|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-441 |
0e+00 |
|
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: 574.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERDVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQL---DGEQRAQVRGISVSGQQ 79
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLlkdAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 80 HGFVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGGAAGsvAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHD 159
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKC--LLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 160 YVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLRDALPPLVETGTVY-ALSDAAAEALNLPAGVLVTTG 238
Cdd:cd07809 159 YLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDLRDLLPEVLPAGEVAgRLTPEGAEELGLPAGIPVAPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 239 GGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSSSGGWLPLICTMNC-TVATEAVMRMFSITRE 317
Cdd:cd07809 239 EGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDSTGGMLPLINTTNClTAWTELFRELLGVSYE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 318 QTEALIASTTPGADGLVLLPFFNGERTPDLPTARGCLFGMDLHNTSPAHFYRAAMEGATYSLRNGFDAFVAAGLQFDTIL 397
Cdd:cd07809 319 ELDELAAQAPPGAGGLLLLPFLNGERTPNLPHGRASLVGLTLSNFTRANLARAALEGATFGLRYGLDILRELGVEIDEIR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1198216907 398 LTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWAC 441
Cdd:cd07809 399 LIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGA 442
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
5-488 |
0e+00 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 516.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 5 IGLDVGTQSVKLVAYDpQERDVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQL---DGEQRAQVRGISVSGQQHG 81
Cdd:TIGR01312 1 LGIDLGTSGVKALLVD-EQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELleqASEMGQDIKGIGISGQMHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 82 FVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGgAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHDYV 161
Cdd:TIGR01312 80 LVLLDANGEVLRPAILWNDTRTAQECEELEAELG-DERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 162 NFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVE-TGTVYALSDAAAEALNLPAGVLVTTGGG 240
Cdd:TIGR01312 159 RYRLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQ---LPELIEsSEKAGTVRPEVAARLGLSAGVPVAAGGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 241 DNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSSS-GGWLPLICTMNCTVATEAVMRMF-SITREQ 318
Cdd:TIGR01312 236 DNAAGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALpGGWLPMGVTLSATSSLEWFRELFgKEDVEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 319 TEALIASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDlHNTSPAHFYRAAMEGATYSLRNGFDAFV-AAGLQFDTI 396
Cdd:TIGR01312 316 LNELAEQSPPGAEGVTFLPYLNGERTPHLdPQARGSFIGLT-HNTTRADLTRAVLEGVTFALRDSLDILReAGGIPIQSI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 397 LLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWACdrddgGADALSDVVLEHLQIDHTlSARPDPQRVVQ 476
Cdd:TIGR01312 395 RLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWAL-----GEKDLAALCSEAVVKQTE-SVLPIAENVEA 468
|
490
....*....|..
gi 1198216907 477 YQQHYQNFLKHL 488
Cdd:TIGR01312 469 YEELYERYKKLY 480
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-496 |
2.25e-173 |
|
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: 497.05 E-value: 2.25e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQL---DGEQRAQVRGISVSGQQ 79
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGE-VVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELlakAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 80 HGFVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGGAAgSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHD 159
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEA-LYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 160 YVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVYA-LSDAAAEALNLPAGVLVTTG 238
Cdd:COG1070 160 YLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDREL---LPELVPPGEVAGtLTAEAAAETGLPAGTPVVAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 239 GGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSSS-GGWLPLICTMNCTVATEAVMRMFSITR- 316
Cdd:COG1070 237 AGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVpGRWLPMGATNNGGSALRWFRDLFADGEl 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 317 ---EQTEALIASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFVAAGLQ 392
Cdd:COG1070 317 ddyEELNALAAEVPPGADGLLFLPYLSGERTPHWdPNARGAFFGLTLS-HTRAHLARAVLEGVAFALRDGLEALEEAGVK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 393 FDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWACdrddGGADALSDVVLEHLQIDHTlsARPDPQ 472
Cdd:COG1070 396 IDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGL----GLYDDLEEAAAAMVRVGET--IEPDPE 469
|
490 500
....*....|....*....|....
gi 1198216907 473 RVVQYQQHYQNFLKHLRGVTPLYA 496
Cdd:COG1070 470 NVAAYDELYERYRELYPALKPLFE 493
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-486 |
8.65e-140 |
|
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: 411.16 E-value: 8.65e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQL---DGEQRAQVRGISVSGQQ 79
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGR-VLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELlakAGISPSDIAAIGLTGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 80 HGFVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGGAAgsVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHD 159
Cdd:cd07808 80 HGLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEI--LIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 160 YVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVE----TGTVyalSDAAAEALNLPAGVLV 235
Cdd:cd07808 158 YLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSI---LPPIVEsteiVGTL---TPEAAEELGLPEGTPV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 236 TTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCS-SSGGWLPLICTMNCTVATEAVMRMFSI 314
Cdd:cd07808 232 VAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHaVPGKWYAMGVTLSAGLSLRWLRDLFGP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 315 TREQTEALI---ASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFVAAG 390
Cdd:cd07808 312 DRESFDELDaeaAKVPPGSEGLLFLPYLSGERTPYWdPNARGSFFGLSLS-HTRAHLARAVLEGVAFSLRDSLEVLKELG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 391 LQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWACdrddGGADALSDVVLEHLQIDHTLsaRPD 470
Cdd:cd07808 391 IKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGA----GVFDDLEEAAAACIKIEKTI--EPD 464
|
490
....*....|....*.
gi 1198216907 471 PQRVVQYQQHYQNFLK 486
Cdd:cd07808 465 PERHEAYDELYARYRE 480
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
5-485 |
3.70e-103 |
|
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: 317.15 E-value: 3.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 5 IGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQL---DGEQRAQVRGISVSGQQHG 81
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGE-LVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALlekSGIDPSDIAAIAFSGQMQG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 82 FVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGGAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHDYV 161
Cdd:cd07805 82 VVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 162 NFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVYA-LSDAAAEALNLPAGVLVTTGGG 240
Cdd:cd07805 162 NFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDK---LPELVPSTEVVGeLTPEAAAELGLPAGTPVVGGGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 241 DNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCS-SSGGWLPLICTMNCTVATEAVMRMFSITREQT 319
Cdd:cd07805 239 DAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASaDPGRYLLAAEQETAGGALEWARDNLGGDEDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 320 -------EALIASTTPGADGLVLLPFFNGERTP-DLPTARGCLFGMDLHNTsPAHFYRAAMEGATYSLRNGFDAFVAAGL 391
Cdd:cd07805 319 addyellDELAAEAPPGSNGLLFLPWLNGERSPvEDPNARGAFIGLSLEHT-RADLARAVLEGVAFNLRWLLEALEKLTR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 392 QFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPE-----GAAFGAGLQALWACDRDDggADALSDVVLEHlqidhtls 466
Cdd:cd07805 398 KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQeagalGAALLAAVGLGLLKSFDE--AKALVKVEKVF-------- 467
|
490
....*....|....*....
gi 1198216907 467 aRPDPQRVVQYQQHYQNFL 485
Cdd:cd07805 468 -EPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-437 |
1.46e-99 |
|
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: 304.87 E-value: 1.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPqERDVVATIAAPIELISRDDGTREQQA-QWW---IDGIVHCFAQLdGEQRAQVRGISVSGQ 78
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPeDWWqavVEAIREVLAKA-GIDPSDIAAIGISGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 79 QHGFVPVAADGSVTAPVKLWCDTstalecgqimdavggaagsvaiagnpimagytasklpwtRKHrpeayaamttVMLPH 158
Cdd:cd00366 79 MPGVVLVDADGNPLRPAIIWLDR---------------------------------------RAK----------FLQPN 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 159 DYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVY-ALSDAAAEALNLPAGVLVTT 237
Cdd:cd00366 110 DYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREK---LPPIVESGEVVgRVTPEAAEETGLPAGTPVVA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 238 GGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSSSGGWLPlictMNCTVATEAVMRMF----- 312
Cdd:cd00366 187 GGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRCHVVPGLWLL----EGAINTGGASLRWFrdefg 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 313 -----SITREQTEALIASTTPGADGLVLLPFFNGERTP-DLPTARGCLFGMDLhNTSPAHFYRAAMEGATYSLRNGFDAF 386
Cdd:cd00366 263 eeedsDAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPiWDPAARGVFFGLTL-SHTRAHLIRAVLEGVAYALRDNLEIL 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1198216907 387 VAAGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQA 437
Cdd:cd00366 342 EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-488 |
2.23e-96 |
|
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: 299.47 E-value: 2.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQ-LDGEQRAQVRGISVSGQQHG 81
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGR-VVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEvLAKLGGGEVDAIGFSSAMHS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 82 FVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGGAAgsvaIA---GNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPH 158
Cdd:cd07770 80 LLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSE----LYrrtGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 159 DYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDlrdALPPLVETGTVYA-LSDAAAEALNLPAGVLVTT 237
Cdd:cd07770 156 EYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEE---QLPELVDPTEVLPgLKPEFAERLGLLAGTPVVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 238 GGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSSSGGWLPLICTMNCTVATEAVMRMF---SI 314
Cdd:cd07770 233 GASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENRWLVGGAINNGGNVLDWLRDTLllsGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 315 TREQTEALIASTTPGADGLVLLPFFNGERTPD-LPTARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFVAAGLQF 393
Cdd:cd07770 313 DYEELDKLAEAVPPGSHGLIFLPYLAGERAPGwNPDARGAFFGLTLN-HTRADILRAVLEGVAFNLKSIYEALEELAGPV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 394 DTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAglqALWACDrddgGADALSDVVLEHLqIDHTLSARPDPQR 473
Cdd:cd07770 392 KEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGA---ALLALE----ALGLISSLEADEL-VKIGKVVEPDPEN 463
|
490
....*....|....*
gi 1198216907 474 VVQYQQHYQNFLKHL 488
Cdd:cd07770 464 HAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-441 |
3.19e-95 |
|
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: 295.27 E-value: 3.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQQAQ--WwiDGIVHCFAQLDGEQRA-QVRGISVSGQQ 79
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGR-ILASASRETPLIHPGPGWAELDPEelW--EAVKEAIREAAAQAGPdPIAAISVSSQG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 80 HGFVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGGAAgSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHD 159
Cdd:cd07773 78 ESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEE-LYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 160 YVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVYA-LSDAAAEALNLPAGVLVTTG 238
Cdd:cd07773 157 YIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASL---LPELVPSGTVIGtVTPEAAEELGLPAGTPVVVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 239 GGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPvVDDDARWAAFCSSSGGWLP----LICTMNCTVATEAVMRMFSI 314
Cdd:cd07773 234 GHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEP-PLDEMLAEGGLSYGHHVPGgyyyLAGSLPGGALLEWFRDLFGG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 315 TREQTEA---LIASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFVAAG 390
Cdd:cd07773 313 DESDLAAadeLAEAAPPGPTGLLFLPHLSGSGTPDFdPDARGAFLGLTLG-TTRADLLRAILEGLAFELRLNLEALEKAG 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1198216907 391 LQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWAC 441
Cdd:cd07773 392 IPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGA 442
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-441 |
4.66e-90 |
|
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: 282.49 E-value: 4.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQLD---GEQRAQVRGISVSGQQ 79
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGK-VLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLakaGISPKEIAAIGVSGLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 80 HGFVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGgAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHD 159
Cdd:cd07804 80 PALVPVDENGKPLRPAILYGDRRATEEIEWLNENIG-EDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 160 YVNFWLTGERFAEVGDASGTGWL-DVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVY-ALSDAAAEALNLPAGVLVTT 237
Cdd:cd07804 159 YIVYKLTGEYVIDYSSAGNEGGLfDIRKRTWDEELLEALGIDPDL---LPELVPSTEIVgEVTKEAAEETGLAEGTPVVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 238 GGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDArWAAFCSSSGGWLPLICTMNCTVATEAVMRMFSITRE 317
Cdd:cd07804 236 GTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRL-WLDYHDIPGTYVLNGGMATSGSLLRWFRDEFAGEEV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 318 QTE------------ALIASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHNTsPAHFYRAAMEGATYSLRNGFD 384
Cdd:cd07804 315 EAEksggdsaydlldEEAEKIPPGSDGLIVLPYFMGERTPIWdPDARGVIFGLTLSHT-RAHLYRALLEGVAYGLRHHLE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1198216907 385 AFVAAGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWAC 441
Cdd:cd07804 394 VIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGV 450
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
5-477 |
4.10e-88 |
|
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: 276.71 E-value: 4.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 5 IGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQL---DGEQRAQVRGISVSGQQHG 81
Cdd:cd07779 3 LGIDVGTTSTRAIIFDLDGN-IVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAvakAGVDPEDIAAIGLTSQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 82 FVPVAADGSVTAPVKLWCDTSTAlecgqimdavggaagsvaiagnpimagytasklpwtrkhrpeayaamtTVMLPHDYV 161
Cdd:cd07779 82 FVPVDEDGRPLRPAISWQDKRTA------------------------------------------------KFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 162 NFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVY-ALSDAAAEALNLPAGVLVTTGGG 240
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDK---LPELVPPGTVIgTLTKEAAEETGLPEGTPVVAGGG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 241 DNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSSS-GGWLPLICTMNCTVA----------TEAVM 309
Cdd:cd07779 191 DQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVpGKWVLEGSINTGGSAvrwfrdefgqDEVAE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 310 RMFSITREQT-EALIASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHNTsPAHFYRAAMEGATYSLRNGFDAFV 387
Cdd:cd07779 271 KELGVSPYELlNEEAAKSPPGSDGLLFLPYLAGAGTPYWnPEARGAFIGLTLSHT-RAHLARAILEGIAFELRDNLEAME 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 388 AAGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWACDRDDGGADALSDVVlehlQIDHTLsa 467
Cdd:cd07779 350 KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMV----RVTDTF-- 423
|
490
....*....|
gi 1198216907 468 RPDPQRVVQY 477
Cdd:cd07779 424 EPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
3-440 |
4.79e-83 |
|
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: 264.03 E-value: 4.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQ--QAQWwiDGIVHCFAQL---DGEQRAQVRGISVSG 77
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGR-EIAVASRPTPVISPRPGWAERdmDELW--QATAEAIRELlekSGVDPSDIAGVGVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 78 QQHGFVPVAADGSVTAPVKLWCDTSTALECGQIMDAvGGAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLP 157
Cdd:cd07802 78 HGNGLYLVDKDGKPVRNAILSNDSRAADIVDRWEED-GTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 158 HDYVNFWLTGERFAEVGDAsGTGWLDVRTRQWSERMLGAVDAqRDLRDALPPLVETGTVYA-LSDAAAEALNLPAGVLVT 236
Cdd:cd07802 157 KDWIRYRLTGEISTDYTDA-GSSLLDLDTGEYDDELLDLLGI-EELKDKLPPLVPSTEIAGrVTAEAAALTGLPEGTPVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 237 TGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDA-RWAAFCsSSGGWLPLICTMNCTVATEAVMRMF--- 312
Cdd:cd07802 235 AGAFDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVgSNSLHA-DPGLYLIVEASPTSASNLDWFLDTLlge 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 313 -----SITREQTEALIASTTPGADGLVLLPFFNGERtpDLPTARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFV 387
Cdd:cd07802 314 ekeagGSDYDELDELIAAVPPGSSGVIFLPYLYGSG--ANPNARGGFFGLTAW-HTRAHLLRAVYEGIAFSHRDHLERLL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1198216907 388 AAGlQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWA 440
Cdd:cd07802 391 VAR-KPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVA 442
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
3-496 |
3.23e-82 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 262.98 E-value: 3.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQErDVVA------TIAAPIELISRDDgtreqQAQWW--IDGIVHCFAQLDGEQraQVRGIS 74
Cdd:PRK15027 1 MYIGIDLGTSGVKVILLNEQG-EVVAsqteklTVSRPHPLWSEQD-----PEQWWqaTDRAMKALGDQHSLQ--DVKALG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 75 VSGQQHGFVPVAADGSVTAPVKLWCDTSTALECGQIMDAVggaAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTV 154
Cdd:PRK15027 73 IAGQMHGATLLDAQQRVLRPAILWNDGRCAQECALLEARV---PQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 155 MLPHDYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQrdlRDALPPLVE----TGTvyaLSDAAAEALNLP 230
Cdd:PRK15027 150 LLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLS---RDQMPALYEgseiTGA---LLPEVAKAWGMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 231 AgVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSSSGGWLPLICTM----NCTVATE 306
Cdd:PRK15027 224 T-VPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMlsaaSCLDWAA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 307 AVMRMFSITreqteALIASTTPG---ADGLVLLPFFNGERTP-DLPTARGCLFGMDlHNTSPAHFYRAAMEGATYSLRNG 382
Cdd:PRK15027 303 KLTGLSNVP-----ALIAAAQQAdesAEPVWFLPYLSGERTPhNNPQAKGVFFGLT-HQHGPNELARAVLEGVGYALADG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 383 FDAFVAAGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPE-GAAFGAGLQALWACDRDDGGADALSDVVLEHlqi 461
Cdd:PRK15027 377 MDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDvGPALGAARLAQIAANPEKSLIELLPQLPLEQ--- 453
|
490 500 510
....*....|....*....|....*....|....*
gi 1198216907 462 dhtlSARPDPQRVVQYQQHYQNFLKHLRGVTPLYA 496
Cdd:PRK15027 454 ----SHLPDAQRYAAYQPRRETFRRLYQQLLPLMA 484
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-441 |
2.14e-74 |
|
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: 240.97 E-value: 2.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPqERDVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQLDGEQR-AQVRGISVSGQQHG 81
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDE-DGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRpRRVVAIAVDGTSGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 82 FVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGGAAgsvAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHDYV 161
Cdd:cd07783 80 LVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVA---PRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 162 NFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVYA-LSDAAAEALNLPAGVLVTTGGG 240
Cdd:cd07783 157 AGRLTGDRGVTDYNNALKLGYDPETGRWPSWLLALLGIPPDL---LPRVVAPGTVIGtLTAEAAEELGLPAGTPVVAGTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 241 DNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSSSGGWLPLICTmNCTvaTEAVMRMFSitREQTE 320
Cdd:cd07783 234 DSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGDGYWLVGGAS-NTG--GAVLRWFFS--DDELA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 321 ALIASTTP-GADGLVLLPF-FNGERTP-DLPTARGCLFGmdlHNTSPAHFYRAAMEGATYSLRNGFDAFVAAGL-QFDTI 396
Cdd:cd07783 309 ELSAQADPpGPSGLIYYPLpLRGERFPfWDPDARGFLLP---RPHDRAEFLRALLEGIAFIERLGYERLEELGApPVEEV 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1198216907 397 LLTGGGSKSAQWRQMVADIFDLQVVVPiQPEGAAFGAGLQALWAC 441
Cdd:cd07783 386 RTAGGGARNDLWNQIRADVLGVPVVIA-EEEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
5-438 |
3.03e-62 |
|
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: 209.79 E-value: 3.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 5 IGLDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQ-QAQWWIDgIVHCFAQLD---GEQRAQVRGISVSGQQH 80
Cdd:cd24121 3 IGIDAGTSVVKAVAFDLDGR-ELAVAARRNAVLYPQPGWAEQdMNETWQA-VVATIREVVaklDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 81 GFVPVAADGSVTAPVKLWCDTSTAlECGQIMDAVGGAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHDY 160
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAA-DIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 161 VNFWLTGERFAEVGDASGTgWLDVRTRQWSERMLGAVDAQrDLRDALPPLVE-TGTVYALSDAAAEALNLPAGVLVTTGG 239
Cdd:cd24121 160 LFYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLE-ELRHLLPPIRPgTEVIGPLTPEAAAATGLPAGTPVVLGP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 240 GDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFC-SSSGGWLPLICTMNCTVATEAVMRMFS-ITRE 317
Cdd:cd24121 238 FDVVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVGYTIClGVPGRWLRAMANMAGTPNLDWFLRELGeVLKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 318 QT-----------EALIASTTPGADGLVLLPFF--NGERTPDL-PTARGCLFGMDLHnTSPAHFYRAAMEGATYSLRngf 383
Cdd:cd24121 318 GAepagsdlfqdlEELAASSPPGAEGVLYHPYLspAGERAPFVnPNARAQFTGLSLE-HTRADLLRAVYEGVALAMR--- 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1198216907 384 DAFVAAGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQAL 438
Cdd:cd24121 394 DCYEHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAA 448
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-486 |
2.52e-61 |
|
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: 208.93 E-value: 2.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERDVVATIAAPIEL--ISRDDGTREQQAQWWIDGIV----HCFAQLdGEQRAQVRGISVS 76
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLADGEELASAVVPYPTgyIPPRPGWAEQNPADYWEALEeavrGALAEA-GVDPEDVVGIGVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 77 GQQHGFVPVAADGSVTAPVKLWCDTSTALECGQImDAVGGAAGSVAIA--GNPIMAGYTASKLPWTRKHRPEAYAAMTTV 154
Cdd:cd07781 80 TTSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEI-NETAHPALEYYLAyyGGVYSSEWMWPKALWLKRNAPEVYDAAYTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 155 MLPHDYVNFWLTGErfaEVGDASGTG--WL-DVRTRQWSERMLGAVDA-QRDLRDALPPLVET-----GTvyaLSDAAAE 225
Cdd:cd07781 159 VEACDWINARLTGR---WVRSRCAAGhkWMyNEWGGGPPREFLAALDPgLLKLREKLPGEVVPvgepaGT---LTAEAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 226 ALNLPAGVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSG--TLFAYADHPV------VDD---DARWA--AFCSSSG-- 290
Cdd:cd07781 233 RLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTchLMVSPKPVDIpgicgpVPDavvPGLYGleAGQSAVGdi 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 291 -GWLPLICtmnCTVATEAVMRMFSITREQTEALiastTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHnTSPAHFY 368
Cdd:cd07781 313 fAWFVRLF---VPPAEERGDSIYALLSEEAAKL----PPGESGLVALDWFNGNRTPLVdPRLRGAIVGLTLG-TTPAHIY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 369 RAAMEGATYSLRNGFDAFVAAGLQFDTILLTGGGS-KSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWACDRDDGG 447
Cdd:cd07781 385 RALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADI 464
|
490 500 510
....*....|....*....|....*....|....*....
gi 1198216907 448 ADALSDVVlehlQIDHTLsaRPDPQRVVQYQQHYQNFLK 486
Cdd:cd07781 465 EEAADAMV----RVDRVY--EPDPENHAVYEELYALYKE 497
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-248 |
2.57e-59 |
|
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: 195.63 E-value: 2.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDpQERDVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFAQLdGEQRA----QVRGISVSGQ 78
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKT-LSQLGislkQIKGIGISNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 79 QHGFVPVAADGSVTAPVKLWCDTSTALECgQIMDAVGGAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPH 158
Cdd:pfam00370 79 GHGTVLLDKNDKPLYNAILWKDRRTAEIV-ENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 159 DYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVY-ALSDAAAEALNLPAGVLVTT 237
Cdd:pfam00370 158 DYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDH---LPPLVESSEIYgELNPELAAMWGLDEGVPVVG 234
|
250
....*....|.
gi 1198216907 238 GGGDNMMAAIG 248
Cdd:pfam00370 235 GGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
3-480 |
4.47e-59 |
|
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: 203.17 E-value: 4.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDpQERDVVATIAAPIE------------LISRDDGTREQQAQWWIDGIVHCFAQL--DGEQRA 68
Cdd:cd07776 1 LYLGLDLSTQSLKAVVID-SDLKVVAEESVNFDsdlpeygtkggvHRDGDGGEVTSPVLMWVEALDLLLEKLkaAGFDFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 69 QVRGISVSGQQHGFVPVAADGSV----------------------TAPVklWCDTSTALECGQIMDAVGGAAGSVAIAGN 126
Cdd:cd07776 80 RVKAISGSGQQHGSVYWSKGAESalanldpskslaeqlegafsvpDSPI--WMDSSTTKQCRELEKAVGGPEALAKLTGS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 127 PIMAGYTASKLPWTRKHRPEAYAAMTTVMLphdyVNFWLT----GeRFAEV--GDASGTGWLDVRTRQWSERMLGAVDAQ 200
Cdd:cd07776 158 RAYERFTGPQIAKIAQTDPEAYENTERISL----VSSFLAslllG-RYAPIdeSDGSGMNLMDIRSRKWSPELLDAATAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 201 rDLRDALPPLVETGTVY-ALSDAAAEALNLPAGVLVTTGGGDNMMAAIGTGnVVPGRLTMSLGTSGTLFAYADHPVVDDD 279
Cdd:cd07776 233 -DLKEKLGELVPSSTVAgGISSYFVERYGFSPDCLVVAFTGDNPASLAGLG-LEPGDVAVSLGTSDTVFLVLDEPKPGPE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 280 ARwaAFCS--SSGGWLPLICTMNCTVATEAVM-RMFSITREQTEALIASTTPGADGLVLLPFFNGERTPDLPTA--RGCL 354
Cdd:cd07776 311 GH--VFANpvDPGSYMAMLCYKNGSLARERVRdRYAGGSWEKFNELLESTPPGNNGNLGLYFDEPEITPPVPGGgrRFFG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 355 FGMDLHNTSPAHFYRAAMEGATYSLRN-----GFDafvaagLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGA 429
Cdd:cd07776 389 DDGVDAFFDPAVEVRAVVESQFLSMRLhaerlGSD------IPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSA 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1198216907 430 AFGAGLQALWACDRDDGGADALSDVVleHLQIDHTLSARPDPQRVVQYQQH 480
Cdd:cd07776 463 ALGAALRAAHGLLCAGSGDFSPEFVV--FSAEEPKLVAEPDPEAAEVYDKL 511
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-437 |
1.34e-54 |
|
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: 189.36 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERdVVATIAAPIELI--SRDDGTREQQAQWWIDGIVHCFAQL---DGEQRAQVRGISVSG 77
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGK-IVAIAYREWEYYtdDDYPDAKEFDPEELWEKICEAIREAlkkAGISPEDISAVSSTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 78 QQHGFVPVAADGSvtapvklwcdtstALECGQIMDAVGGAAG----------SVAIAGNPIMAGYTASKLPWTRKHRPEA 147
Cdd:cd07798 80 QREGIVFLDKDGR-------------ELYAGPNIDARGVEEAaeiddefgeeIYTTTGHWPTELFPAARLLWFKENRPEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 148 YAAMTTVMLPHDYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVYA-LSDAAAEA 226
Cdd:cd07798 147 FERIATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEI---LPEIVPSGTVLGtVSEEAARE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 227 LNLPAGVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDAR-WAAFCSSSGGWL----PLICTMNC 301
Cdd:cd07798 224 LGLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRlWTGCHLVPGKWVlesnAGVTGLNY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 302 TVATEAVMRMFSITREQTEALIASTTPGADGlvLLPFFnGERTPDLPTARGCLFG------MDLHNTSPAHFYRAAMEGA 375
Cdd:cd07798 304 QWLKELLYGDPEDSYEVLEEEASEIPPGANG--VLAFL-GPQIFDARLSGLKNGGflfptpLSASELTRGDFARAILENI 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198216907 376 TYSLRNGFDAFVA-AGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQA 437
Cdd:cd07798 381 AFAIRANLEQLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICA 443
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-437 |
1.78e-43 |
|
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: 159.31 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDPQERDVVA--TIAAPIELISRDDGTREQQAQWWIDGIVHCFAQLDGEQRAQVRGISVSGQQH 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILEsvSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYLSDVTGIGITGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 81 GFVPVAADGS-----VTapvklWCDTSTALECGQIMDAVGGAAGSvaIAGNPIMAGYTASKLPWTRKHRP--EAYAAMTT 153
Cdd:cd07777 81 GIVLWDEDGNpvsplIT-----WQDQRCSEEFLGGLSTYGEELLP--KSGMRLKPGYGLATLFWLLRNGPlpSKADRAGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 154 VMlphDYVNFWLTGER--FAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVyalsdAAAEALNLPA 231
Cdd:cd07777 154 IG---DYIVARLTGLPkpVMHPTNAASWGLFDLETGTWNKDLLEALGLPVIL---LPEIVPSGEI-----VGTLSSALPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 232 GVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDarWAAFCSSSGGWLPLICTMNCTVATEAVMRM 311
Cdd:cd07777 223 GIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELSGS--VEIRPFFDGRYLLVAASLPGGRALAVLVDF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 312 F-SITREQT---------EALI-ASTTPGADGLVLLPFFNGERTpdLPTARGCLFGMDLHNTSPAHFYRAAMEGATYSLR 380
Cdd:cd07777 301 LrEWLRELGgslsddeiwEKLDeLAESEESSDLSVDPTFFGERH--DPEGRGSITNIGESNFTLGNLFRALCRGIAENLH 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1198216907 381 NGFDAFVAAGLQFDTILLTGGGS-KSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQA 437
Cdd:cd07777 379 EMLPRLDLDLSGIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-486 |
3.88e-32 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 129.08 E-value: 3.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 1 MSLYIGLDVGTQSVKLVAYDPQERDVVATIAAPIElISRDDGTREQQAQW-------WIDGIVHC----FAQLdGEQRAQ 69
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAADGEELASAVHPYP-RWVIGLYLPPPPDQarqhpldYLEALEAAvreaLAQA-GVDPAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 70 VRGISVSGQQHGFVPVAADG---SVT--------APVKLWCD-TSTAlECGQIMDavggaagsVAIAGNPimaGYTA--- 134
Cdd:COG1069 79 VVGIGVDATGCTPVPVDADGtplALLpefaenphAMVILWKDhTAQE-EAERINE--------LAKARGE---DYLRyvg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 135 ---------SKLPWTRKHRPEAYAAMTTVMLPHDYVNFWLTGERFAEVGDA--------SGTGWLDvrtrqwsERMLGAV 197
Cdd:COG1069 147 giissewfwPKILHLLREDPEVYEAADSFVELCDWITWQLTGSLKRSRCTAghkalwhaHEGGYPS-------EEFFAAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 198 D-AQRDLRDALP-PLVETGT-VYALSDAAAEALNLPAGVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHP 274
Cdd:COG1069 220 DpLLDGLADRLGtEIYPLGEpAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGTSTCHMLVSPEE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 275 --------VVDD---DARW------AAFcsssG---GWLPLICTMNCTVATEAVMRMFSITREQTEALiASTTPGADGLV 334
Cdd:COG1069 300 rfvpgicgQVDGsivPGMWgyeagqSAV----GdifAWFVRLLVPPLEYEKEAEERGISLHPLLTEEA-AKLPPGESGLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 335 LLPFFNGERTPDL-PTARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFVAAGLQFDTILLTGGGS-KSAQWRQMV 412
Cdd:COG1069 375 ALDWFNGNRSPLAdQRLKGVILGLTLG-TDAEDIYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVMQIY 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 413 ADIFDLQVVVPIQPEGAAFGAGLQALWACdrddgGA--------DALSDVvlehlqIDHTLsaRPDPQRVVQYQQHYQNF 484
Cdd:COG1069 454 ADVTGRPIKVAASEQACALGAAMFAAVAA-----GAypdveeamAAMGSG------FDKVY--TPDPENVAVYDALYAEY 520
|
..
gi 1198216907 485 LK 486
Cdd:COG1069 521 LQ 522
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
136-484 |
6.42e-31 |
|
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: 125.14 E-value: 6.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 136 KLPWTRKHRPEAYAAMTTVMLPHDYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVdaqrDLR-DALPPLVETG 214
Cdd:cd07775 137 RLLWLKNNRPEIYRKAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMA----GLKaDILPPVVESG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 215 TVYA-LSDAAAEALNLPAGVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARWAAFCSS-SGGW 292
Cdd:cd07775 213 TVIGkVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHViPDMW 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 293 LplicTMNCTVATEAVMRMFSITREQTEALIA----------------STTPGADGLVLLpFFNGERTPDLPTARGCLFG 356
Cdd:cd07775 293 Q----AEGISFFPGLVMRWFRDAFCAEEKEIAerlgidaydlleemakDVPPGSYGIMPI-FSDVMNYKNWRHAAPSFLN 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 357 MDL--HNTSPAHFYRAAMEGATYSLRNGFDAFVAA-GLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGA 433
Cdd:cd07775 368 LDIdpEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGA 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1198216907 434 GLQALWACDRDDGGADALSDVVlehlQIDHTLsaRPDPQRVVQYQQHYQNF 484
Cdd:cd07775 448 AIAAGVGAGIYSSLEEAVESLV----KWEREY--LPNPENHEVYQDLYEKW 492
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-434 |
3.29e-29 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 119.75 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 1 MSLYIGLDVGTQSVKLVAYDPQERdVVATIAAPIEliSRDDGTREQQAQWWIDGIVHCFA----QLDGEQRAQ-VRGISV 75
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGK-IVARASTPNA--SDIAAENSDWHQWSLDAILQRFAdccrQINSELTEChIRGITV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 76 SGQQHGFVPVAADGSVTAPVKLW-CDTSTAlecgqIMDAVG---GAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAM 151
Cdd:PRK10331 78 TTFGVDGALVDKQGNLLYPIISWkCPRTAA-----VMENIEryiSAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 152 TTVMLPHDYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETG-TVYALSDAAAEALNLP 230
Cdd:PRK10331 153 HAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRL---FPRLVEAGeQIGTLQPSAAALLGLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 231 AGVLVTTGGGDNMMAAIGTGnVVPGRLTMSLGTSGTLFAYADHPvvddDARW--------AAFCSSSGGWLPLICTMNCT 302
Cdd:PRK10331 230 VGIPVISAGHDTQFALFGSG-AGQNQPVLSSGTWEILMVRSAQV----DTSLlsqyagstCELDSQSGLYNPGMQWLASG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 303 VaTEAVMRMFSITREQTEALIA---STTPGADGLVLLPFFngertpdLPTARGCLFGMDLHnTSPAHFYRAAMEGATYSL 379
Cdd:PRK10331 305 V-LEWVRKLFWTAETPYQTMIEearAIPPGADGVKMQCDL-------LACQNAGWQGVTLN-TTRGHFYRAALEGLTAQL 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1198216907 380 RNGFDAFVAAG-LQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPE----GAAF----GAG 434
Cdd:PRK10331 376 KRNLQVLEKIGhFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAEttvaGAAMfgwyGVG 439
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
257-441 |
1.63e-28 |
|
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: 111.65 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 257 LTMSLGTSGTLFAYADHPVVDDDARWAAFCSS--SGGWLpLICTMNCTVATEAVMRMFSITREQ----------TEALIA 324
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEmlPGYWG-LEGGQSAAGSLLAWLLQFHGLREElrdagnveslAELAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 325 STTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFVA-AGLQFDTILLTGGG 402
Cdd:pfam02782 80 AAVAPAGGLLFYPDFSGNRAPGAdPGARGSITGLSSP-TTLAHLYRAILESLALQLRQILEALTKqEGHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1198216907 403 SKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWAC 441
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-439 |
1.22e-26 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 112.76 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 1 MSLYIGLDVGTQSVKLVAYDpQERDVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFA----QLDGE-QRAQVRGISV 75
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFD-EKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNeaikKLREKgPSFKIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 76 SGQQHgfVPVAADGSVTAPVK---LWCDTSTALECGQIMDAVGGAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMT 152
Cdd:PTZ00294 80 TNQRE--TVVAWDKVTGKPLYnaiVWLDTRTYDIVNELTKKYGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 153 TVMLPHDYVNFW----LTGER--FAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDlrdALPPLVETGTVYalSDAAAEA 226
Cdd:PTZ00294 158 EGTLLFGTIDTWliwnLTGGKshVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKE---TLPEIKSSSENF--GTISGEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 227 LNLPAGVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVdddarwaafcSSSGGWLPLIC-----TMNC 301
Cdd:PTZ00294 233 VPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIV----------FSKHGLLTTVCyqlgpNGPT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 302 TVATE---AV-----------MRMFSITREQTEalIASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHnTSPAH 366
Cdd:PTZ00294 303 VYALEgsiAVagagvewlrdnMGLISHPSEIEK--LARSVKDTGGVVFVPAFSGLFAPYWrPDARGTIVGMTLK-TTRAH 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1198216907 367 FYRAAMEGATYSLRNGFDAFV-AAGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPE----GAAFGAGLQA-LW 439
Cdd:PTZ00294 380 IVRAALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAEttalGAALLAGLAVgVW 458
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
136-486 |
3.29e-26 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 111.64 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 136 KLPWTRKHRPEAYAAMTTVMLPHDYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGT 215
Cdd:PRK10939 140 RLLWLAHHRPDIYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADI---LPPVKETGT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 216 VY-ALSDAAAEALNLPAGVLVTTGGGDNMMAAIGTGNVVPGRlTMSLGtsGTLFAYA---DHPVVDDDARWAAFCSssgg 291
Cdd:PRK10939 217 VLgHVTAKAAAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQ-TAVLG--GTFWQQVvnlPAPVTDPNMNIRINPH---- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 292 wlpLICTMN----CTVATEAVMRMFSITREQTEALIAStTPGADGLVLLPffngERTPDLPT-ARGCL--------FGMD 358
Cdd:PRK10939 290 ---VIPGMVqaesISFFTGLTMRWFRDAFCAEEKLLAE-RLGIDAYSLLE----EMASRVPVgSHGIIpifsdvmrFKSW 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 359 LH------NTS-------PAHFYRAAMEGATY-SLRNGFDAFVAAGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPI 424
Cdd:PRK10939 362 YHaapsfiNLSidpekcnKATLFRALEENAAIvSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPV 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1198216907 425 QPEGAAFGAglqALWACdrddGGA---DALSDVVLEHLQIDHTLsaRPDPQRVVQYQQHYQNFLK 486
Cdd:PRK10939 442 VKEATALGC---AIAAG----VGAgiySSLAETGERLVRWERTF--EPNPENHELYQEAKEKWQA 497
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
2-446 |
7.28e-22 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 98.69 E-value: 7.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 2 SLYIGLDVGTQSVKLVAYDPQERdVVAT--IAAPIEL--------ISRD---DGTREQQAQWWIDGIVHCFAQLDGEQR- 67
Cdd:PLN02669 8 SLFLGFDSSTQSLKATVLDSNLR-IVASeiVHFDSDLphygtkdgVYRDpkvNGRIVSPTLMWVEALDLLLQKLAKEKFp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 68 -AQVRGISVSGQQHG--------------------FVPVAADGSVTAPVKLWCDTSTALECGQIMDAVGGAAGSVAIAGN 126
Cdd:PLN02669 87 fHKVVAISGSGQQHGsvywrkgasavlksldpsksLVAQLQDAFSTKDSPIWMDSSTTKQCREIEEAVGGAAELSKLTGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 127 PIMAGYTAsklPWTRK---HRPEAYAAMTTVMLPHDYVNFWLTGeRFAEV--GDASGTGWLDVRTRQWSERMLGAVdAQR 201
Cdd:PLN02669 167 RAYERFTG---PQIRKiyeTQPEVYHDTERISLVSSFMASLLVG-DYASIdeTDGAGMNLMDIEKRCWSKAALEAT-APG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 202 dLRDALPPLVETGTVYA-LSDAAAEALNLPAGVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPvvddda 280
Cdd:PLN02669 242 -LEEKLGKLAPAHAVAGkIHPYFVQRFGFSSNCLVVQWSGDNPNSLAGLTLSTPGDLAISLGTSDTVFGITREP------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 281 rwaaFCSSSGGWLPlictmNcTVATEAVMRMF-----SITREQTE------------ALIASTTPGADGLVLLPFFNGER 343
Cdd:PLN02669 315 ----QPSLEGHVFP-----N-PVDPESYMVMLcykngSLTREDIRnrcadgswdvfnKLLEQTPPLNGGKLGFYYKEHEI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 344 TPDLPTA--RGCLFGMDLHNTS-----------PAHFYRAAMEGATYSLRNGFDAFvaaGLQF--DTILLTGGGSKSAQW 408
Cdd:PLN02669 385 LPPLPVGfhRYILENFSGEALDglveeevgefdPPSEVRAIIEGQFLSMRAHAERF---GMPVppKRIIATGGASANQSI 461
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1198216907 409 RQMVADIFDLQVVVPIQPEGAAFGAGLQAL--WACDRDDG 446
Cdd:PLN02669 462 LKLIASIFGCDVYTVQRPDSASLGAALRAAhgWLCNEQGS 501
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
125-438 |
6.69e-21 |
|
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: 95.29 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 125 GNPIMAGYTASKLPWTRKHRPEAYA-AMTTVMLPhDYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDL 203
Cdd:cd07771 122 GIQFQPINTLYQLYALKKEGPELLErADKLLMLP-DLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 204 rdaLPPLVETGTVY-ALSDAAAEALNLPAGVLVTTGGGDNMMAAIGTGNVVPGRLTMSLGTSGTLFAYADHPVVDDDARW 282
Cdd:cd07771 201 ---FPPIVPPGTVLgTLKPEVAEELGLKGIPVIAVASHDTASAVAAVPAEDEDAAFISSGTWSLIGVELDEPVITEEAFE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 283 AAF---CSSSGGWLPLIctmNCT---VATEaVMRMFSITREQT--EALI--ASTTPGADGLVLL---PFFNGErtpDLPT 349
Cdd:cd07771 278 AGFtneGGADGTIRLLK---NITglwLLQE-CRREWEEEGKDYsyDELValAEEAPPFGAFIDPddpRFLNPG---DMPE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 350 A-RGCL--FGMDLHNTsPAHFYRAAMEGATYSLRNGFDAFVA-AGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVV-PI 424
Cdd:cd07771 351 AiRAYCreTGQPVPES-PGEIARCIYESLALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAgPV 429
|
330
....*....|....*
gi 1198216907 425 qpEGAAFG-AGLQAL 438
Cdd:cd07771 430 --EATAIGnLLVQLI 442
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-486 |
1.97e-18 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 87.98 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 1 MSLYIGLDVGTQSVKLVAYDPQERDVVATIAAPIELISRD---DGTRE---QQAQWWIDGIVHCFAQL---DGEQRAQVR 71
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDCATGEELATAVVEYPHWVKGrylDLPPNqalQHPLDYIESLEAAIPAVlkeAGVDPAAVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 72 GISVSGQQHGFVPVAADGSVTA--------P---VKLWCDtSTALECGQIMDAVGGAAGSVAIA---GNPIMAGYTASKL 137
Cdd:PRK04123 82 GIGVDFTGSTPAPVDADGTPLAllpefaenPhamVKLWKD-HTAQEEAEEINRLAHERGEADLSryiGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 138 PWTRKHRPEAYAAMTTVMLPHDYVNFWLTGERFAEVGDAS--GTG----WLDVRTRQWSERMLGAVDAQ--RDLRDALPp 209
Cdd:PRK04123 161 LHVLREDPAVYEAAASWVEACDWVVALLTGTTDPQDIVRSrcAAGhkalWHESWGGLPSADFFDALDPLlaRGLRDKLF- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 210 lVETGT----VYALSDAAAEALNLPAGVLVTTGGGDNMMAAIGTGnVVPGRLTMSLGTSGTLFAYADHP--------VVD 277
Cdd:PRK04123 240 -TETWTagepAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAG-AEPGTLVKVMGTSTCDILLADKQravpgicgQVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 278 D---DARWA--AFCSSSG---GWLPLICtMNCTVATEAVMRMFSITREQTEALiASTTPGADGLVLLPFFNGERTPDL-P 348
Cdd:PRK04123 318 GsivPGLIGyeAGQSAVGdifAWFARLL-VPPEYKDEAEARGKQLLELLTEAA-AKQPPGEHGLVALDWFNGRRTPLAdQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 349 TARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFVAAGLQFDTILLTGG-GSKSAQWRQMVADIFDLQVVVPIQPE 427
Cdd:PRK04123 396 RLKGVITGLTLG-TDAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQ 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198216907 428 GAAFGAG-LQALWACDRDD--GGADALSDVVLEHLQidhtlsarPDPQRVVQYQQHYQNFLK 486
Cdd:PRK04123 475 CPALGAAiFAAVAAGAYPDipEAQQAMASPVEKTYQ--------PDPENVARYEQLYQEYKQ 528
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
3-486 |
4.21e-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: 87.21 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 3 LYIGLDVGTQSVKLVAYDpQERDVVATIAAPIELISRDDGTREQQ-AQWWiDGIVHCF------AQLDGEQraqVRGIS- 74
Cdd:cd07782 1 YYIGVDVGTGSARAGLFD-LDGRLLATASQPITTWNPKPDFYEQSsEDIW-QAVCEAVkevlegAGVDPEQ---VKGIGf 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 75 -------VSGQQHGFVPVAADGSVTAPVKLWCD---TSTALEC----GQIMDAVGGAAgsvaiagNPIMAgytASKLPWT 140
Cdd:cd07782 76 datcslvVLDAEGKPVSVSPSGDDERNVILWMDhraVEEAERInatgHEVLKYVGGKI-------SPEME---PPKLLWL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 141 RKHRPEAYAAMTTVM-LPhDYVNFWLTGERFA-----------EVGDASGTGWLDvrtRQWSERMLGAV---DAQRDLRD 205
Cdd:cd07782 146 KENLPETWAKAGHFFdLP-DFLTWKATGSLTRslcslvckwtyLAHEGSEGGWDD---DFFKEIGLEDLvedNFAKIGSV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 206 ALPPLVETGTvyALSDAAAEALNLPAGVLVTTG------GGDNMMAAIGTGNV-----VPGRLTMSLGTSGTLFAYADHP 274
Cdd:cd07782 222 VLPPGEPVGG--GLTAEAAKELGLPEGTPVGVSlidahaGGLGTLGADVGGLPceadpLTRRLALICGTSSCHMAVSPEP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 275 V----VdddarWAAFC--------------SSSGGWLPLICTMNCTVAT---EAVMRMFSIT----------REQTEALI 323
Cdd:cd07782 300 VfvpgV-----WGPYYsamlpglwlneggqSATGALLDHIIETHPAYPElkeEAKAAGKSIYeylnerleqlAEEKGLPL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 324 ASTTpgaDGLVLLPFFNGERTP--DlPTARGCLFGMDLHNT--SPAHFYRAAMEGATYSLRNGFDAFVAAGLQFDTILLT 399
Cdd:cd07782 375 AYLT---RDLHVLPDFHGNRSPlaD-PTLRGMISGLTLDTSldDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMC 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 400 GGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGLQALWACdrddGGADALSDVVLEHLQIDHTLsaRPDPQRVVQYQQ 479
Cdd:cd07782 451 GGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVAS----GDFPSLWDAMAAMSGPGKVV--EPNEELKKYHDR 524
|
....*..
gi 1198216907 480 HYQNFLK 486
Cdd:cd07782 525 KYEVFLK 531
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
4-439 |
5.57e-17 |
|
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: 83.28 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 4 YIG-LDVGTQSVKLVAYDPQERdVVATIAAPIELISRDDGTREQQA-QWW---IDGIVHCFAQLdGEQRAQVRGISVSGQ 78
Cdd:cd07769 1 YILaIDQGTTSTRAILFDEDGN-IVASAQKEHEQIYPQPGWVEHDPeEIWentLEVIREALAKA-GISASDIAAIGITNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 79 QHGFV--------PVAadgsvtaPVKLWCDTSTALECGQIMDAvGGAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAA 150
Cdd:cd07769 79 RETTVvwdkktgkPLY-------NAIVWQDRRTADICEELKAK-GLEERIREKTGLPLDPYFSATKIKWILDNVPGARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 151 MT-------TVmlphD-YVNFWLTGER--FAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVYALS 220
Cdd:cd07769 151 AErgellfgTI----DtWLIWKLTGGKvhVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSM---LPEVRPSSEVFGYT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 221 DAAAEALNLP-AGVLvttggGDNMMAAIGTGNVVPGrltMSLGTSGT----LFAYADHPVVdddarwaafcsSSGGWLPL 295
Cdd:cd07769 224 DPEGLGAGIPiAGIL-----GDQQAALFGQGCFEPG---MAKNTYGTgcflLMNTGEKPVP-----------SKNGLLTT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 296 IC---TMNCTVATE--------AV------MRMFSiTREQTEALiASTTPGADGLVLLPFFNGERTP--DlPTARGCLFG 356
Cdd:cd07769 285 IAwqiGGKVTYALEgsifiagaAIqwlrdnLGLIE-DAAETEEL-ARSVEDNGGVYFVPAFSGLGAPywD-PDARGAIVG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 357 MDlHNTSPAHFYRAAMEGATYSLRNGFDAFVA-AGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPE----GAAF 431
Cdd:cd07769 362 LT-RGTTKAHIVRAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAEttalGAAY 440
|
....*....
gi 1198216907 432 GAGLQA-LW 439
Cdd:cd07769 441 LAGLAVgFW 449
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-489 |
8.44e-17 |
|
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: 82.99 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 4 YI-GLDVGTQSVKLVAYDpQERDVVATIAAPIELISRDDGTREQQAQWWIDGIVH----CFAQLdGEQRAQVRGISVSGQ 78
Cdd:cd07793 1 YIlAVDVGTTNIRCHIFD-KKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKvikeALKNA-GLTPEDIAAIGISTQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 79 QHGFVPVAAD-GSVTAPVKLWCDTSTALEC--------GQIMDAVGGAAGSvaIAGNP---------IMAGYTASKLPWT 140
Cdd:cd07793 79 RNTFLTWDKKtGKPLHNFITWQDLRAAELCeswnrsllLKALRGGSKFLHF--LTRNKrflaasvlkFSTAHVSIRLLWI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 141 RKHRPEAYAAMttvmlPHDYVNF-----W----LTGER-FA-EVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPP 209
Cdd:cd07793 157 LQNNPELKEAA-----EKGELLFgtidtWllwkLTGGKvHAtDYSNASATGLFDPFTLEWSPILLSLFGIPSSI---LPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 210 LVETGTVYALSDAAAEALNLPagvlVTTGGGDNMMAAIGTGNVVPGRLTMSLGTsGTLF-------AYAdhpvvdddarw 282
Cdd:cd07793 229 VKDTSGDFGSTDPSIFGAEIP----ITAVVADQQAALFGECCFDKGDVKITMGT-GTFIdintgskPHA----------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 283 aafcsSSGGWLPLI---------CTMNCTVATEAV-------MRMFSiTREQTEAlIASTTPGADGLVLLPFFNGERTP- 345
Cdd:cd07793 293 -----SVKGLYPLVgwkiggeitYLAEGNASDTGTvidwaksIGLFD-DPSETED-IAESVEDTNGVYFVPAFSGLQAPy 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 346 -DlPTARGCLFGMDLhNTSPAHFYRAAMEGATYSLRNGFDAFVA-AGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVP 423
Cdd:cd07793 366 nD-PTACAGFIGLTP-STTKAHLVRAILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLIADLLGKPVERP 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198216907 424 IQPE----GAAFGAGLQA-LWAcDRDDggadalsdvvLEHL-QIDHTLSARPDPQRvvqYQQHYQNFLKHLR 489
Cdd:cd07793 444 KNTEmsalGAAFLAGLASgIWK-SKEE----------LKKLrKIEKIFEPKMDNEK---REELYKNWKKAVK 501
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
4-439 |
3.01e-16 |
|
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: 81.03 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 4 YIG-LDVGTQSVKLVAYDpQERDVVATIAAPIELISRDDGTREQQAQWWIDGIVHCFA------QLDGEQRAQVRGISVS 76
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFD-STGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEeaveklKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 77 GQQHgfVPVAADgSVT------APVklWCDTSTALECGQ-IMDAVGGAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYA 149
Cdd:cd07792 81 NQRE--TTVVWD-KSTgkplynAIV--WLDTRTSDTVEElSAKTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVPEVKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 150 AMT--TVMLphDYVNFW----LTGER-----FAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDLrdaLPPLVETGTVYA 218
Cdd:cd07792 156 AVDdgRLLF--GTVDSWliwnLTGGKnggvhVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSI---LPEIRSSSEVYG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 219 LSDAAAEAlNLP-AGVLvttggGDNMMAAIGTGNVVPGrltMSLGTSGT----LFAYADHPVVdddarwaafcSSSGgwl 293
Cdd:cd07792 231 KIASGPLA-GVPiSGCL-----GDQQAALVGQGCFKPG---EAKNTYGTgcflLYNTGEEPVF----------SKHG--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 294 pLICTM------NCT----------VATEAV------MRMFSiTREQTEALiASTTPGADGLVLLPFFNGERTP--DlPT 349
Cdd:cd07792 289 -LLTTVayklgpDAPpvyalegsiaIAGAAVqwlrdnLGIIS-SASEVETL-AASVPDTGGVYFVPAFSGLFAPywR-PD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 350 ARGCLFGMDLHnTSPAHFYRAAMEGATYSLRNGFDAFVA-AGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPE- 427
Cdd:cd07792 365 ARGTIVGLTQF-TTKAHIARAALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVEt 443
|
490
....*....|....*.
gi 1198216907 428 ---GAAFGAGLQA-LW 439
Cdd:cd07792 444 talGAAIAAGLAVgVW 459
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
98-439 |
3.17e-14 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 74.74 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 98 WCDTSTALECGQIM-DAVGGAAGSVAIAGNPIMAGYTASKLPWTRKHRPEAYAAMTTVMLPHDYVNFWL---------TG 167
Cdd:PLN02295 103 WMDSRTSSICRRLEkELSGGRKHFVETCGLPISTYFSATKLLWLLENVDAVKEAVKSGDALFGTIDSWLiwnltggasGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 168 ERFAEVGDASGTGWLDVRTRQWSERMLGAVDAQRDlrdALPPLVETGTVYALSDAAAEALNLP-AGVLvttggGDNMMAA 246
Cdd:PLN02295 183 VHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAE---ILPKIVSNSEVIGTIAKGWPLAGVPiAGCL-----GDQHAAM 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 247 IGTGnVVPGRLTMSLGTS----------------GTLFAYADHPVVDDDARWA-----AFCSSSGGWL----PLICTmnc 301
Cdd:PLN02295 255 LGQR-CRPGEAKSTYGTGcfillntgeevvpskhGLLTTVAYKLGPDAPTNYAlegsvAIAGAAVQWLrdnlGIIKS--- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 302 tvATEAvmrmfsitreqtEALiASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGMDLHnTSPAHFYRAAMEGATYSLR 380
Cdd:PLN02295 331 --ASEI------------EAL-AATVDDTGGVYFVPAFSGLFAPRWrDDARGVCVGITRF-TNKAHIARAVLESMCFQVK 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 381 NGFDAFVA-AGLQFDTILLT-----GGGSKSAQWRQMVADIFDLQVVVPIQPE----GAAFGAGLQA-LW 439
Cdd:PLN02295 395 DVLDAMRKdAGEEKSHKGLFllrvdGGATANNLLMQIQADLLGSPVVRPADIEttalGAAYAAGLAVgLW 464
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-484 |
1.86e-13 |
|
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: 72.66 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 4 YIGLDVGTQSVKLVAYDPQERDVVATIAAPI-ELISRDDGTREQQAQWWIDGIVHCFAQLDGEQRA---QVRGISVSGQQ 79
Cdd:cd07768 2 GIGVDVGTSSARAGVYDLYAGLEMAQEPVPYyQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVdayEVKGCGVDATC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 80 hGFVPVAADG-SVTAP--------VKLWCDTSTALECG--------QIMDAVGGAagsvaiagnpIMAGYTASKLPWTRK 142
Cdd:cd07768 82 -SLAIFDREGtPLMALipypnednVIFWMDHSAVNEAQwinmqcpqQLLDYLGGK----------ISPEMGVPKLKYFLD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 143 HRPEAYAAMTTVMLPHDYVNFWLTGERFAEVGDASGTGWLDVRTRQWSERMLGAVD-AQRDLRDA--LPPLVETGT--VY 217
Cdd:cd07768 151 EYSHLRDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDpRLEHLTTTknLPSNVPIGTtsGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 218 ALSDAAAEaLNLPAGVLVTTGGGDNMMAAIGTGNV-VPGRLTMSLGTSGTLFAYA-------------DHPVVDDDARWA 283
Cdd:cd07768 231 ALPEMAEK-MGLHPGTAVVVSCIDAHASWFAVASPhLETSLFMIAGTSSCHMYGTtisdripgvwgpfDTIIDPDYSVYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 284 AFCSSSGGWLPLI-----CTMNCTVATEAVMRMFSITrEQTEALIASTTPGADGLVLLPFFNGERTPDL-PTARGCLFGM 357
Cdd:cd07768 310 AGQSATGKLIEHLfeshpCARKFDEALKKGADIYQVL-EQTIRQIEKNNGLSIHILTLDMFFGNRSEFAdPRLKGSFIGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 358 DLHNT--SPAHFYRAAMEGATYSLRNGFDAFVAAGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGAAFGAGL 435
Cdd:cd07768 389 SLDTSmlNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAV 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1198216907 436 QALWACDRDDgGADALSDVVLEHLQIDHTLsaRPDPQRVVQ-YQQHYQNF 484
Cdd:cd07768 469 LAKVAAGKKQ-LADSITEADISNDRKSETF--EPLAYRLGAdYILLYKLL 515
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
134-445 |
1.04e-10 |
|
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: 63.66 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 134 ASKLPWTRKHRPEAYA-------AMTTVmlphdyvNFWLT-----GERFA-EVGDASGTGWLDVRTRQWSERMLGAVDAQ 200
Cdd:cd07786 134 ATKIRWILDNVPGAREraergelAFGTI-------DSWLIwkltgGKVHAtDVTNASRTMLFNIHTLEWDDELLELFGIP 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 201 RDLrdaLPPLVETGTVYALSDAAaealNLPAGVLVTTGGGDNMMAAIGTGNVVPGrltMSLGTSGT----LFAYADHPVV 276
Cdd:cd07786 207 ASM---LPEVKPSSEVFGYTDPD----LLGAEIPIAGIAGDQQAALFGQACFEPG---MAKNTYGTgcfmLMNTGEKPVR 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 277 dddarwaafcSSSGgwlpLICTMNCT--------------VATEAV------MRMFSITREqTEALiASTTPGADGLVLL 336
Cdd:cd07786 277 ----------SKNG----LLTTIAWQlggkvtyalegsifIAGAAVqwlrdgLGLIESAAE-TEAL-ARSVPDNGGVYFV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 337 PFFNGERTP--DlPTARGCLFGMDlHNTSPAHFYRAAMEGATYSLRNGFDAFVA-AGLQFDTILLTGGGSKSAQWRQMVA 413
Cdd:cd07786 341 PAFTGLGAPywD-PDARGAIFGLT-RGTTRAHIARAALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQA 418
|
330 340 350
....*....|....*....|....*....|....*..
gi 1198216907 414 DIFDLQVVVPIQPE----GAAFGAGLQA-LWAcDRDD 445
Cdd:cd07786 419 DILGVPVERPKVTEttalGAAYLAGLAVgLWK-SLDE 454
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
309-435 |
5.17e-09 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 58.30 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 309 MRMFSiTREQTEALiASTTPGADGLVLLPFFNGERTP--DlPTARGCLFGMDLHNTSpAHFYRAAMEGATYSLRNGFDAF 386
Cdd:PRK00047 321 LKIIS-DASDSEAL-ARKVEDNDGVYVVPAFTGLGAPywD-SDARGAIFGLTRGTTK-EHIIRATLESIAYQTRDVLDAM 396
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1198216907 387 VA-AGLQFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPE----GAAFGAGL 435
Cdd:PRK00047 397 QAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAEttalGAAYLAGL 450
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-241 |
1.83e-08 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. 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: 466792 [Multi-domain] Cd Length: 424 Bit Score: 56.50 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 7 LDVGTQSVKLVAYDPQeRDVVATIAAPIELIsRDDGTR----EQQAQWWIDGIVHCfaqldgEQRAQVRGISVSGqqHG- 81
Cdd:cd07772 5 FDIGKTNKKLLLFDEN-GEVLAERSTPNPEI-EEDGYPcedvEAIWEWLLDSLAEL------AKRHRIDAINFTT--HGa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 82 -FVPVAADGSVTAPVK--LWcDTStalecGQIMDAVGGAAGSVAIAGNPIM-AGYTASK-LPWTRKHRPEAYAAMTTVM- 155
Cdd:cd07772 75 tFALLDENGELALPVYdyEK-PIP-----DEINEAYYAERGPFEETGSPPLpGGLNLGKqLYWLKREKPELFARAKTILp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 156 LPhDYVNFWLTGERFAEVgdaSGTG-----WlDVRTRQWSermlgAVDAQRDLRDALPPLVETG-TVYALSDAAAEALNL 229
Cdd:cd07772 149 LP-QYWAWRLTGKAASEI---TSLGchtdlW-DFEKNEYS-----SLVKKEGWDKLFPPLRKAWeVLGPLRPDLARRTGL 218
|
250
....*....|..
gi 1198216907 230 PAGVLVTTGGGD 241
Cdd:cd07772 219 PKDIPVGCGIHD 230
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
4-454 |
6.02e-06 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 48.94 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 4 YIGLDVGTQSVKLVAYDpQERDVVATIAAPIELI--SRDDGTREQQAQWWIDGIVHCFAQLDGEQRA-QVRGISVS---- 76
Cdd:cd07778 2 GIGIDVGSTSVRIGIFD-YHGTLLATSERPISYKqdPKDLWFVTQSSTEIWKAIKTALKELIEELSDyIVSGIGVSatcs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 77 --------GQQHgFVPVAADGSVTAP---VKLWCDTSTALECGQI-----MDAVGGAAGSVaiagNPIMAgytASKLPWT 140
Cdd:cd07778 81 mvvmqrdsDTSY-LVPYNVIHEKSNPdqdIIFWMDHRASEETQWLnnilpDDILDYLGGGF----IPEMA---IPKLKYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 141 RKHRPEAYAAMTTVMLPHDYVNFWLTGER--------FAEVG-----DASGTGWlDVRTRQWSERMLGAVDAQRDLRDAL 207
Cdd:cd07778 153 IDLIKEDTFKKLEVFDLHDWISYMLATNLghsnivpvNAPPSigigiDGSLKGW-SKDFYSKLKISTKVCNVGNTFKEAP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 208 P-PLVETGTVYALSDAAAEaLNLPAGVLVTTGGGDNMMAAIGT---GNVVPGRLTMSLGTSgTLFAYA-----DHP---- 274
Cdd:cd07778 232 PlPYAGIPIGKVNVILASY-LGIDKSTVVGHGCIDCYAGWFSTfaaAKTLDTTLFMVAGTS-TCFLYAtsssqVGPipgi 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 275 ------VVDDDARWAAFCSSSGGWLP-LICTMNCTV-ATEAVMRMFSITREQTEALIASTTPGADGLVLLPFFNGE---- 342
Cdd:cd07778 310 wgpfdqLLKNYSVYEGGQSATGKLIEkLFNSHPAIIeLLKSDANFFETVEEKIDKYERLLGQSIHYLTRHMFFYGDylgn 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198216907 343 RTPDLPTARGCLF---GMDLHNTSPAHFYRAAMEGATYSLRNGFDAFVAAGLQFDTILLTGGGSKSAQWRQMVADIfdLQ 419
Cdd:cd07778 390 RTPYNDPNMSGSFigeSTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTV--LS 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1198216907 420 VVVPIQP-----EGAAFGAGLQALWACDRDDGGADALSDV 454
Cdd:cd07778 468 KIHIIVPlsdskYAVVKGAALLGKAAFLHNQSIEERLISL 507
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
384-437 |
3.57e-04 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 42.89 E-value: 3.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1198216907 384 DAFVAAGL---QFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGA-AFGAGLQA 437
Cdd:COG0443 289 QALADAGLspsDIDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAvALGAAIQA 346
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
392-439 |
1.29e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466879 [Multi-domain] Cd Length: 351 Bit Score: 41.02 E-value: 1.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1198216907 392 QFDTILLTGGGSKSAQWRQMVADIFDLQVVVPIQPEGA-AFGAGLQALW 439
Cdd:cd24029 301 DIDRVLLVGGSSRIPLVREMLEEYFGREPISSVDPDEAvAKGAAIYAAS 349
|
|
| |
