|
Name |
Accession |
Description |
Interval |
E-value |
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
31-533 |
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: 797.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 31 GLVGVIDEGTKTIGFSIYTtPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPEQgfsASDIVTVGI 110
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAGIK---PDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 111 TNQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDpNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRER 190
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKAEGYG-EFIREKTGLPLDPYFSATKLRWLLDNVPGVREAAERG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 191 RCKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERsPLRGMT 270
Cdd:TIGR01311 156 ELLFGTIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPREILPEVRSSSEVYGYTDPGL-LGAEIP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 271 LSGIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGPQAPTiYAIEGAVSVAGHALSWL 350
Cdd:TIGR01311 235 ITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVISKHGLLTTVAYQLGGKKPV-YALEGSVFVAGAAVQWL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 351 QNKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMH 430
Cdd:TIGR01311 314 RDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAME 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 431 QECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVNLCQFEPEKRYYENvhyDTFLAT 510
Cdd:TIGR01311 394 KDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTALGAAYAAGLAVGYWKSLEEIEALWRVE---KTFEPE 470
|
490 500
....*....|....*....|...
gi 24655555 511 TTDVERKERYGKWKRAVERSLGW 533
Cdd:TIGR01311 471 MDEEEREARYAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
32-530 |
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: 762.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 32 LVGVIDEGTKTIGFSIYTTpDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPEQGFSASDIVTVGIT 111
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 112 NQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKV-QDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRER 190
Cdd:cd07792 81 NQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTpGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 191 RCKAGTVDSWIVWNLT---NGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSErsPLR 267
Cdd:cd07792 161 RLLFGTVDSWLIWNLTggkNGGVHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYGKIASG--PLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 268 GMTLSGIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGPQAPTIYAIEGAVSVAGHAL 347
Cdd:cd07792 239 GVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFSKHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 348 SWLQNKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILE 427
Cdd:cd07792 319 QWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDARGTIVGLTQFTTKAHIARAALEAVCFQTREILD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 428 CMHQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVNLCQFEPEKryYENVHYDTF 507
Cdd:cd07792 399 AMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKS--LNEGGRTVF 476
|
490 500
....*....|....*....|...
gi 24655555 508 LATTTDVERKERYGKWKRAVERS 530
Cdd:cd07792 477 EPQISEEERERRYKRWKKAVERS 499
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
32-534 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 655.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 32 LVGVIDEGTKTIGFSIYTTpDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPEQGFSAsDIVTVGIT 111
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFDE-KGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSF-KIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 112 NQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRERR 191
Cdd:PTZ00294 81 NQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVKEGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 192 CKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSER-SPLRGMT 270
Cdd:PTZ00294 161 LLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAvPLLEGVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 271 LSGIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGPQAPTIYAIEGAVSVAGHALSWL 350
Cdd:PTZ00294 241 ITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 351 QNKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMH 430
Cdd:PTZ00294 321 RDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESME 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 431 QECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVnlcqFE--PEKRYYENVHYDTFL 508
Cdd:PTZ00294 401 KDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGV----WKslEEVKKLIRRSNSTFS 476
|
490 500
....*....|....*....|....*.
gi 24655555 509 ATTTDVERKERYGKWKRAVERSLGWV 534
Cdd:PTZ00294 477 PQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
33-534 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 641.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 33 VGVIDEGT---KTIGFsiytTPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQlpeQGFSASDIVTVG 109
Cdd:COG0554 5 ILAIDQGTtstRAILF----DRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAK---AGISAEDIAAIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 110 ITNQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDPnHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRE 189
Cdd:COG0554 78 ITNQRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKADGLED-LIREKTGLVLDPYFSATKIKWILDNVPGARERAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 190 RRCKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKiTSERSPLRGM 269
Cdd:COG0554 157 GELLFGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFGE-TDPDLFGAEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 270 TLSGIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGPQapTIYAIEGAVSVAGHALSW 349
Cdd:COG0554 236 PIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKNGLLTTIAWGLGGK--VTYALEGSIFVAGAAVQW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 350 LQNKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECM 429
Cdd:COG0554 314 LRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 430 HQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGV--NLCQFEpekryyENVHYD-T 506
Cdd:COG0554 394 EADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFwkSLEELA------ALWKVDrR 467
|
490 500
....*....|....*....|....*...
gi 24655555 507 FLATTTDVERKERYGKWKRAVERSLGWV 534
Cdd:COG0554 468 FEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
33-528 |
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: 639.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 33 VGVIDEGT---KTIGFSiyttPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLpeqGFSASDIVTVG 109
Cdd:cd07769 2 ILAIDQGTtstRAILFD----EDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKA---GISASDIAAIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 110 ITNQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDPNhFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRE 189
Cdd:cd07769 75 ITNQRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKAKGLEER-IREKTGLPLDPYFSATKIKWILDNVPGARERAER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 190 RRCKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKiTSERSPLRGM 269
Cdd:cd07769 154 GELLFGTIDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGY-TDPEGLGAGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 270 TLSGIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGpqAPTIYAIEGAVSVAGHALSW 349
Cdd:cd07769 233 PIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKNGLLTTIAWQIG--GKVTYALEGSIFIAGAAIQW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 350 LQNKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECM 429
Cdd:cd07769 311 LRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIVRAALESIAYQTRDVLEAM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 430 HQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVNLCQFEPEKRYyenVHYDTFLA 509
Cdd:cd07769 391 EKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLW---QVDKRFEP 467
|
490
....*....|....*....
gi 24655555 510 TTTDVERKERYGKWKRAVE 528
Cdd:cd07769 468 SMDEEERERLYRGWKKAVE 486
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
32-534 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 627.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 32 LVGVIDEGTKTIGFSIYTTpDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPEQGFS-ASDIVTVGI 110
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDR-DARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNvDSGLKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 111 TNQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDPN-HFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRE 189
Cdd:PLN02295 80 TNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSGGRkHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 190 RRCKAGTVDSWIVWNLTNGA---LHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITsERSPL 266
Cdd:PLN02295 160 GDALFGTIDSWLIWNLTGGAsggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIA-KGWPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 267 RGMTLSGIMGNQQASLLGQMCvKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGPQAPTIYAIEGAVSVAGHA 346
Cdd:PLN02295 239 AGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 347 LSWLQNKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDIL 426
Cdd:PLN02295 318 VQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIARAVLESMCFQVKDVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 427 ECMHQECGYEINK-----LHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVNLCQFEPEKRYYEN 501
Cdd:PLN02295 398 DAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKN 477
|
490 500 510
....*....|....*....|....*....|...
gi 24655555 502 VhyDTFLATTTDVERKERYGKWKRAVERSLGWV 534
Cdd:PLN02295 478 T--TTFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
35-528 |
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: 590.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 35 VIDEGT---KTIGFSiyttPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLpeqGFSASDIVTVGIT 111
Cdd:cd07786 4 AIDQGTtssRAILFD----HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKA---GIRASDIAAIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 112 NQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDPNhFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRERR 191
Cdd:cd07786 77 NQRETTVVWDRETGKPVYNAIVWQDRRTADICEELKAEGHEEM-IREKTGLVLDPYFSATKIRWILDNVPGARERAERGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 192 CKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPlRGMTL 271
Cdd:cd07786 156 LAFGTIDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDPDLLG-AEIPI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 272 SGIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGpqAPTIYAIEGAVSVAGHALSWLQ 351
Cdd:cd07786 235 AGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGLLTTIAWQLG--GKVTYALEGSIFIAGAAVQWLR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 352 NKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMHQ 431
Cdd:cd07786 313 DGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDLLEAMEA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 432 ECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGV--NL----CQFEPEKRyyenvhyd 505
Cdd:cd07786 393 DSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLwkSLdelaKLWQVDRR-------- 464
|
490 500
....*....|....*....|...
gi 24655555 506 tFLATTTDVERKERYGKWKRAVE 528
Cdd:cd07786 465 -FEPSMSEEEREALYAGWKKAVK 486
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
33-534 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 586.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 33 VGVIDEGTkTIGFSIYTTPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAikqLPEQGFSASDIVTVGITN 112
Cdd:PRK00047 7 ILALDQGT-TSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEA---LAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 113 QRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDpNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRERRC 192
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAIVWQDRRTADICEELKRDGYE-DYIREKTGLVIDPYFSGTKIKWILDNVEGARERAEKGEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 193 KAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRGMTLS 272
Cdd:PRK00047 162 LFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYGFFGGEVPIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 273 GIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGpqAPTIYAIEGAVSVAGHALSWLQN 352
Cdd:PRK00047 242 GIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIAWGID--GKVVYALEGSIFVAGSAIQWLRD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 353 KVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMHQE 432
Cdd:PRK00047 320 GLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQAD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 433 CGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGV--NL----CQFEPEKRyyenvhydt 506
Cdd:PRK00047 400 SGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFwkDLdelkEQWKIDRR--------- 470
|
490 500
....*....|....*....|....*...
gi 24655555 507 FLATTTDVERKERYGKWKRAVERSLGWV 534
Cdd:PRK00047 471 FEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
35-528 |
1.57e-136 |
|
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: 406.18 E-value: 1.57e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 35 VIDEGTKTIGFSIYTTpDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLpeqGFSASDIVTVGITNQR 114
Cdd:cd07793 4 AVDVGTTNIRCHIFDK-KGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNA---GLTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 115 ETTIVWDAVTGKPLYNALLWKDIRTSTTVEQ---------------IVAKVQDPNHFRSSTGLPISTYFSALKIRWLRDN 179
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFITWQDLRAAELCESwnrslllkalrggskFLHFLTRNKRFLAASVLKFSTAHVSIRLLWILQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 180 VPEVRQAIRERRCKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKI 259
Cdd:cd07793 160 NPELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFGST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 260 TSERS----PLRGmtlsgIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGpqAPTIYA 335
Cdd:cd07793 240 DPSIFgaeiPITA-----VVADQQAALFGECCFDKGDVKITMGTGTFIDINTGSKPHASVKGLYPLVGWKIG--GEITYL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 336 IEGAVSVAGHALSWLQNKVRIlPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAAL 415
Cdd:cd07793 313 AEGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVRAIL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 416 ESICFQTRDILECMHQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAaqadGVNLCQFEPE 495
Cdd:cd07793 392 ESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLA----GLASGIWKSK 467
|
490 500 510
....*....|....*....|....*....|....
gi 24655555 496 KRYYENVH-YDTFLATTTDVERKERYGKWKRAVE 528
Cdd:cd07793 468 EELKKLRKiEKIFEPKMDNEKREELYKNWKKAVK 501
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
36-529 |
2.87e-92 |
|
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: 292.12 E-value: 2.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGT---KTIGFSiyttPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASInkcaEEAIKQLPEQ-GFSASDIVTVGIT 111
Cdd:COG1070 6 IDIGTtsvKAVLFD----ADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAV----VEAIRELLAKaGVDPEEIAAIGVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 112 NQRETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVqDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRerr 191
Cdd:COG1070 78 GQMHGLVLLDA-DGEPLRPAILWNDTRAAAEAAELREEL-GEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIA--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 192 cKAGTVDSWIVWNLTnGALHiTDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRGMtL 271
Cdd:COG1070 153 -KVLLPKDYLRYRLT-GEFV-TDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGL-P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 272 SGI-----MGNQQASLLGQMCVKPGQ------TkntyrSGCFLLCNtgDKPVFSRHGLLTTVAYklgpQAPTIYAIEGAV 340
Cdd:COG1070 229 AGTpvvagAGDNAAAALGAGAVEPGDaavslgT-----SGVVFVVS--DKPLPDPEGRVHTFCH----AVPGRWLPMGAT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 341 SVAGHALSWLQNKVrilpDSRDAEKYAEMV-------PTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRA 413
Cdd:COG1070 298 NNGGSALRWFRDLF----ADGELDDYEELNalaaevpPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 414 ALESICFQTRDILECMhQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVN----- 488
Cdd:COG1070 374 VLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYddlee 452
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24655555 489 -LCQFEPEKRyyenvhydTFLATTTDVER-KERYGKWKRAVER 529
Cdd:COG1070 453 aAAAMVRVGE--------TIEPDPENVAAyDELYERYRELYPA 487
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
35-487 |
4.33e-79 |
|
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: 255.52 E-value: 4.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 35 VIDEGT---KTIGFsiytTPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPEqgfSASDIVTVGIT 111
Cdd:cd07779 4 GIDVGTtstRAIIF----DLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGV---DPEDIAAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 112 NQRETTIVWDAvTGKPLYNALLWKDIRTSttveqivakvqdpnhfrsstglpistYFSalkirwlrdnvpevrqairerr 191
Cdd:cd07779 77 SQRSTFVPVDE-DGRPLRPAISWQDKRTA--------------------------KFL---------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 192 ckagTVDSWIVWNLTngALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRGMTl 271
Cdd:cd07779 108 ----TVQDYLLYRLT--GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLP- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 272 SGIM-----GNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTgDKPVFSRHGLLTTVAYKLgpqaPTIYAIEGAVSVAGHA 346
Cdd:cd07779 181 EGTPvvaggGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPERRIPCNPSAV----PGKWVLEGSINTGGSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 347 LSWL-----QNKVRILPDSRDAEKY-----AEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALE 416
Cdd:cd07779 256 VRWFrdefgQDEVAEKELGVSPYELlneeaAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILE 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24655555 417 SICFQTRDILECMhQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGV 487
Cdd:cd07779 336 GIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGI 405
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
36-481 |
1.07e-78 |
|
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: 253.26 E-value: 1.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGT---KTIGFsiytTPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLpeqGFSASDIVTVGITN 112
Cdd:cd00366 5 IDIGTtsvKAALF----DEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKA---GIDPSDIAAIGISG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 113 QRETTIVWDAvTGKPLYNALLWKDirtsttveqivakvqdpnhfrsstglpistyfsalkirwlrdnvpevrqaireRRC 192
Cdd:cd00366 78 QMPGVVLVDA-DGNPLRPAIIWLD-----------------------------------------------------RRA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 193 KAGTVDSWIVWNLTnGALhITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSE---RSPLRgm 269
Cdd:cd00366 104 KFLQPNDYIVFRLT-GEF-AIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEaaeETGLP-- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 270 tlSGI-----MGNQQASLLGQMCVKPGQTKNTY-RSGCFLLCntGDKPVFSRHGLLTTVAYKLGPqaptiYAIEGAVSVA 343
Cdd:cd00366 180 --AGTpvvagGGDTAAAALGAGVVEPGDAVDSTgTSSVLSVC--TDEPVPPDPRLLNRCHVVPGL-----WLLEGAINTG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 344 GHALSWLQNKvrILPDSRDAEKYAEMV-------PTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALE 416
Cdd:cd00366 251 GASLRWFRDE--FGEEEDSDAEYEGLDelaaevpPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLE 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655555 417 SICFQTRDILECMhQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCA 481
Cdd:cd00366 329 GVAYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
36-487 |
7.14e-75 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 246.30 E-value: 7.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGT---KTIGFSiyttPDFKEIAAHRVELSVITPQDGWYEQDPLEMMasinKCAEEAIKQLPEQ-GFSASDIVTVGIT 111
Cdd:cd07808 5 IDLGTssvKAVLVD----EDGRVLASASAEYPTSSPKPGWAEQDPEDWW----QATKEALRELLAKaGISPSDIAAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 112 NQRETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVQDpnHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRerr 191
Cdd:cd07808 77 GQMHGLVLLDK-NGRPLRPAILWNDQRSAAECEELEARLGD--EILIITGNPPLPGFTLPKLLWLKENEPEIFARIR--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 192 ckagTV----DsWIVWNLTnGALHiTDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLR 267
Cdd:cd07808 151 ----KIllpkD-YLRYRLT-GELA-TDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 268 GMTlSGI-----MGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTgDKPVFSRHGLLTTVAYklgPQAPTIYAIeGAVSV 342
Cdd:cd07808 224 GLP-EGTpvvagAGDNAAAALGAGVVEPGDALISLGTSGVVFAPT-DKPVPDPKGRLHTFPH---AVPGKWYAM-GVTLS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 343 AGHALSWLQNKvrILPDSRDAEKYAEMV----PTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESI 418
Cdd:cd07808 298 AGLSLRWLRDL--FGPDRESFDELDAEAakvpPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGV 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24655555 419 CFQTRDILECMHqECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGV 487
Cdd:cd07808 376 AFSLRDSLEVLK-ELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGV 443
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
32-486 |
8.17e-73 |
|
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: 239.41 E-value: 8.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 32 LVGvIDEGT---KTIGFSiyttPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPeqgfsASDIVTV 108
Cdd:cd07773 2 LLG-IDIGTtnvKAVLFD----EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG-----PDPIAAI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 109 GITNQRETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVqDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIR 188
Cdd:cd07773 72 SVSSQGESGVPVDR-DGEPLGPAIVWFDPRGKEEAEELAERI-GAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 189 errcKAGTVDSWIVWNLTnGAlHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRG 268
Cdd:cd07773 150 ----KWLSVADYIAYRLT-GE-PVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 269 mtLSG----IMG--NQQASLLGQMCVKPGQTKNTyrSGCFL-LCNTGDKPVFSRHGLLTTVAYklGPQAPTIYAIEGAVS 341
Cdd:cd07773 224 --LPAgtpvVVGghDHLCAALGAGVIEPGDVLDS--TGTAEaLLAVVDEPPLDEMLAEGGLSY--GHHVPGGYYYLAGSL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 342 VAGHALSWLQNKVRILPDSRDAEKY--AEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESIC 419
Cdd:cd07773 298 PGGALLEWFRDLFGGDESDLAAADElaEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24655555 420 FQTRDILECMhQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADG 486
Cdd:cd07773 378 FELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
32-284 |
3.11e-68 |
|
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: 221.06 E-value: 3.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 32 LVGVIDEGT---KTIGFSiyttPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLpeqGFSASDIVTV 108
Cdd:pfam00370 1 YYLGIDCGTtstKAILFN----EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQL---GISLKQIKGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 109 GITNQRETTIVWDAVTgKPLYNALLWKDIRTSTTVEQIVAKVqDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIR 188
Cdd:pfam00370 74 GISNQGHGTVLLDKND-KPLYNAILWKDRRTAEIVENLKEEG-NNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 189 errcKAGTVDSWIVWNLTNgaLHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRG 268
Cdd:pfam00370 152 ----KFLTIHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWG 225
|
250 260
....*....|....*....|
gi 24655555 269 MT----LSGIMGNQQASLLG 284
Cdd:pfam00370 226 LDegvpVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
35-523 |
4.66e-65 |
|
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: 220.12 E-value: 4.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 35 VIDEGTKTIGFSIYTtPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPeqgfsASDIVTVGITNQR 114
Cdd:cd07770 4 GIDIGTTSTKAVLFD-EDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG-----GGEVDAIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 115 ETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIvAKVQDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRerrcKA 194
Cdd:cd07770 78 HSLLGVDE-DGEPLTPVITWADTRAAEEAERL-RKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAA----KF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 195 GTVDSWIVWNLTNGalHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERS---PLRGMT- 270
Cdd:cd07770 152 VSIKEYLLYRLTGE--LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAerlGLLAGTp 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 271 -LSGImGNQQASLLGQMCVKPGQtkntyrsgcfLLCNTG---------DKPVFSRHGLLTTvaYKLGPQAptiYAIEGAV 340
Cdd:cd07770 230 vVLGA-SDGALANLGSGALDPGR----------AALTVGtsgairvvsDRPVLDPPGRLWC--YRLDENR---WLVGGAI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 341 SVAGHALSWLQNKVRILPDS-RDAEKYAE-MVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESI 418
Cdd:cd07770 294 NNGGNVLDWLRDTLLLSGDDyEELDKLAEaVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 419 CFQTRDILECMhQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVNLCQFEPEKRY 498
Cdd:cd07770 374 AFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEADELVK 452
|
490 500
....*....|....*....|....*
gi 24655555 499 YENVHydtflatTTDVERKERYGKW 523
Cdd:cd07770 453 IGKVV-------EPDPENHAIYAEL 470
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
35-487 |
7.61e-62 |
|
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: 211.61 E-value: 7.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 35 VIDEGT---KTIGFSIyttpDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQlpeQGFSASDIVTVGIT 111
Cdd:cd07805 4 AIDLGTsgvKAALVDL----DGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEK---SGIDPSDIAAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 112 NQRETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVQDPNHFRSSTGLPISTYFSALKIRWLRDNVPEvrqaIRERR 191
Cdd:cd07805 77 GQMQGVVPVDK-DGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSGKDPLAKILWLKENEPE----IYAKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 192 CKA-GTVDsWIVWNLTnGALhITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSplRGMT 270
Cdd:cd07805 152 HKFlDAKD-YLNFRLT-GRA-ATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAA--AELG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 271 LS-GI-----MGNQQASLLGQMCVKPGQTkNTY--RSGcFLLCNTGDKPVFSRHGLLTtvaykLGPQAPTIYAIEGAVSV 342
Cdd:cd07805 227 LPaGTpvvggGGDAAAAALGAGAVEEGDA-HIYlgTSG-WVAAHVPKPKTDPDHGIFT-----LASADPGRYLLAAEQET 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 343 AGHALSWLQNKVrILPDSRDAEKYAEM-------VPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAAL 415
Cdd:cd07805 300 AGGALEWARDNL-GGDEDLGADDYELLdelaaeaPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVL 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24655555 416 ESICFQTRDILECMHQECGyEINKLHADGKLTTNNLLMQLQADTIGMPVFR-SQLMDSTAFGAAMCAAQADGV 487
Cdd:cd07805 379 EGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVpENPQEAGALGAALLAAVGLGL 450
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
32-482 |
4.46e-55 |
|
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: 192.74 E-value: 4.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 32 LVGvIDEGT---KtigfSIYTTPDFKEIAAHRVELSVITPQDGWYEQDP---LEMMASInkcaeeaIKQLPEQ-GFSASD 104
Cdd:cd07804 2 LLG-IDIGTtgtK----GVLVDEDGKVLASASIEHDLLTPKPGWAEHDPevwWGAVCEI-------IRELLAKaGISPKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 105 IVTVGITNQRETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVqDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVR 184
Cdd:cd07804 70 IAAIGVSGLVPALVPVDE-NGKPLRPAILYGDRRATEEIEWLNENI-GEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 185 QAIRerrcKAGTVDSWIVWNLTnGALHItDVTNASRT-LLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSER 263
Cdd:cd07804 148 KKTR----KFLGAYDYIVYKLT-GEYVI-DYSSAGNEgGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 264 SPLRGMTlSGI-----MGNQQASLLGQMCVKPGQTKNTY-RSGCFLLCNtgDKPVFsrhglLTTVAYKLGPQaPTIYAIE 337
Cdd:cd07804 222 AEETGLA-EGTpvvagTVDAAASALSAGVVEPGDLLLMLgTAGDIGVVT--DKLPT-----DPRLWLDYHDI-PGTYVLN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 338 GAVSVAGHALSWLQNkvRILPDSRDAEKY------------AEMVP-TSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQF 404
Cdd:cd07804 293 GGMATSGSLLRWFRD--EFAGEEVEAEKSggdsaydlldeeAEKIPpGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLS 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655555 405 TRKNHIVRAALESICFQTRDILECMHQEcGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAA 482
Cdd:cd07804 371 HTRAHLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAG 447
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
32-486 |
6.08e-54 |
|
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: 189.30 E-value: 6.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 32 LVGvIDEGTKTIGFSIYTTpDFKEIAAHRVELSVITPQDGWYEQDPLEMmasINKCAEeAIKQLPEQ-GFSASDIVTVGI 110
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDL-DGREIAVASRPTPVISPRPGWAERDMDEL---WQATAE-AIRELLEKsGVDPSDIAGVGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 111 TNQRETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVQDPNHFRSSTGLPISTYFSALkIRWLRDNVPEVRQAIRer 190
Cdd:cd07802 76 TGHGNGLYLVDK-DGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVAL-LRWLKENEPERYDRIR-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 191 rcKAGTVDSWIVWNLTnGALHiTDVTNASrTLLMNLETQAWDPVLLKTFGIRE--EMLPTIHSCSEIFGKITSE---RSP 265
Cdd:cd07802 152 --TVLFCKDWIRYRLT-GEIS-TDYTDAG-SSLLDLDTGEYDDELLDLLGIEElkDKLPPLVPSTEIAGRVTAEaaaLTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 266 LR-GMTLSGIMGNQQASLLGQMCVKPGQTkntyrsgCFLL----CNTG--DKPVFSRHGLLTTVAYKLGpqapTIYAIEG 338
Cdd:cd07802 227 LPeGTPVAAGAFDVVASALGAGAVDEGQL-------CVILgtwsINEVvtDEPVVPDSVGSNSLHADPG----LYLIVEA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 339 AVSVAGhALSWLQN------KVRILPDSRDAEKYAEMV-PTSGDVYFVPaFtgLYAPYWRQNARGIIIGLTQFTRKNHIV 411
Cdd:cd07802 296 SPTSAS-NLDWFLDtllgeeKEAGGSDYDELDELIAAVpPGSSGVIFLP-Y--LYGSGANPNARGGFFGLTAWHTRAHLL 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655555 412 RAALESICFQTRDILECMHQECgyEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADG 486
Cdd:cd07802 372 RAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
299-484 |
7.36e-49 |
|
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: 168.27 E-value: 7.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 299 SGCFLLcnTGDKPVFSRHGLLTTVAyklGPQAPTIYAIEGAVSVAGHALSWLQNKVRILPDSRDAEK---YAEM-----V 370
Cdd:pfam02782 8 SSFVLV--ETPEPVLSVHGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAGNvesLAELaalaaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 371 PTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMHQECGYEINKLHADGKLTTNN 450
Cdd:pfam02782 83 APAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGGSRNP 162
|
170 180 190
....*....|....*....|....*....|....
gi 24655555 451 LLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQA 484
Cdd:pfam02782 163 LLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
36-487 |
8.74e-45 |
|
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: 165.79 E-value: 8.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGTKTIGFSIYTTPDFKEIAAHRVE--LSVITPQDGWYEQDPLEMMASInkcaEEAIKQ-LPEQGFSASDIVTVGITN 112
Cdd:cd07781 5 IDFGTQSVRAGLVDLADGEELASAVVPypTGYIPPRPGWAEQNPADYWEAL----EEAVRGaLAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 113 QRETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAkVQDPNH--FRSSTGLPIS--TYFSalKIRWLRDNVPEVRQAIR 188
Cdd:cd07781 81 TSSTVVPVDE-DGNPLAPAILWMDHRAQEEAAEINE-TAHPALeyYLAYYGGVYSseWMWP--KALWLKRNAPEVYDAAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 189 eRRCKAGtvdSWIVWNLTNgalHIT-DVTNASRTLLMNLETQAWDPVLLKTFG-----IREEMLPTIHSCSEIFGKITSE 262
Cdd:cd07781 157 -TIVEAC---DWINARLTG---RWVrSRCAAGHKWMYNEWGGGPPREFLAALDpgllkLREKLPGEVVPVGEPAGTLTAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 263 RSPLRGMTlSGI---MGNQQA--SLLGQMCVKPGQ-TKNTYRSGCFLLcnTGDKPVFSRhGLLTTVAyklGPQAPTIYAI 336
Cdd:cd07781 230 AAERLGLP-AGIpvaQGGIDAhmGAIGAGVVEPGTlALIMGTSTCHLM--VSPKPVDIP-GICGPVP---DAVVPGLYGL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 337 EGAVSVAGHALSWLQNKVRILPDSRDAEKYAEMV-------PTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNH 409
Cdd:cd07781 303 EAGQSAVGDIFAWFVRLFVPPAEERGDSIYALLSeeaaklpPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGTTPAH 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24655555 410 IVRAALESICFQTRDILECMhQECGYEINKLHADGKLTTNN-LLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGV 487
Cdd:cd07781 383 IYRALLEATAFGTRAIIERF-EEAGVPVNRVVACGGIAEKNpLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGV 460
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
36-484 |
3.14e-43 |
|
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: 159.70 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGTKTIGFSIYTtPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPeqgfsASDIVTVGITNQRE 115
Cdd:cd07783 5 IDLGTSGVRAVVVD-EDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELR-----PRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 116 TTIVWDAvTGKPLYNALLWKDIRtSTTVEQIVAKVQDPNHFRssTGLPISTYFSALKIRWLRDNVPEVRQAIRERRCKAg 195
Cdd:cd07783 79 TLVLVDR-EGEPLRPAIMYNDAR-AVAEAEELAEAAGAVAPR--TGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQA- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 196 tvDsWIVWNLTnGALHITDVTNASRTLLmNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKIT---SERSPLR----- 267
Cdd:cd07783 154 --D-WLAGRLT-GDRGVTDYNNALKLGY-DPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTaeaAEELGLPagtpv 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 268 --GMTLSgimgnqQASLLGQMCVKPGQtkntyrsgCFLLCNTG-------DKPVFSRHGLLTTvaYKLGPQAptiYAIEG 338
Cdd:cd07783 229 vaGTTDS------IAAFLASGAVRPGD--------AVTSLGTTlvlkllsDKRVPDPGGGVYS--HRHGDGY---WLVGG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 339 AVSVAGHALSWLQNKVRIlpdsRDAEKYAEMVPTSGdVYFVP-AFTGLYAPYWRQNARGIIIGLTQfTRKnHIVRAALES 417
Cdd:cd07783 290 ASNTGGAVLRWFFSDDEL----AELSAQADPPGPSG-LIYYPlPLRGERFPFWDPDARGFLLPRPH-DRA-EFLRALLEG 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24655555 418 ICFQTRDILECMHQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQlMDSTAFGAAMCAAQA 484
Cdd:cd07783 363 IAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAG 428
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
33-486 |
2.15e-39 |
|
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: 149.68 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 33 VGVIDEGTKTIGFS----IYTTPDFKEIAahrvelsvitpqdgwYEQDPLEMMASINKCAEEAIKQLpeqGFSASDIVTV 108
Cdd:cd07798 14 CALVDSEGKIVAIAyrewEYYTDDDYPDA---------------KEFDPEELWEKICEAIREALKKA---GISPEDISAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 109 GITNQRETTIVWDAvTGKPLYnALLWKDIRTSTTVEQIVAKVQDPNHFRssTGLPISTYFSALKIRWLRDNVPEVRQAIR 188
Cdd:cd07798 76 SSTSQREGIVFLDK-DGRELY-AGPNIDARGVEEAAEIDDEFGEEIYTT--TGHWPTELFPAARLLWFKENRPEIFERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 189 errcKAGTVDSWIVWNLTnGALHItDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSplRG 268
Cdd:cd07798 152 ----TVLSISDWIGYRLT-GELVS-EPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAA--RE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 269 MTLSG----IMG--NQQASLLGQMCVKPGQTkntyrsgCFLLCNTG------DKPVFSRHGLLTTVAYKLgpqaPTIYAI 336
Cdd:cd07798 224 LGLPEgtpvVVGgaDTQCALLGSGAIEPGDI-------GIVAGTTTpvqmvtDEPIIDPERRLWTGCHLV----PGKWVL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 337 EGAVSVAGHALSWLqnKVRILPDSRD-----AEKYAEMVPTSGDVYfvpAFTGLYAPywrqNARGIIIGLTQF------- 404
Cdd:cd07798 293 ESNAGVTGLNYQWL--KELLYGDPEDsyevlEEEASEIPPGANGVL---AFLGPQIF----DARLSGLKNGGFlfptpls 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 405 ----TRKnHIVRAALESICFQTRDILECMHQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMC 480
Cdd:cd07798 364 aselTRG-DFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAIC 442
|
....*.
gi 24655555 481 AAQADG 486
Cdd:cd07798 443 AAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
36-482 |
9.50e-39 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 147.70 E-value: 9.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGTKTIGFSIYTTPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLpeqGFSASDIVTVGITNQRE 115
Cdd:cd07809 5 IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDA---GAELRDVAAIGISGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 116 TTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVQDPnhFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRerrcKAG 195
Cdd:cd07809 82 GLVALDA-DGKVLRPAKLWCDTRTAPEAEELTEALGGK--KCLLVGLNIPARFTASKLLWLKENEPEHYARIA----KIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 196 TVDSWIVWNLTNGAlhITDVTNASRTLLMNLETQAWDPVLLKTF---GIREEMLPTIHSCSEIFGKITSERSPLRGMTlS 272
Cdd:cd07809 155 LPHDYLNWKLTGEK--VTGLGDASGTFPIDPRTRDYDAELLAAIdpsRDLRDLLPEVLPAGEVAGRLTPEGAEELGLP-A 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 273 GIM-----GNQQASLLGQMCVKPGQ------TkntyrSGCflLCNTGDKPVFSRHGLLTTVAYKLGPQAPtiyaiegAVS 341
Cdd:cd07809 232 GIPvapgeGDNMTGALGTGVVNPGTvavslgT-----SGT--AYGVSDKPVSDPHGRVATFCDSTGGMLP-------LIN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 342 VAGHALSWLqNKVRILPDSrDAEKYAEMV----PTSGDVYFVPAFTGLYAPYWRqNARGIIIGLT--QFTRKnHIVRAAL 415
Cdd:cd07809 298 TTNCLTAWT-ELFRELLGV-SYEELDELAaqapPGAGGLLLLPFLNGERTPNLP-HGRASLVGLTlsNFTRA-NLARAAL 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24655555 416 ESICFQTRDILECMHQEcGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAA 482
Cdd:cd07809 374 EGATFGLRYGLDILREL-GVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAA 439
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
32-486 |
1.12e-36 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 141.99 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 32 LVGvIDEGT---KTIGFSIyttpDFKEIAAHRVELSVITPQDGWYEQDpleMMASINKCAeEAIKQLPEQ-GFSASDIVT 107
Cdd:cd24121 2 LIG-IDAGTsvvKAVAFDL----DGRELAVAARRNAVLYPQPGWAEQD---MNETWQAVV-ATIREVVAKlDVLPDRVAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 108 VGITNQRETTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVQDPNHFRsSTGLPISTYFSALKIRWLRDNVPEVRQAI 187
Cdd:cd24121 73 IGVTGQGDGTWLVDE-DGRPVRDAILWLDGRAADIVERWQADGIAEAVFE-ITGTGLFPGSQAAQLAWLKENEPERLERA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 188 RER-RCKagtvdSWIVWNLTnGALhITDVTNASRTLLmNLETQAWDPVLLKTFGI--REEMLPTIHSCSEIFGKITSERS 264
Cdd:cd24121 151 RTAlHCK-----DWLFYKLT-GEI-ATDPSDASLTFL-DFRTRQYDDEVLDLLGLeeLRHLLPPIRPGTEVIGPLTPEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 265 PLRGMtLSGI---MG--NQQASLLGQMCVKPGQtkntyrsGCFLLCNTG------DKPVFSRHGLLTTVAykLGPQA--- 330
Cdd:cd24121 223 AATGL-PAGTpvvLGpfDVVATALGSGAIEPGD-------ACSILGTTGvhevvvDEPDLEPEGVGYTIC--LGVPGrwl 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 331 ---PTIYA---IEGAVSVAGHALSWLQNKVRILpDSRDAEKYAEMVPT-SGDVYFVP--AFTGLYAPYWRQNARGIIIGL 401
Cdd:cd24121 293 ramANMAGtpnLDWFLRELGEVLKEGAEPAGSD-LFQDLEELAASSPPgAEGVLYHPylSPAGERAPFVNPNARAQFTGL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 402 TQFTRKNHIVRAALESICFQTRDILECMhqecGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCA 481
Cdd:cd24121 372 SLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNA 447
|
....*
gi 24655555 482 AQADG 486
Cdd:cd24121 448 AVALG 452
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
36-481 |
1.84e-33 |
|
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: 132.73 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGTKTIGFSIYTTPDFKEIAAHRVELSVITPQD--GWYEQDPLEMMASINKCaeeaIKQLPEqgFSASDIVTVGITNQ 113
Cdd:cd07777 5 IDIGTTSIKAALLDLESGRILESVSRPTPAPISSDdpGRSEQDPEKILEAVRNL----IDELPR--EYLSDVTGIGITGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 114 RETTIVWDAvTGKPLYNALLWKDIRTST----TVEQIVAKVQDPNHFRSSTGLPISTYFsalkirWLRdnvpeVRQAIRE 189
Cdd:cd07777 79 MHGIVLWDE-DGNPVSPLITWQDQRCSEeflgGLSTYGEELLPKSGMRLKPGYGLATLF------WLL-----RNGPLPS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 190 RRCKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSplRGM 269
Cdd:cd07777 147 KADRAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALP--KGI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 270 TLSGIMGNQQASLLG-----------------QMCVkpgQTKNTYRSGCFLLcntgdKPVFSRHGLLTtvayklgpqapt 332
Cdd:cd07777 225 PVYVALGDNQASVLGsglneendavlnigtgaQLSF---LTPKFELSGSVEI-----RPFFDGRYLLV------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 333 iyaieGAVSVAGHALSWLQNKVR-----ILPDSRDAEKYAEM-----VPTSGDVYFVPAFTGlyaPYWRQNARGII--IG 400
Cdd:cd07777 285 -----AASLPGGRALAVLVDFLRewlreLGGSLSDDEIWEKLdelaeSEESSDLSVDPTFFG---ERHDPEGRGSItnIG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 401 LTQFTRKNhIVRAALESICfqtRDILECMHQEC--GYEINKLHADGK-LTTNNLLMQLQADTIGMPVFRSQLMDSTAFGA 477
Cdd:cd07777 357 ESNFTLGN-LFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGA 432
|
....
gi 24655555 478 AMCA 481
Cdd:cd07777 433 ALLA 436
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
375-487 |
1.69e-18 |
|
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: 88.75 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 375 DVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVR---AALESICFQTRDILECMhQECGYEINKLHADGKLTTNNL 451
Cdd:cd07782 380 DLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAM-NAAGHKIDTIFMCGGLSKNPL 458
|
90 100 110
....*....|....*....|....*....|....*.
gi 24655555 452 LMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGV 487
Cdd:cd07782 459 FVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGD 494
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
36-531 |
4.97e-18 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 86.94 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGTKTIGfSIYTTPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKcaeeAIKQLPEQgFSASDIVTVGITNQRE 115
Cdd:PRK15027 5 IDLGTSGVK-VILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDR----AMKALGDQ-HSLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 116 TTIVWDAvTGKPLYNALLWKDIRTSTTVEQIVAKVQDPnhfRSSTGLPISTYFSALKIRWLRDNVPEVRQAIrerrCKAG 195
Cdd:PRK15027 79 GATLLDA-QQRVLRPAILWNDGRCAQECALLEARVPQS---RVITGNLMMPGFTAPKLLWVQRHEPEIFRQI----DKVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 196 TVDSWIVWNLTnGALhITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRGMTLSGIM 275
Cdd:PRK15027 151 LPKDYLRLRMT-GEF-ASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 276 ---GNQQASLLGQMCVKPGQTKNTY-RSGCFLLCNTG--DKPVFSRHGLLTTVayklgpqaPTIYAIEGAVSVAGHALSW 349
Cdd:PRK15027 229 aggGDNAAGAVGVGMVDANQAMLSLgTSGVYFAVSEGflSKPESAVHSFCHAL--------PQRWHLMSVMLSAASCLDW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 350 ------LQNKVRILPDSRDAEKYAemvptsGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTR 423
Cdd:PRK15027 301 aakltgLSNVPALIAAAQQADESA------EPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 424 DILECMHqECGYEINKLHADGKLTTNNLLMQLQADTIGMPV-FRSQLMDSTAFGAAMCA--AQADGVNLCQFEPEKRyYE 500
Cdd:PRK15027 375 DGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAqiAANPEKSLIELLPQLP-LE 452
|
490 500 510
....*....|....*....|....*....|.
gi 24655555 501 NVHYdtflattTDVERKERYGKwKRAVERSL 531
Cdd:PRK15027 453 QSHL-------PDAQRYAAYQP-RRETFRRL 475
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
72-500 |
5.60e-18 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 87.01 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 72 WYEQDPLEMMASINKCAEEAIKQLPEQGFSASDIVTVGItnqrETTIVWDAvtGKPLYNALLWKDIRTSTTVEQIvAKVQ 151
Cdd:PRK10331 44 WHQWSLDAILQRFADCCRQINSELTECHIRGITVTTFGV----DGALVDKQ--GNLLYPIISWKCPRTAAVMENI-ERYI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 152 DPNHFRSSTGlpISTY-FSAL-KIRWLRDNVPEV-RQAirerrckagtvDSWI-VWNLTNGAL---HITDVTNASRTLLM 224
Cdd:PRK10331 117 SAQQLQQISG--VGAFsFNTLyKLVWLKENHPQLlEQA-----------HAWLfISSLINHRLtgeFTTDITMAGTSQML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 225 NLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRGMTlSGI----MG-NQQASLLGqmcvkpgqtkntyrS 299
Cdd:PRK10331 184 DIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLP-VGIpvisAGhDTQFALFG--------------S 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 300 GCFLlcntgDKPVFSRHGLLTTVAYKLGPQAPTIYAIEGAV----SVAGH---ALSWLQNKV----RILPDSRDaEKYAE 368
Cdd:PRK10331 249 GAGQ-----NQPVLSSGTWEILMVRSAQVDTSLLSQYAGSTceldSQSGLynpGMQWLASGVlewvRKLFWTAE-TPYQT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 369 MV-------PTSGDVYFVPAFTGlyapywrqNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMHQECGYEINKLH 441
Cdd:PRK10331 323 MIeearaipPGADGVKMQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24655555 442 ADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCA------------AQAdgvnlcQFEPEKRYYE 500
Cdd:PRK10331 395 LVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGwygvgefsspeqARA------QMKYQYRYFY 459
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
84-487 |
1.06e-17 |
|
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: 86.23 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 84 INKCAEEAIKQLpeqGFSASDIVTVGITNQRETTIVWDAvTGKPLY---NAllwkDIRTSTTVEQIvaKVQDP---NHFR 157
Cdd:cd07775 54 ICECIREALKKA---GIAPKSIAAISTTSMREGIVLYDN-EGEEIWacaNV----DARAAEEVSEL--KELYNtleEEVY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 158 SSTGlpiSTY-FSAL-KIRWLRDNVPEVRQAIrerrCKAGTVDSWIVWNLTnGALhITDVTNASRTLLMNLETQAWDPVL 235
Cdd:cd07775 124 RISG---QTFaLGAIpRLLWLKNNRPEIYRKA----AKITMLSDWIAYKLS-GEL-AVEPSNGSTTGLFDLKTRDWDPEI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 236 LKTFGIREEMLPTIHSCSEIFGKITSERSPLRGMTlSGIM-----GNQQASLLGQMCVKPGQTknTYRSGCF--LLCNTg 308
Cdd:cd07775 195 LEMAGLKADILPPVVESGTVIGKVTKEAAEETGLK-EGTPvvvggGDVQLGCLGLGVVRPGQT--AVLGGSFwqQEVNT- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 309 DKPVFSRHGLLTTVAYKLgpqaPTIYAIEGAVSVAGHALSWLQN------KVRILPDSRDA----EKYAEMVPtSGDVYF 378
Cdd:cd07775 271 AAPVTDPAMNIRVNCHVI----PDMWQAEGISFFPGLVMRWFRDafcaeeKEIAERLGIDAydllEEMAKDVP-PGSYGI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 379 VPAFTGL--YApYWRQNARGII---IGLTQFTRKNhIVRAALESICFQTRDILECMHQECGYEINKLHADGKLTTNNLLM 453
Cdd:cd07775 346 MPIFSDVmnYK-NWRHAAPSFLnldIDPEKCNKAT-FFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWC 423
|
410 420 430
....*....|....*....|....*....|....
gi 24655555 454 QLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGV 487
Cdd:cd07775 424 QILADVLGLPVKVPVVKEATALGAAIAAGVGAGI 457
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
36-487 |
2.54e-17 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 84.98 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGTKTIGFSIYTTPDFKEIAAHRVELSV-ITPQDGWYEQDPLEMMASINKCAEEAIKQlpeQGFSASDIVTVGITN-- 112
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIR---EGVDAYEVKGCGVDAtc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 113 -----QRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAkvQDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRqai 187
Cdd:cd07768 82 slaifDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINM--QCPQQLLDYLGGKISPEMGVPKLKYFLDEYSHLR--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 188 rERRCKAGTVDSWIVWNLTNgalhitDVTNASRTLL----MNLETQAWDPVLLKTFGIREE------MLPTIHSCSEIFG 257
Cdd:cd07768 157 -DKHFHIFDLHDYIAYELTR------LYEWNICGLLgkenLDGEESGWSSSFFKNIDPRLEhltttkNLPSNVPIGTTSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 258 KITSERSPLRGMTLS---------------GIMG-NQQASLLGQM----CVKPGQTKNTYRSGCFLLCNTGDKPVFSRH- 316
Cdd:cd07768 230 VALPEMAEKMGLHPGtavvvscidahaswfAVASpHLETSLFMIAgtssCHMYGTTISDRIPGVWGPFDTIIDPDYSVYe 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 317 ------GLLTTVAYKLGPQAPTI-YAIEGAVSVagHALswLQNKVRilpdsrDAEKYAEMvptSGDVYFVPAFTGLYAPY 389
Cdd:cd07768 310 agqsatGKLIEHLFESHPCARKFdEALKKGADI--YQV--LEQTIR------QIEKNNGL---SIHILTLDMFFGNRSEF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 390 WRQNARGIIIGLTQFTRK---NHIVRAALESICFQTRDILECMHQEcGYEINKLHADGKLTTNNLLMQLQADTIGMPVFR 466
Cdd:cd07768 377 ADPRLKGSFIGESLDTSMlnlTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELRASGGQAKNERLLQLIALVTNVAIIK 455
|
490 500
....*....|....*....|.
gi 24655555 467 SQLMDSTAFGAAMCAAQADGV 487
Cdd:cd07768 456 PKENMMGILGAAVLAKVAAGK 476
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
388-487 |
1.05e-15 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 80.28 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 388 PYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMHQEcGYEINKLHADGKLTTNN-LLMQLQADTIGMPVfr 466
Cdd:PRK04123 391 PLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQ-GVPVEEVIAAGGIARKNpVLMQIYADVLNRPI-- 467
|
90 100
....*....|....*....|....
gi 24655555 467 sQLMDS---TAFGAAMCAAQADGV 487
Cdd:PRK04123 468 -QVVASdqcPALGAAIFAAVAAGA 490
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
88-293 |
1.67e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 70.03 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 88 AEEAIKQ-LPEQGFSASDIVTVGITNQRETTIVWDAvTGKPLYnALLWKDIRTSttvEQIVAKVQDPNHFRS----STGl 162
Cdd:PRK10939 57 ACQCIRQaLQKAGIPASDIAAVSATSMREGIVLYDR-NGTEIW-ACANVDARAS---REVSELKELHNNFEEevyrCSG- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 163 piSTY-FSAL-KIRWLRDNVPEVRQAIRerrcKAGTVDSWIVWNLTnGALHItDVTNASRTLLMNLETQAWDPVLLKTFG 240
Cdd:PRK10939 131 --QTLaLGALpRLLWLAHHRPDIYRQAH----TITMISDWIAYMLS-GELAV-DPSNAGTTGLLDLVTRDWDPALLEMAG 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24655555 241 IREEMLPTIHSCSEIFGKITSERSPLRGMtLSG---IMGNQQASL--LGQMCVKPGQT 293
Cdd:PRK10939 203 LRADILPPVKETGTVLGHVTAKAAAETGL-RAGtpvVMGGGDVQLgcLGLGVVRPGQT 259
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
52-486 |
2.49e-11 |
|
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: 66.01 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 52 DFKEIaaHRVELSVITPQDGWYeQDPLEMMASInkcaEEAIKQLPEQGfsaSDIVTVGITnqreTTIVwDAV----TGKP 127
Cdd:cd07771 25 ELEEI--HRFPNRPVEINGHLY-WDIDRLFDEI----KEGLKKAAEQG---GDIDSIGID----TWGV-DFGlldkNGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 128 LYNALLWKDIRTSTTVEQIVAKVQDPNHFRSsTG---LPISTYFsalKIRWLRDNVPEVRQairerrcKAGTV----DsW 200
Cdd:cd07771 90 LGNPVHYRDPRTEGMMEELFEKISKEELYER-TGiqfQPINTLY---QLYALKKEGPELLE-------RADKLlmlpD-L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 201 IVWNLTNGAlhITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRGmtLSGI-----M 275
Cdd:cd07771 158 LNYLLTGEK--VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELG--LKGIpviavA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 276 GNQQASLLgqMCVkPGQTKNTYrsgcFLLCNT----G---DKPVfsrhglLTTVAYKLGpqaptiYAIEGAV-------- 340
Cdd:cd07771 234 SHDTASAV--AAV-PAEDEDAA----FISSGTwsliGvelDEPV------ITEEAFEAG------FTNEGGAdgtirllk 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 341 SVAGhalSWL-QNKVRILPDSRDAEKYAEMV----PTSGDVYFV----PAFtglyapywrQNARGIIIGLTQFTRKN--- 408
Cdd:cd07771 295 NITG---LWLlQECRREWEEEGKDYSYDELValaeEAPPFGAFIdpddPRF---------LNPGDMPEAIRAYCRETgqp 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 409 ------HIVRAALESICFQTRDILECMHQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSqLMDSTAFGAAMCAA 482
Cdd:cd07771 363 vpespgEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQL 441
|
....
gi 24655555 483 QADG 486
Cdd:cd07771 442 IALG 445
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
36-478 |
2.15e-04 |
|
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: 43.93 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 36 IDEGTKTIGFSIYTTPDfKEIAAHRVELS-VITPQDGWY-EQDPLEMMASINKCAEEAIKQLPEQ-----GFSASDIVTV 108
Cdd:cd07778 5 IDVGSTSVRIGIFDYHG-TLLATSERPISyKQDPKDLWFvTQSSTEIWKAIKTALKELIEELSDYivsgiGVSATCSMVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 109 GitnQRETT----IVWDAVTGK--PLYNALLWKDIRTSTTVEQIVAKVQDP--NHFRSS----TGLPistyfsalKIRWL 176
Cdd:cd07778 84 M---QRDSDtsylVPYNVIHEKsnPDQDIIFWMDHRASEETQWLNNILPDDilDYLGGGfipeMAIP--------KLKYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 177 RDNVPEvrqaIRERRCKAGTVDSWIVWNLTNGALHITDV-TNASRTLLMNL--ETQAWDPVLLKTFGIR----------E 243
Cdd:cd07778 153 IDLIKE----DTFKKLEVFDLHDWISYMLATNLGHSNIVpVNAPPSIGIGIdgSLKGWSKDFYSKLKIStkvcnvgntfK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 244 EMLPTIHSCSEIfGKITSERSPLRGMTLSGIMGNQ----QASLLGQMCVKPgqTKNTY------RSGCFLLCNT------ 307
Cdd:cd07778 229 EAPPLPYAGIPI-GKVNVILASYLGIDKSTVVGHGcidcYAGWFSTFAAAK--TLDTTlfmvagTSTCFLYATSssqvgp 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 308 ------------GDKPVF----SRHGLLTTVAYKLGPQAPTIyaiegavsVAGHALSW--LQNKVRILPDSR-DAEKY-- 366
Cdd:cd07778 306 ipgiwgpfdqllKNYSVYeggqSATGKLIEKLFNSHPAIIEL--------LKSDANFFetVEEKIDKYERLLgQSIHYlt 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 367 AEMVpTSGDVYfvpaftGLYAPYWRQNARGIIIG-LTQFTRKNHIVR--AALESICFQTRDILECMHQECGyEINKLHAD 443
Cdd:cd07778 378 RHMF-FYGDYL------GNRTPYNDPNMSGSFIGeSTDSSLTDLVLKyiLILEFLAFQTKLIIDNFQKEKI-IIQKVVIS 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 24655555 444 GKLTTNNLLMQLQA---DTIGMPVFRSQLMDSTAFGAA 478
Cdd:cd07778 450 GSQAKNARLLQLLStvlSKIHIIVPLSDSKYAVVKGAA 487
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
368-522 |
7.65e-04 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; 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. The subfamily includes XKs mainly from eukaryote. 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: 466795 [Multi-domain] Cd Length: 514 Bit Score: 42.16 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655555 368 EMVPTS--GDVYFVPAFTGLYAPYWRQNARGIIIGltQFTRKnhivRAALESICFQTRdilecmhqecgyeINKLHADGK 445
Cdd:cd07776 374 EITPPVpgGGRRFFGDDGVDAFFDPAVEVRAVVES--QFLSM----RLHAERLGSDIP-------------PTRILATGG 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655555 446 LTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQA-DGVNLCQFEPEKRYYENVHYDtfLATTTDVERKERYGK 522
Cdd:cd07776 435 ASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGlLCAGSGDFSPEFVVFSAEEPK--LVAEPDPEAAEVYDK 510
|
|
| |
