLSHHQVEIKQ-EFPREGWVEQDPKEILHSVYECIEKTcekLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDATC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 95 eTTVVWDKiTGEPLYnavaapvspgpsvpvavvpsgSSVPAPGTSSV--WLDLRTQSTVESLskripgnnNFVKSKTGLP 172
Cdd:cd07768 82 -SLAIFDR-EGTPLM---------------------ALIPYPNEDNVifWMDHSAVNEAQWI--------NMQCPQQLLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 173 -----LSTYFSAVKLRWLLDNVRKVQKAVEEkraLFGTIDsWLIWSLTGgvnggvhctDVTNASRTMLF--NIHSLE--W 243
Cdd:cd07768 131 ylggkISPEMGVPKLKYFLDEYSHLRDKHFH---IFDLHD-YIAYELTR---------LYEWNICGLLGkeNLDGEEsgW 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 244 DKQLCEFFGIPME------ILPNVRSSSEIYGLM------KAGALEGVPISGCLGDQSAALvgqmcfqIGQAKNTYGTGC 311
Cdd:cd07768 198 SSSFFKNIDPRLEhltttkNLPSNVPIGTTSGVAlpemaeKMGLHPGTAVVVSCIDAHASW-------FAVASPHLETSL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 312 FLLCNTGhkcvfSDHGLLTTVAYKL-GRDKPVYYAL-------EGSVAIAGAVIRWL-------RDNLGIIKTSEEI--- 373
Cdd:cd07768 271 FMIAGTS-----SCHMYGTTISDRIpGVWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqv 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 374 -----EKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREILDAMNRDcGI 445
Cdd:cd07768 346 leqtiRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GI 424
|
490 500 510
....*....|....*....|....*....|....*..
gi 578837869 446 PLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 482
Cdd:cd07768 425 HIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
144-475 |
2.24e-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: 72.56 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 144 DLRTQSTVESLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLldnvrkvqkaVEEKRALFGTIDSWLI------WSLTGg 217
Cdd:cd07771 98 DPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL----------KKEGPELLERADKLLMlpdllnYLLTG- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 218 vnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIYG-----LMKAGALEGVP-ISGCLGDQSAA 291
Cdd:cd07771 165 ----EKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGtlkpeVAEELGLKGIPvIAVASHDTASA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 292 LVGqmcfqI-GQAKNTYgtgcFLLCNT----GhkcVFSDHGLLTTVAYKLGrdkpvyYALEGSVA--------IAGaviR 358
Cdd:cd07771 241 VAA-----VpAEDEDAA----FISSGTwsliG---VELDEPVITEEAFEAG------FTNEGGADgtirllknITG---L 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 359 WL----RDNL---GIIKTSEEIEKLAKEVgTSYGCYFVPAFSGLYAPywePSARGIICGLTQFTN------KCHIAFAAL 425
Cdd:cd07771 300 WLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFLNP---GDMPEAIRAYCRETGqpvpesPGEIARCIY 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 578837869 426 EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 475
Cdd:cd07771 376 ESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVI 425
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-486 |
9.12e-13 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 70.91 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 5 KKAVLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQ------EFPREGWVEQDPKEILHSVYECIektCEKLGQL 78
Cdd:COG1069 1 EKYVIG-----VDFGTDSVRAVVVDAADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAV---REALAQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 79 NIDISNIKAIGVSNQRETTVVWDKiTGEPLynavaaPVSPGPS-VPVA-VVpsgssvpapgtssVWLDLRTQSTVEslsk 156
Cdd:COG1069 73 GVDPADVVGIGVDATGCTPVPVDA-DGTPL------ALLPEFAeNPHAmVI-------------LWKDHTAQEEAE---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 157 RIpgnnNFVKSKTGLPLSTY---------FSAvKLRWLLdnvrkvqkavEEKRALFGTIDS------WLIWSLTGGVNGG 221
Cdd:COG1069 129 RI----NELAKARGEDYLRYvggiissewFWP-KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 222 VhCTdvtnASRTMLFNIHSLEW-DKqlcEFF---GIPMEILPNvRSSSEIYGL-MKAGAL-----------EGVPISGCL 285
Cdd:COG1069 194 R-CT----AGHKALWHAHEGGYpSE---EFFaalDPLLDGLAD-RLGTEIYPLgEPAGTLtaewaarlglpPGTAVAVGA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 286 GDQSAALVGqmcfqIGQAKNTY-----GT-GCFLLCNTGHKCVFS-----DHGLLttvayklgrdkPVYYALEGSVAIAG 354
Cdd:COG1069 265 IDAHAGAVG-----AGGVEPGTlvkvmGTsTCHMLVSPEERFVPGicgqvDGSIV-----------PGMWGYEAGQSAVG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 355 AVIRWLRDNLGiikTSEEIEKLAKEVGTS----------------YGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKC 418
Cdd:COG1069 329 DIFAWFVRLLV---PPLEYEKEAEERGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAE 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578837869 419 HIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGG-MTSNKILMQLQADILYIPVVKPSMPETTALG 486
Cdd:COG1069 406 DIYRALVEATAFGTRAIIERFE-EEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALG 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-483 |
1.66e-07 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 53.86 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPR-EGWVEQDPKEILHSVYECIEktcEKLGQLNIDISNIKAIGVSNQ 93
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 94 RETTVVWDKiTGEPLYnAVAApvspgpsvpvavvpsgssvpapgtssvwLDLRTQSTVESLSKRIPGNNNFVKSKTGLPL 173
Cdd:PRK10939 84 REGIVLYDR-NGTEIW-ACAN----------------------------VDARASREVSELKELHNNFEEEVYRCSGQTL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 174 StyFSAV-KLRWLldnvRKVQKAVEEKRALFGTIDSWLIWSLTGgvnggVHCTDVTNASRTMLFNIHSLEWDKQLCEFFG 252
Cdd:PRK10939 134 A--LGALpRLLWL----AHHRPDIYRQAHTITMISDWIAYMLSG-----ELAVDPSNAGTTGLLDLVTRDWDPALLEMAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 253 IPMEILPNVRSSSEIYGLMKA------GALEGVPI--------SGCLG------DQSAALVGQMCFQIgqakntygtgcf 312
Cdd:PRK10939 203 LRADILPPVKETGTVLGHVTAkaaaetGLRAGTPVvmgggdvqLGCLGlgvvrpGQTAVLGGTFWQQV------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 313 llCNTGHKCVFSDHGLlttvayklgRDKPvyYALEGSV---AIA---GAVIRWLRD-----------NLGiIKTSEEIEK 375
Cdd:PRK10939 271 --VNLPAPVTDPNMNI---------RINP--HVIPGMVqaeSISfftGLTMRWFRDafcaeekllaeRLG-IDAYSLLEE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 376 LAKEVGT-SYGcyFVPAFSG-LYAPYWEPSARGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHL 450
Cdd:PRK10939 337 MASRVPVgSHG--IIPIFSDvMRFKSWYHAAPSFI-NLSIDPEKCNKAtlFRALeENAAIVSACNLQQIAAFSGVFPSSL 413
|
490 500 510
....*....|....*....|....*....|...
gi 578837869 451 QVDGGMTSNKILMQLQADILYIPVVKPSMPETT 483
Cdd:PRK10939 414 VFAGGGSKGKLWSQILADVTGLPVKVPVVKEAT 446
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
16-476 |
1.22e-05 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 48.17 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 16 VDQGTSSTRFLVFNSKTaELLSHHQVEI-KQEFPREGW-VEQDPKEILHSVYECIEKTCEKLgqlniDISNIKAIGVSnq 93
Cdd:cd07778 5 IDVGSTSVRIGIFDYHG-TLLATSERPIsYKQDPKDLWfVTQSSTEIWKAIKTALKELIEEL-----SDYIVSGIGVS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 94 reTT---VVWDKITGEPLYnavaapvspgpsVPVAVVPSGSSvpaPGTSSV-WLDLRTQSTVESLskripgNNNFVKSKT 169
Cdd:cd07778 77 --ATcsmVVMQRDSDTSYL------------VPYNVIHEKSN---PDQDIIfWMDHRASEETQWL------NNILPDDIL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 170 GLPLSTYF---SAVKLRWLLDNVrkvqKAVEEKRALFGTIDSWLIWSLTGGVNGG--VHCTDVTNASRTM---LFNihsl 241
Cdd:cd07778 134 DYLGGGFIpemAIPKLKYLIDLI----KEDTFKKLEVFDLHDWISYMLATNLGHSniVPVNAPPSIGIGIdgsLKG---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 242 eWDKQLCEFFGIPMEILPNVRSSSEIYGLMKAG-----------ALEGVPIS-----GCLgDQSAALVGQMCfQIGQAKN 305
Cdd:cd07778 206 -WSKDFYSKLKISTKVCNVGNTFKEAPPLPYAGipigkvnvilaSYLGIDKStvvghGCI-DCYAGWFSTFA-AAKTLDT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 306 TY----GTG-CFLLcntGHKCVFSDH-----GLLTTvaykLGRDKPVYyalEGSVAIAG-----------AVIRWLRDNL 364
Cdd:cd07778 283 TLfmvaGTStCFLY---ATSSSQVGPipgiwGPFDQ----LLKNYSVY---EGGQSATGklieklfnshpAIIELLKSDA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 365 GIIKTSEE-IEKLAKEVGTS----YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTNKCHIAF---AALEAVCFQT 432
Cdd:cd07778 353 NFFETVEEkIDKYERLLGQSihylTRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQT 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 578837869 433 REILDAMNRDCgIPLSHLQVDGGMTSNKILMQLQADILYIPVVK 476
Cdd:cd07778 430 KLIIDNFQKEK-IIIQKVVISGSQAKNARLLQLLSTVLSKIHII 472
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
405-486 |
2.19e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 44.07 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837869 405 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGM-TSNKILMQLQADILYIPV-VKPSmPET 482
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475
|
....
gi 578837869 483 TALG 486
Cdd:PRK04123 476 PALG 479
|
|
| |
