|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
2-445 |
7.03e-177 |
|
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: 504.01 E-value: 7.03e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVETGKSLGVVQEPEEEMGMfaqKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAETGRVVASGSAPHENILI---DPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSPANFTASKLKWVQENEPDIYSQIHKFMLPG 161
Cdd:cd07809 78 GQMHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 162 DYIAYKFSNKintTISGLSE--GIFWDFKNDSVADFLLEYYG----INKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTP 235
Cdd:cd07809 158 DYLNWKLTGE---KVTGLGDasGTFPIDPRTRDYDAELLAAIdpsrDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 236 IFYRAGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHVNYqkgaaariGKLLCINGAGIQYRWL 315
Cdd:cd07809 235 VAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDSTG--------GMLPLINTTNCLTAWT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 316 --LNNLAVSSYEEMNNLASEIPVGSDGVCLIPFGNGaERMLNNKEIGTRIVNMNLNNHHKGHMCRAALEGIAFSFVYGME 393
Cdd:cd07809 307 elFRELLGVSYEELDELAAQAPPGAGGLLLLPFLNG-ERTPNLPHGRASLVGLTLSNFTRANLARAALEGATFGLRYGLD 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1199785844 394 ILKSDGIKPSVIRA-GndNLFRSEIFANTVATLIEQEIEIYNT--TGAIGAARAA 445
Cdd:cd07809 386 ILRELGVEIDEIRLiG--GGSKSPVWRQILADVFGVPVVVPETgeGGALGAALQA 438
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-486 |
6.28e-157 |
|
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: 455.06 E-value: 6.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPeeeMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFD-ADGEVVASASAE---YPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSP-ANFTASKLKWVQENEPDIYSQIHKFMLP 160
Cdd:COG1070 78 GQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLhPGFTAPKLLWLKENEPEIFARIAKVLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 161 GDYIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFYRA 240
Cdd:COG1070 158 KDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 241 GDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHVnyqkgAAARIGKLLCINGAGIQYRWLLNNLA 320
Cdd:COG1070 238 GDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHA-----VPGRWLPMGATNNGGSALRWFRDLFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 321 ---VSSYEEMNNLASEIPVGSDGVCLIPFGNGAERMLNNKEIGTRIVNMNLnNHHKGHMCRAALEGIAFSFVYGMEILKS 397
Cdd:COG1070 313 dgeLDDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTL-SHTRAHLARAVLEGVAFALRDGLEALEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 398 DGIKPSVIRAGnDNLFRSEIFANTVATLIEQEIEIYNT--TGAIGAARAANLHKGDFETFGKVIMDNDHV-MTFMPFKDK 474
Cdd:COG1070 392 AGVKIDRIRAT-GGGARSPLWRQILADVLGRPVEVPEAeeGGALGAALLAAVGLGLYDDLEEAAAAMVRVgETIEPDPEN 470
|
490
....*....|...
gi 1199785844 475 KP-YLEAYNNWKN 486
Cdd:COG1070 471 VAaYDELYERYRE 483
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
2-486 |
2.00e-111 |
|
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: 338.36 E-value: 2.00e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEpeeEMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVD-EDGRVLASASA---EYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKcASHLLNSPAN-FTASKLKWVQENEPDIYSQIHKFMLP 160
Cdd:cd07808 77 GQMHGLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEI-LIITGNPPLPgFTLPKLLWLKENEPEIFARIRKILLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 161 GDYIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFYRA 240
Cdd:cd07808 156 KDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 241 GDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHV----NYQKGAaarigkllcINGAGIQYRWLL 316
Cdd:cd07808 236 GDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAvpgkWYAMGV---------TLSAGLSLRWLR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 317 NNLA--VSSYEEMNNLASEIPVGSDGVCLIPFGNGaERMLNNKE------IGTRIvnmnlnNHHKGHMCRAALEGIAFSF 388
Cdd:cd07808 307 DLFGpdRESFDELDAEAAKVPPGSEGLLFLPYLSG-ERTPYWDPnargsfFGLSL------SHTRAHLARAVLEGVAFSL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 389 VYGMEILKSDGIKPSVIRA---GNdnlfRSEIFANTVATLIEQEIEIYNTT--GAIGAARAANLHKGDFETFGKVIMDND 463
Cdd:cd07808 380 RDSLEVLKELGIKVKEIRLiggGA----KSPLWRQILADVLGVPVVVPAEEegSAYGAALLAAVGAGVFDDLEEAAAACI 455
|
490 500
....*....|....*....|....*
gi 1199785844 464 HV-MTFMPFKDKKP-YLEAYNNWKN 486
Cdd:cd07808 456 KIeKTIEPDPERHEaYDELYARYRE 480
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
4-445 |
2.02e-91 |
|
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: 286.90 E-value: 2.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 4 LGLDIGSSSIKAALVEvETGKSLGVVQEPeeeMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGISYQ 83
Cdd:TIGR01312 1 LGIDLGTSGVKALLVD-EQGEVIASGSAP---HTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 84 MHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSP-ANFTASKLKWVQENEPDIYSQIHKFMLPGD 162
Cdd:TIGR01312 77 MHGLVLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLAlPGFTAPKLLWVRKHEPEVFARIAKVMLPKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 163 YIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFYRAGD 242
Cdd:TIGR01312 157 YLRYRLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 243 QPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHvnyqkgaaARIGK---LLCINGAGIQYRWLLNNL 319
Cdd:TIGR01312 237 NAAGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCH--------ALPGGwlpMGVTLSATSSLEWFRELF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 320 AVSSYEEMNNLASEIPVGSDGVCLIPFGNGaERMLNNKEIGtRIVNMNLN-NHHKGHMCRAALEGIAFSFVYGMEILK-S 397
Cdd:TIGR01312 309 GKEDVEALNELAEQSPPGAEGVTFLPYLNG-ERTPHLDPQA-RGSFIGLThNTTRADLTRAVLEGVTFALRDSLDILReA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1199785844 398 DGIKPSVIRA---GNdnlfRSEIFANTVATLIEQEIEIYNTT--GAIGAARAA 445
Cdd:TIGR01312 387 GGIPIQSIRLiggGA----KSPAWRQMLADIFGTPVDVPEGEegPALGAAILA 435
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
2-445 |
2.11e-89 |
|
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: 281.72 E-value: 2.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVEtGKSLGVVQEPEEemgMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLD-GELVASAFAPYP---TYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSP--ANFTASKLKWVQENEPDIYSQIHKFML 159
Cdd:cd07805 77 GQMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPpsGKDPLAKILWLKENEPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 160 PGDYIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFYR 239
Cdd:cd07805 157 AKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 240 AGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHVNyqKGAAARIGKLLCingAGIQYRWLLNNL 319
Cdd:cd07805 237 GGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASAD--PGRYLLAAEQET---AGGALEWARDNL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 320 A------VSSYEEMNNLASEIPVGSDGVCLIPFGNGaERM-LNNKEI-GTrIVNMNLnNHHKGHMCRAALEGIAFSFVYG 391
Cdd:cd07805 312 GgdedlgADDYELLDELAAEAPPGSNGLLFLPWLNG-ERSpVEDPNArGA-FIGLSL-EHTRADLARAVLEGVAFNLRWL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 392 MEILKSDGIKPSVIRA---GndnlFRSEIFANTVATLIEQEIEIYNT---TGAIGAARAA 445
Cdd:cd07805 389 LEALEKLTRKIDELRLvggG----ARSDLWCQILADVLGRPVEVPENpqeAGALGAALLA 444
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
2-442 |
4.85e-89 |
|
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: 279.80 E-value: 4.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKslgVVQEPEEEMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVD-EDGK---VLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 yQMHG-LVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKcashLLNSPAN-----FTASKLKWVQENEPDIYSQIH 155
Cdd:cd07804 77 -GLVPaLVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDR----IFEITGNpldsqSVGPKLLWIKRNEPEVFKKTR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 156 KFMLPGDYIAYKFSNKINT-TISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGT 234
Cdd:cd07804 152 KFLGAYDYIVYKLTGEYVIdYSSAGNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 235 PIFYRAGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLsaKESSRVNNFAHVNYQK----GAAARIGKLLcingagi 310
Cdd:cd07804 232 PVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKL--PTDPRLWLDYHDIPGTyvlnGGMATSGSLL------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 311 qyRWLLNNLA-----------VSSYEEMNNLASEIPVGSDGVCLIPFGNGAERMLNNKEI-GTrIVNMNLNnHHKGHMCR 378
Cdd:cd07804 303 --RWFRDEFAgeeveaeksggDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDArGV-IFGLTLS-HTRAHLYR 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199785844 379 AALEGIAFSFVYGMEILKSDGIKPSVIRAgNDNLFRSEIFANTVATLIEQEIEIY-NTTGA-IGAA 442
Cdd:cd07804 379 ALLEGVAYGLRHHLEVIREAGLPIKRLVA-VGGGAKSPLWRQIVADVTGVPQEYVkDTVGAsLGDA 443
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
2-445 |
3.34e-82 |
|
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: 260.19 E-value: 3.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPEEemgMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd00366 1 YLLGIDIGTTSVKAALFD-EDGNLVASASREYP---LIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRavetgnkafneigeekcashllnspanftasklkwvqenepdiysqiHKFMLPG 161
Cdd:cd00366 77 GQMPGVVLVDADGNPLRPAIIWLDRR-----------------------------------------------AKFLQPN 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 162 DYIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFYRAG 241
Cdd:cd00366 110 DYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 242 DQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAkESSRVNNFAHVnyqkgaaaRIGKLL---CINGAGIQYRWLLNN 318
Cdd:cd00366 190 DTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVP-PDPRLLNRCHV--------VPGLWLlegAINTGGASLRWFRDE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 319 LA-----VSSYEEMNNLASEIPVGSDGVCLIPFGNGaERM-LNNKEIGTRIVNMNLNnHHKGHMCRAALEGIAFSFVYGM 392
Cdd:cd00366 261 FGeeedsDAEYEGLDELAAEVPPGSDGLIFLPYLSG-ERSpIWDPAARGVFFGLTLS-HTRAHLIRAVLEGVAYALRDNL 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199785844 393 EILKSDGIKPSVIRAG----NDNLFRsEIFAN----TVATLIEQEieiyntTGAIGAARAA 445
Cdd:cd00366 339 EILEELGVKIKEIRVTgggaKSRLWN-QIKADvlgvPVVVPEVAE------GAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
2-445 |
3.15e-73 |
|
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: 238.22 E-value: 3.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPeeeMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFD-LDGREIAVASRP---TPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSP-ANFTASKLKWVQENEPDIYSQIHKFMLP 160
Cdd:cd07802 77 GHGNGLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLwPGQPVALLRWLKENEPERYDRIRTVLFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 161 GDYIAYKFSNKINTTISGLSEGiFWDFKNDSVADFLLEYYGIN--KDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFY 238
Cdd:cd07802 157 KDWIRYRLTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 239 RAGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVnNFAHVN---YQKGAAARigkllciNGAGiQYRWL 315
Cdd:cd07802 236 GAFDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGS-NSLHADpglYLIVEASP-------TSAS-NLDWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 316 LNNLA-------VSSYEEMNNLASEIPVGSDGVCLIPFGNGAermlnNKEIGTRIVNMNLNNHH-KGHMCRAALEGIAFS 387
Cdd:cd07802 307 LDTLLgeekeagGSDYDELDELIAAVPPGSSGVIFLPYLYGS-----GANPNARGGFFGLTAWHtRAHLLRAVYEGIAFS 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199785844 388 FVYGMEILKSDGiKPSVIR-AGndNLFRSEIFANTVATLIEQEIEIYNT--TGAIGAARAA 445
Cdd:cd07802 382 HRDHLERLLVAR-KPETIRlTG--GGARSPVWAQIFADVLGLPVEVPDGeeLGALGAAICA 439
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
2-442 |
4.91e-71 |
|
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: 233.60 E-value: 4.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVeVETGKslgVVQEPEEEMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISrtQIKGIGIS 81
Cdd:cd07770 1 LILGIDIGTTSTKAVLF-DEDGR---VVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGnKAFNEIGEEK-------CASHllnspANFTASKLKWVQENEPDIYSQI 154
Cdd:cd07770 75 SAMHSLLGVDEDGEPLTPVITWADTRAAEEA-ERLRKEGDGSelyrrtgCPIH-----PMYPLAKLLWLKEERPELFAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 155 HKFMLPGDYIAYKFSNKINTTISGLS-EGIF------WDfkndsvaDFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEE 227
Cdd:cd07770 149 AKFVSIKEYLLYRLTGELVTDYSTASgTGLLnihtldWD-------EEALELLGIDEEQLPELVDPTEVLPGLKPEFAER 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 228 CGLAAGTPIFYRAGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDslSAKESSRVNNFAHVNYQK----GAAarigkll 303
Cdd:cd07770 222 LGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSD--RPVLDPPGRLWCYRLDENrwlvGGA------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 304 cINGAGIQYRWLLNNLA--VSSYEEMNNLASEIPVGSDGVCLIPFGNGaER--MLNNKEIGTrIVNMNLnNHHKGHMCRA 379
Cdd:cd07770 293 -INNGGNVLDWLRDTLLlsGDDYEELDKLAEAVPPGSHGLIFLPYLAG-ERapGWNPDARGA-FFGLTL-NHTRADILRA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199785844 380 ALEGIAFSFVYGMEILKSDGIKPSVIRAGNdNLFRSEIFANTVATLIEQEIEIYNT--TGAIGAA 442
Cdd:cd07770 369 VLEGVAFNLKSIYEALEELAGPVKEIRASG-GFLRSPLWLQILADVLGRPVLVPEEeeASALGAA 432
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
2-455 |
9.27e-71 |
|
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: 231.64 E-value: 9.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPEEemgMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd07779 1 YILGIDVGTTSTRAIIFD-LDGNIVASGYREYP---PYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAvetgnkafneigeekcashllnspanftasklkwvqenepdiysqiHKFMLPG 161
Cdd:cd07779 77 SQRSTFVPVDEDGRPLRPAISWQDKRT----------------------------------------------AKFLTVQ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 162 DYIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFYRAG 241
Cdd:cd07779 111 DYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 242 DQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHVNYqkgaaariGKLLC---INGAGIQYRWLLNN 318
Cdd:cd07779 191 DQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVP--------GKWVLegsINTGGSAVRWFRDE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 319 LA----------VSSYEEMNNLASEIPVGSDGVCLIPFGNGAERMLNNKEIGTRIVNMNLnNHHKGHMCRAALEGIAFSF 388
Cdd:cd07779 263 FGqdevaekelgVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTL-SHTRAHLARAILEGIAFEL 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199785844 389 VYGMEILKSDGIKPSVIRA--GndnLFRSEIFANTVATLIEQEIEIYNT--TGAIGAARAANLHKGDFETF 455
Cdd:cd07779 342 RDNLEAMEKAGVPIEEIRVsgG---GSKSDLWNQIIADVFGRPVERPETseATALGAAILAAVGAGIYPDF 409
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
2-445 |
3.11e-70 |
|
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: 230.55 E-value: 3.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPeeeMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNisRTQIKGIGIS 81
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFD-EDGRILASASRE---TPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCA--SHLLNSPaNFTASKLKWVQENEPDIYSQIHKFML 159
Cdd:cd07773 75 SQGESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYriTGLPPSP-MYSLAKLLWLREHEPEIFAKAAKWLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 160 PGDYIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFyr 239
Cdd:cd07773 154 VADYIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVV-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 240 AG--DQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHvnyqkGAAARIGKLLCING--AGIQYRWL 315
Cdd:cd07773 232 VGghDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSY-----GHHVPGGYYYLAGSlpGGALLEWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 316 LNNLAV--SSYEEMNNLASEIPVGSDGVCLIPFGNGAERMLNNKEIGTRIVNMNLnNHHKGHMCRAALEGIAFSFVYGME 393
Cdd:cd07773 307 RDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTL-GTTRADLLRAILEGLAFELRLNLE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1199785844 394 ILKSDGIKPSVIRA--GndnLFRSEIFANTVATLIEQEIEIYNT--TGAIGAARAA 445
Cdd:cd07773 386 ALEKAGIPIDEIRAvgG---GARSPLWLQLKADILGRPIEVPEVpeATALGAALLA 438
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
2-446 |
1.25e-62 |
|
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: 210.54 E-value: 1.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVEtGKSLGVVQEP----EEEMGMFAQkngwaEQKPNDWWLHICNAITKLKKEYNISRTQIKG 77
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSE-GKIVAIAYREweyyTDDDYPDAK-----EFDPEELWEKICEAIREALKKAGISPEDISA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 78 IGISYQMHGLVLVDKKGeplrKSIIWC---DSRAVETGNKAFNEIGEEKCASHLLNSPANFTASKLKWVQENEPDIYSQI 154
Cdd:cd07798 75 VSSTSQREGIVFLDKDG----RELYAGpniDARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 155 HKFMLPGDYIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGT 234
Cdd:cd07798 151 ATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 235 PIFYRAGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHV---NYQKGAAARIgkllcingAGIQ 311
Cdd:cd07798 231 PVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLvpgKWVLESNAGV--------TGLN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 312 YRWLLNNLAVS---SYEEMNNLASEIPVGSDGvCLIPFGNGAERMLNNKEIGTRIVNMNLNNH---HKGHMCRAALEGIA 385
Cdd:cd07798 303 YQWLKELLYGDpedSYEVLEEEASEIPPGANG-VLAFLGPQIFDARLSGLKNGGFLFPTPLSAselTRGDFARAILENIA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199785844 386 FSFVYGMEILK--SDGIKPSVIRAGndNLFRSEIFANTVATLIEQEI---EIYNTTgAIGAARAAN 446
Cdd:cd07798 382 FAIRANLEQLEevSGREIPYIILCG--GGSRSALLCQILADVLGKPVlvpEGREAS-ALGAAICAA 444
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
2-243 |
3.31e-50 |
|
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: 171.75 E-value: 3.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPEEemgMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENP---QITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLN--SPAnFTASKLKWVQENEPDIYSQIHKFML 159
Cdd:pfam00370 77 NQGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLpiWPG-FTLSKLRWIKENEPEVFEKIHKFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 160 PGDYIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPIFYR 239
Cdd:pfam00370 156 IHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGG 235
|
....
gi 1199785844 240 AGDQ 243
Cdd:pfam00370 236 GGDQ 239
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
2-445 |
6.39e-50 |
|
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: 176.26 E-value: 6.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPEEEMGMFAqknGWAEQKPNDWWLHICNAITKLKKEynISRTQIKGIGIS 81
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVD-EDGTVLASASEPYPTSRPGP---GWVEQDPEDWWEALRSLLRELPAE--LRPRRVVAIAVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSPAnFTASKLKWVQENEPDIYSQIHKFMLPG 161
Cdd:cd07783 75 GTSGTLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPS-SSLAKLLWLKRHEPEVLAKTAKFLHQA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 162 DYIAYKFSNKINTT--ISGLSEGifWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAGTPI--- 236
Cdd:cd07783 154 DWLAGRLTGDRGVTdyNNALKLG--YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVvag 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 237 -------FYRAGdqpnnalslnVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHVN--YQKGAAarigkllcIN- 306
Cdd:cd07783 232 ttdsiaaFLASG----------AVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGVYSHRHGDgyWLVGGA--------SNt 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 307 GAGIqYRWLLNNlavssyEEMNNLASEI-PVGSDGVCLIPFGNGAERM-LNNKEIGTRIVNmnlNNHHKGHMCRAALEGI 384
Cdd:cd07783 294 GGAV-LRWFFSD------DELAELSAQAdPPGPSGLIYYPLPLRGERFpFWDPDARGFLLP---RPHDRAEFLRALLEGI 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199785844 385 AFSFVYGMEILKSDGIKP--SVIRAGNDNlfRSEIFANTVATLIEQEIEIY-NTTGAIGAARAA 445
Cdd:cd07783 364 AFIERLGYERLEELGAPPveEVRTAGGGA--RNDLWNQIRADVLGVPVVIAeEEEAALGAALLA 425
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
3-447 |
2.53e-48 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 173.61 E-value: 2.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 3 YLGLDIGSSSIKAALVEvETGKslgVVQEPEEEMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYniSRTQIKGIGISY 82
Cdd:PRK15027 2 YIGIDLGTSGVKVILLN-EQGE---VVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 83 QMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSPAnFTASKLKWVQENEPDIYSQIHKFMLPGD 162
Cdd:PRK15027 76 QMHGATLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPG-FTAPKLLWVQRHEPEIFRQIDKVLLPKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 163 YIAYKFSNKINTTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEEECGLAAgTPIFYRAGD 242
Cdd:PRK15027 155 YLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 243 QPNNALSLNVFNPGEVAATGGTSGVVYAVTDSLSAKESSRVNNFAHVNYQKG--AAARIGKLLCINgagiqyrWLLNNLA 320
Cdd:PRK15027 234 NAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWhlMSVMLSAASCLD-------WAAKLTG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 321 VSSYEEMNNLASEIPVGSDGVCLIPFGNGAERMLNNKEigTRIVNMNLNNHH-KGHMCRAALEGIAFSFVYGMEILKSDG 399
Cdd:PRK15027 307 LSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQ--AKGVFFGLTHQHgPNELARAVLEGVGYALADGMDVVHACG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1199785844 400 IKP-SVIRAGNDNlfRSEIFANTVATLIEQEIEiYNTTG----AIGAARAANL 447
Cdd:PRK15027 385 IKPqSVTLIGGGA--RSEYWRQMLADISGQQLD-YRTGGdvgpALGAARLAQI 434
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
2-455 |
1.58e-42 |
|
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: 158.08 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVETGKSLGVVQEPEEeMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLADGEELASAVVPYP-TGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVEtgnKAfNEIgEEKCASHLLNSPANFTA--------SKLKWVQENEPDIYSQ 153
Cdd:cd07781 80 TTSSTVVPVDEDGNPLAPAILWMDHRAQE---EA-AEI-NETAHPALEYYLAYYGGvyssewmwPKALWLKRNAPEVYDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 154 IHKFMLPGDYIAYKFSNKI-----NTTISGL--SEGIFWDfkndsvADFL----LEYYGINKDLVPDIVDtfsvqslVDE 222
Cdd:cd07781 155 AYTIVEACDWINARLTGRWvrsrcAAGHKWMynEWGGGPP------REFLaaldPGLLKLREKLPGEVVP-------VGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 223 K-GE------EECGLAAGTPIFYRAGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSlsakessrvnnfahVNYQKGa 295
Cdd:cd07781 222 PaGTltaeaaERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPK--------------PVDIPG- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 296 aarigkllcING--------------AGiQ------YRWLLNNLA-------VSSYEEMNNLASEIPVGSDGVCLIPFGN 348
Cdd:cd07781 287 ---------ICGpvpdavvpglygleAG-QsavgdiFAWFVRLFVppaeergDSIYALLSEEAAKLPPGESGLVALDWFN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 349 GAERMLNNKEIGTRIVNMNLnNHHKGHMCRAALEGIAFsfvyG----MEILKSDGIKPSVIRAGNDNLFRSEIFANTVAT 424
Cdd:cd07781 357 GNRTPLVDPRLRGAIVGLTL-GTTPAHIYRALLEATAF----GtraiIERFEEAGVPVNRVVACGGIAEKNPLWMQIYAD 431
|
490 500 510
....*....|....*....|....*....|...
gi 1199785844 425 LIEQEIEI--YNTTGAIGAARAANLHKGDFETF 455
Cdd:cd07781 432 VLGRPIKVpkSDQAPALGAAILAAVAAGVYADI 464
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
2-484 |
6.33e-34 |
|
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: 133.61 E-value: 6.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQE-------PEEEMGM-FAQKNGWAeqkpndwwlHICNAITKLKKEYNISRT 73
Cdd:cd07775 1 YLLALDAGTGSGRAVIFD-LEGNQIAVAQRewrhkevPDVPGSMdFDTEKNWK---------LICECIREALKKAGIAPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 74 QIKGIGISYQMHGLVLVDKKGEPlrksiIW-C---DSRA---VETGNKAFNEIGEE--KCAShllNSPANFTASKLKWVQ 144
Cdd:cd07775 71 SIAAISTTSMREGIVLYDNEGEE-----IWaCanvDARAaeeVSELKELYNTLEEEvyRISG---QTFALGAIPRLLWLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 145 ENEPDIYSQIHKFMLPGDYIAYKFSNKINTTIS-GLSEGIFwDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEK 223
Cdd:cd07775 143 NNRPEIYRKAAKITMLSDWIAYKLSGELAVEPSnGSTTGLF-DLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 224 GEEECGLAAGTPIFYRAGDQPNNALSLNVFNPGEVAATGGT-----SGVVYAVTDSlsaKESSRVNnfAHV--------- 289
Cdd:cd07775 222 AAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSfwqqeVNTAAPVTDP---AMNIRVN--CHVipdmwqaeg 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 290 -NYQKGAAAR-IGKLLCINGAGIQYRwllnnLAVSSYEEMNNLASEIPVGSDGVclIPFGNGAERMLNNKEIGTRIVNMN 367
Cdd:cd07775 297 iSFFPGLVMRwFRDAFCAEEKEIAER-----LGIDAYDLLEEMAKDVPPGSYGI--MPIFSDVMNYKNWRHAAPSFLNLD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 368 LN--NHHKGHMCRAALEGIAF-SFVYGMEILKSDGIKP-SVIRAGNDNlfRSEIFANTVATLIEQEIEIY---NTT---G 437
Cdd:cd07775 370 IDpeKCNKATFFRAIMENAAIvSAGNLERIAEFSGIFPdSLVFAGGAS--KGKLWCQILADVLGLPVKVPvvkEATalgA 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1199785844 438 AIGAARAANLHKgDFETFGKVIMDNDHvmTFMPFKD-KKPYLEAYNNW 484
Cdd:cd07775 448 AIAAGVGAGIYS-SLEEAVESLVKWER--EYLPNPEnHEVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
2-445 |
1.22e-31 |
|
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: 126.18 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVETGKSLGVVQEPEEEmGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNIsrtQIKGIGIS 81
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVSRPTPA-PISSDDPGRSEQDPEKILEAVRNLIDELPREYLS---DVTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSPANFTASKLKWVQENEPdIYSQIHKFMLPG 161
Cdd:cd07777 77 GQMHGIVLWDEDGNPVSPLITWQDQRCSEEFLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGP-LPSKADRAGTIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 162 DYIAYKFSNKINTTISGL---SEGIF------WDFKndsvadfLLEYYGINKDLVPDIVDTFSVqslvdeKGEEECGLAA 232
Cdd:cd07777 156 DYIVARLTGLPKPVMHPTnaaSWGLFdletgtWNKD-------LLEALGLPVILLPEIVPSGEI------VGTLSSALPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 233 GTPIFYRAGDQ----------PNNALSLNVfnpgevaatgGTSGVVYAVTDSLSAKESSRV-----NNFAHVnyqkgAAA 297
Cdd:cd07777 223 GIPVYVALGDNqasvlgsglnEENDAVLNI----------GTGAQLSFLTPKFELSGSVEIrpffdGRYLLV-----AAS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 298 rigkllcINGaGIQYRWLLNNLA------------VSSYEEMNNLASEIpvGSDGVCLIPFGNGaERMlnNKEIGTRIVN 365
Cdd:cd07777 288 -------LPG-GRALAVLVDFLRewlrelggslsdDEIWEKLDELAESE--ESSDLSVDPTFFG-ERH--DPEGRGSITN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 366 MNLNNHHKGHMCRAALEGIA--FSFVYGMEILKSDGIKpSVIRAGNdNLFRSEIFANTVATLIEQEIEI--YNTTGAIGA 441
Cdd:cd07777 355 IGESNFTLGNLFRALCRGIAenLHEMLPRLDLDLSGIE-RIVGSGG-ALRKNPVLRRIIEKRFGLPVVLseGSEEAAVGA 432
|
....
gi 1199785844 442 ARAA 445
Cdd:cd07777 433 ALLA 436
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
2-485 |
1.33e-31 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 127.43 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQE----PEEE-----MGmFAQKNGWAeqkpndwwlHICNAITKLKKEYNISR 72
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFD-LNGNQIAVGQAewrhLAVPdvpgsME-FDLEKNWQ---------LACQCIRQALQKAGIPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 73 TQIKGIGISYQMHGLVLVDKKGEPlrksiIW-C---DSRAVETGN---KAFNEIGEE--KCASHLLNSPAnftASKLKWV 143
Cdd:PRK10939 73 SDIAAVSATSMREGIVLYDRNGTE-----IWaCanvDARASREVSelkELHNNFEEEvyRCSGQTLALGA---LPRLLWL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 144 QENEPDIYSQIHKFMLPGDYIAYKFSNKINTTIS-GLSEGIFwDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDE 222
Cdd:PRK10939 145 AHHRPDIYRQAHTITMISDWIAYMLSGELAVDPSnAGTTGLL-DLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 223 KGEEECGLAAGTPIFYRAGDQPNNALSLNVFNPGEVAATGGT--SGVV---YAVTDslsAKESSRVNnfAHVnyqkgaaa 297
Cdd:PRK10939 224 KAAAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTfwQQVVnlpAPVTD---PNMNIRIN--PHV-------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 298 rigkllcING----------AGIQYRW-----------LLNNLAVSSYEEMNNLASEIPVGSDGVclIPFGNGAERMLNN 356
Cdd:PRK10939 291 -------IPGmvqaesisffTGLTMRWfrdafcaeeklLAERLGIDAYSLLEEMASRVPVGSHGI--IPIFSDVMRFKSW 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 357 KEIGTRIVNMNL--NNHHKGHMCRAALEGIAFSFVYGME-ILKSDGIKP-SVIRAG--NDNLFRSEIFANtvATLIEQEI 430
Cdd:PRK10939 362 YHAAPSFINLSIdpEKCNKATLFRALEENAAIVSACNLQqIAAFSGVFPsSLVFAGggSKGKLWSQILAD--VTGLPVKV 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199785844 431 EIYNTTGAIGAARAANLHKGDFETF---GKVIMDNDHvmTFMPFKD-KKPYLEAYNNWK 485
Cdd:PRK10939 440 PVVKEATALGCAIAAGVGAGIYSSLaetGERLVRWER--TFEPNPEnHELYQEAKEKWQ 496
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
2-387 |
4.36e-31 |
|
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: 125.04 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVEtGKSLGVVQEPeeeMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLD-GRELAVAARR---NAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMHGLVLVDKKGEPLRKSIIWCDSRAVE---------TGNKAFNEIGEEKCASHllnspanfTASKLKWVQENEPDIYS 152
Cdd:cd24121 77 GQGDGTWLVDEDGRPVRDAILWLDGRAADiverwqadgIAEAVFEITGTGLFPGS--------QAAQLAWLKENEPERLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 153 QIHKFMLPGDYIAYKFSNKINTTISGLSEgIFWDFKNDSVADFLLEYYGIN--KDLVPDIVDTFSVQSLVDEKGEEECGL 230
Cdd:cd24121 149 RARTALHCKDWLFYKLTGEIATDPSDASL-TFLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 231 AAGTPIFYRAGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDS--LSAKESSRVnnFAHvnyqkGAAARIGKLLCINGA 308
Cdd:cd24121 228 PAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVVDEpdLEPEGVGYT--ICL-----GVPGRWLRAMANMAG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 309 GIQYRWLL-----------NNLAVSSYEEMNNLASEIPVGSDGVCLIPFGNGAermlnnkeiGTR--IVNMN-------L 368
Cdd:cd24121 301 TPNLDWFLrelgevlkegaEPAGSDLFQDLEELAASSPPGAEGVLYHPYLSPA---------GERapFVNPNaraqftgL 371
|
410 420
....*....|....*....|
gi 1199785844 369 NNHH-KGHMCRAALEGIAFS 387
Cdd:cd24121 372 SLEHtRADLLRAVYEGVALA 391
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
2-485 |
2.23e-30 |
|
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: 123.35 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPeeemgmFAQ---KNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGI 78
Cdd:cd07769 1 YILAIDQGTTSTRAILFD-EDGNIVASAQKE------HEQiypQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 79 GISYQMHGLVLVDKK-GEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASH--LLNSPAnFTASKLKWVQENEPDIYSQIH 155
Cdd:cd07769 74 GITNQRETTVVWDKKtGKPLYNAIVWQDRRTADICEELKAKGLEERIREKtgLPLDPY-FSATKIKWILDNVPGARERAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 156 KfmlpGD--------YIAYKFSNKIN--TTISGLSE-GIF------WDfkndsvaDFLLEYYGINKDLVPDIVDTFSVQS 218
Cdd:cd07769 153 R----GEllfgtidtWLIWKLTGGKVhvTDVTNASRtMLFnihtleWD-------DELLELFGIPRSMLPEVRPSSEVFG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 219 LVDekgeeECGLAAGTPIFYRAGDQPNNALSLNVFNPGEVAATGGTSGVVYAVTDSlSAKESSR--VNNFA-----HVNY 291
Cdd:cd07769 222 YTD-----PEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGE-KPVPSKNglLTTIAwqiggKVTY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 292 Q-KGAAArigkllcINGAGIQyrWLLNNL-AVSSYEEMNNLASEIPvGSDGVCLIP-F-GNGAERMLNNkeigTR--IVN 365
Cdd:cd07769 296 AlEGSIF-------IAGAAIQ--WLRDNLgLIEDAAETEELARSVE-DNGGVYFVPaFsGLGAPYWDPD----ARgaIVG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 366 MNLnNHHKGHMCRAALEGIAFSFVYGMEILKSD-GIKPSVIRAG-----NDNL--FRSEIFANTVATLIEQEieiynTTg 437
Cdd:cd07769 362 LTR-GTTKAHIVRAALESIAYQTRDVLEAMEKDsGIKLKELRVDggataNNFLmqFQADILGVPVVRPKVAE-----TT- 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1199785844 438 AIGAARAANLHKGDFETFGKVIMDNDHVMTFMPFKDKKPYLEAYNNWK 485
Cdd:cd07769 435 ALGAAYLAGLAVGFWKDLDELASLWQVDKRFEPSMDEEERERLYRGWK 482
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
2-493 |
9.57e-30 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 122.00 E-value: 9.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPEEEmgmFAQKNGWAEQKPNDWWLHICNAIT---KLKKEYNISRtQIKGI 78
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFD-EKGNVVSSHQIPHEQ---ITPHPGWLEHDPEEILRNVYKCMNeaiKKLREKGPSF-KIKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 79 GISYQMHGLVLVDKK-GEPLRKSIIWCDSRAVETGNKAFNEIGEEKCASHLLNSPAN--FTASKLKWVQENEPDIYSQIH 155
Cdd:PTZ00294 78 GITNQRETVVAWDKVtGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQKITGLPIStyFSAFKIRWMLENVPAVKDAVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 156 K----FMLPGDYIAYKFSNKIN--TTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVdeKGEEECG 229
Cdd:PTZ00294 158 EgtllFGTIDTWLIWNLTGGKShvTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTI--SGEAVPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 230 LaAGTPIFYRAGDQPNNALSLNVFNPGEVAATGGTSgvVYAVTDSLSAKESSRVNNFAHVNYQKGAAARIGKLL--CING 307
Cdd:PTZ00294 236 L-EGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTG--CFLLMNTGTEIVFSKHGLLTTVCYQLGPNGPTVYALegSIAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 308 AGIQYRWLLNNLA-VSSYEEMNNLASEIPvGSDGVCLIP-F-GNGAERMlNNKEIGTrIVNMNLNNhHKGHMCRAALEGI 384
Cdd:PTZ00294 313 AGAGVEWLRDNMGlISHPSEIEKLARSVK-DTGGVVFVPaFsGLFAPYW-RPDARGT-IVGMTLKT-TRAHIVRAALEAI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 385 AFSFVYGMEILKSD-GIKPSVIRAgNDNLFRSEIFANTVATLIEQEIE--IYNTTGAIGAARAANLHKGDFETFGKV-IM 460
Cdd:PTZ00294 389 ALQTNDVIESMEKDaGIELNSLRV-DGGLTKNKLLMQFQADILGKDIVvpEMAETTALGAALLAGLAVGVWKSLEEVkKL 467
|
490 500 510
....*....|....*....|....*....|...
gi 1199785844 461 DNDHVMTFMPFKDKKPYLEAYNNWKNELELILN 493
Cdd:PTZ00294 468 IRRSNSTFSPQMSAEERKAIYKEWNKAVERSLK 500
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
2-489 |
6.34e-29 |
|
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: 119.20 E-value: 6.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVEtGKSLGVVQE------PEEemgmfaqknGWAEQKPNDWWLHICNAITKLKKEYNISRTQI 75
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKK-GKIIGSSSEkvevlyPEP---------GWVEIDPEELWQQFVKVIKEALKNAGLTPEDI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 76 KGIGISYQMHGLVLVDKK-GEPLRKSIIWCDSRA---VETGN-----KAFNEIGeeKCASHLLNSPANFTAS-------- 138
Cdd:cd07793 71 AAIGISTQRNTFLTWDKKtGKPLHNFITWQDLRAaelCESWNrslllKALRGGS--KFLHFLTRNKRFLAASvlkfstah 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 139 ---KLKWVQENEPDIYSQIHKfmlpGD--------YIAYKFSN-KINTTisglsegifwDFKNDSV-----------ADF 195
Cdd:cd07793 149 vsiRLLWILQNNPELKEAAEK----GEllfgtidtWLLWKLTGgKVHAT----------DYSNASAtglfdpftlewSPI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 196 LLEYYGINKDLVPDIVDTFSVQSLVDEKgeeecGLAAGTPIFYRAGDQPNNALSLNVFNPGEVAATGGTSGvvyavtdsl 275
Cdd:cd07793 215 LLSLFGIPSSILPEVKDTSGDFGSTDPS-----IFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGT--------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 276 sakessrvnnFAHVNYQKGAAARIGKL--LC---INGaGIQY-------------RWLLNNLAVSSYEEMNNLASEIPvG 337
Cdd:cd07793 281 ----------FIDINTGSKPHASVKGLypLVgwkIGG-EITYlaegnasdtgtviDWAKSIGLFDDPSETEDIAESVE-D 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 338 SDGVCLIPFGNGAERMLNNKEIGTRIVNMNLNNhHKGHMCRAALEGIAFSFVYGMEILKSD-GIKPSVIRAgNDNLFRSE 416
Cdd:cd07793 349 TNGVYFVPAFSGLQAPYNDPTACAGFIGLTPST-TKAHLVRAILESIAFRVKQLLETMEKEtSIKISSIRV-DGGVSNND 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 417 IFANTVATLIEQEIE-IYNT-TGAIGAARAANLHKG------DFETFGKVimdnDHVmtFMPFKDKKPYLEAYNNWKNEL 488
Cdd:cd07793 427 FILQLIADLLGKPVErPKNTeMSALGAAFLAGLASGiwkskeELKKLRKI----EKI--FEPKMDNEKREELYKNWKKAV 500
|
.
gi 1199785844 489 E 489
Cdd:cd07793 501 K 501
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
3-485 |
1.69e-25 |
|
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: 109.15 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 3 YLG-LDIGSSSIKAALVEvETGKSLGVVQEPeeemgmFAQ---KNGWAEQKPNDWWLH----ICNAITKLKKEyNISRTQ 74
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFD-STGELVASHQVE------HKQiypKPGWVEHDPMEILESvyecIEEAVEKLKAL-GISPSD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 75 IKGIGISYQMHGLVLVDKK-GEPLRKSIIWCDSRAVETGNKAFNEIGE------EKCAshLLNSPAnFTASKLKWVQENE 147
Cdd:cd07792 74 IKAIGITNQRETTVVWDKStGKPLYNAIVWLDTRTSDTVEELSAKTPGgkdhfrKKTG--LPISTY-FSAVKLRWLLDNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 148 PDIYSQIHKfmlpGD--------YIAYKFSNKIN-----TTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVdtf 214
Cdd:cd07792 151 PEVKKAVDD----GRllfgtvdsWLIWNLTGGKNggvhvTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIR--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 215 svqSLVDEKGEEECGLAAGTPIFYRAGDQpNNALslnV----FNPGEVAATGGTsGVVYAVTDSLSAKESSrvnnfaH-- 288
Cdd:cd07792 224 ---SSSEVYGKIASGPLAGVPISGCLGDQ-QAAL---VgqgcFKPGEAKNTYGT-GCFLLYNTGEEPVFSK------Hgl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 289 ---VNYQKGAAAR--------IGkllcINGAGIQyrWLLNNLA-VSSYEEMNNLASEIPvGSDGVCLIPFGNG------- 349
Cdd:cd07792 290 lttVAYKLGPDAPpvyalegsIA----IAGAAVQ--WLRDNLGiISSASEVETLAASVP-DTGGVYFVPAFSGlfapywr 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 350 --AErmlnnkeiGTrIVNMNLNNhHKGHMCRAALEGIAFSfvyGMEILKS---D-GIKPSVIRAG----NDNLFRsEIFA 419
Cdd:cd07792 363 pdAR--------GT-IVGLTQFT-TKAHIARAALEAVCFQ---TREILDAmnkDsGIPLTSLRVDggmtKNNLLM-QIQA 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199785844 420 NTVATLIEQEiEIYNTTgAIGAARAANLHKGDF-ETFGKVIMDNDHVMTFMPFKDKKPYLEAYNNWK 485
Cdd:cd07792 429 DILGIPVERP-SMVETT-ALGAAIAAGLAVGVWkSLDELKSLNEGGRTVFEPQISEEERERRYKRWK 493
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
2-450 |
1.41e-21 |
|
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: 97.56 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQEPeeemgmFAQ---KNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGI 78
Cdd:cd07786 1 YILAIDQGTTSSRAILFD-HDGNIVAVAQRE------FTQiypKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 79 GISYQMHGLVLVDKK-GEPLRKSIIWCDSRAVETGNKaFNEIGEEKC---ASHLLNSPAnFTASKLKWVQENEPDIYSQI 154
Cdd:cd07786 74 GITNQRETTVVWDREtGKPVYNAIVWQDRRTADICEE-LKAEGHEEMireKTGLVLDPY-FSATKIRWILDNVPGARERA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 155 HKfmlpGD--------YIAYKFSN-KINTT------------ISGLSegifWDfkndsvaDFLLEYYGINKDLVPDIVDT 213
Cdd:cd07786 152 ER----GElafgtidsWLIWKLTGgKVHATdvtnasrtmlfnIHTLE----WD-------DELLELFGIPASMLPEVKPS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 214 FSVQSLVDEKgeeecGLAAGTPIFYRAGDQpNNAL-SLNVFNPGEVAATGGTSGVVYAVTDSlSAKESsrvnnfahvnyQ 292
Cdd:cd07786 217 SEVFGYTDPD-----LLGAEIPIAGIAGDQ-QAALfGQACFEPGMAKNTYGTGCFMLMNTGE-KPVRS-----------K 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 293 KG----AAARIGKLLC--------INGAGIQyrWLLNNL-AVSSYEEMNNLASEIPvGSDGVCLIP-F-GNGA------- 350
Cdd:cd07786 279 NGllttIAWQLGGKVTyalegsifIAGAAVQ--WLRDGLgLIESAAETEALARSVP-DNGGVYFVPaFtGLGApywdpda 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 351 -------ERmlnnkeiGTRivnmnlnnhhKGHMCRAALEGIAFSFVYGMEILKSD-GIKPSVIR-----AGNDNL--FRS 415
Cdd:cd07786 356 rgaifglTR-------GTT----------RAHIARAALESIAYQTRDLLEAMEADsGIPLKELRvdggaSANDFLmqFQA 418
|
490 500 510
....*....|....*....|....*....|....*..
gi 1199785844 416 EIFANTVA--TLIEqeieiynTTgAIGAARAANLHKG 450
Cdd:cd07786 419 DILGVPVErpKVTE-------TT-ALGAAYLAGLAVG 447
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
2-452 |
2.07e-20 |
|
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: 94.23 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVETGKSLGvvQEPEEEMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGIS 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYAGLEMA--QEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 82 YQMhGLVLVDKKGEPLRKS---------IIWCDSRAVETGNkAFNEIGEEKCASHLLN--SPANFTAsKLKWVQENEPDI 150
Cdd:cd07768 79 ATC-SLAIFDREGTPLMALipypnednvIFWMDHSAVNEAQ-WINMQCPQQLLDYLGGkiSPEMGVP-KLKYFLDEYSHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 151 YSQIHKFMLPGDYIAYKFSNKINTTISGLSEGIFWD----------FKNDSVADFLLEYYGINKDLVPdiVDTFSVQSLv 220
Cdd:cd07768 156 RDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDgeesgwsssfFKNIDPRLEHLTTTKNLPSNVP--IGTTSGVAL- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 221 dEKGEEECGLAAGTPIFYRAGDQPNNALSLNVFN-PGEVAATGGTS-----------------GVVYAVTDS----LSAK 278
Cdd:cd07768 233 -PEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHlETSLFMIAGTSschmygttisdripgvwGPFDTIIDPdysvYEAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 279 ESSRVNNFAHVnYQKGAAARigKLLCINGAGiqyrwllnnlaVSSYEEMNNLASEI---PVGSDGVCLIPFGNGAERMLN 355
Cdd:cd07768 312 QSATGKLIEHL-FESHPCAR--KFDEALKKG-----------ADIYQVLEQTIRQIeknNGLSIHILTLDMFFGNRSEFA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 356 NKEIGTRIVNMNLNNHHK--GHMCRAALEGIAFSFVYGMEILKSDGIKPSVIRAG----NDNLFRSEI-FANTVATLIEQ 428
Cdd:cd07768 378 DPRLKGSFIGESLDTSMLnlTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASggqaKNERLLQLIaLVTNVAIIKPK 457
|
490 500
....*....|....*....|....
gi 1199785844 429 EieiyNTTGAIGAARAANLHKGDF 452
Cdd:cd07768 458 E----NMMGILGAAVLAKVAAGKK 477
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
2-406 |
5.42e-19 |
|
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: 89.51 E-value: 5.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVETGK-SLgvvqepeEEMGMFA----QKNG---WaeqkpnDW---WLHICNAITKLKKEYNi 70
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKlEL-------EEIHRFPnrpvEINGhlyW------DIdrlFDEIKEGLKKAAEQGG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 71 srtQIKGIGI-----SYqmhglVLVDKKGEPLRKsiIWC--DSRAVETGNKAFNEIGEEKCASHLLNSPANF-TASKLKW 142
Cdd:cd07771 67 ---DIDSIGIdtwgvDF-----GLLDKNGELLGN--PVHyrDPRTEGMMEELFEKISKEELYERTGIQFQPInTLYQLYA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 143 VQENEPDIYSQIHKFMLPGDYIAYKFSNKINT--TISGLSEgiFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLV 220
Cdd:cd07771 137 LKKEGPELLERADKLLMLPDLLNYLLTGEKVAeyTIASTTQ--LLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 221 DEKGEEECGLAAgtpifyragdqpnnalsLNVFNPGE------VAATG-----------GTSGVVYAVTDSLSAKESSRV 283
Cdd:cd07771 215 KPEVAEELGLKG-----------------IPVIAVAShdtasaVAAVPaededaafissGTWSLIGVELDEPVITEEAFE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 284 NNFAhvNyQKGAAARIgkLLCINGAGiqyRWLLNNLA--------VSSYEEMNNLASEIPvgsDGVCLIPFgnGAERMLN 355
Cdd:cd07771 278 AGFT--N-EGGADGTI--RLLKNITG---LWLLQECRreweeegkDYSYDELVALAEEAP---PFGAFIDP--DDPRFLN 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199785844 356 NKEIGTRIVNM--NLNN---HHKGHMCRAALEGIAFSFVYGMEILKS-DGIKPSVIR 406
Cdd:cd07771 345 PGDMPEAIRAYcrETGQpvpESPGEIARCIYESLALKYAKTIEELEElTGKRIDRIH 401
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
2-169 |
7.18e-16 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 79.89 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVqepEEEMGMFAQKNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGIGI- 80
Cdd:cd07782 1 YYIGVDVGTGSARAGLFD-LDGRLLATA---SQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 81 ---SyqmhgLVLVDKKGEPL---------RKSIIWCDSRAVETGNKaFNEIGEEkcashLLN------SPANFTaSKLKW 142
Cdd:cd07782 77 atcS-----LVVLDAEGKPVsvspsgddeRNVILWMDHRAVEEAER-INATGHE-----VLKyvggkiSPEMEP-PKLLW 144
|
170 180
....*....|....*....|....*...
gi 1199785844 143 VQENEPDIYSQIHKFM-LPgDYIAYKFS 169
Cdd:cd07782 145 LKENLPETWAKAGHFFdLP-DFLTWKAT 171
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-167 |
1.09e-14 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 76.31 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 1 MYYLGLDIGSSSIKAALVEVETGKSLG--VVQEPEEEMGMFAQKNG-WAEQKPNDWWLHICNAITKLKKEYNISRTQIKG 77
Cdd:COG1069 2 KYVIGVDFGTDSVRAVVVDAADGEELAsaVHPYPRWVIGLYLPPPPdQARQHPLDYLEALEAAVREALAQAGVDPADVVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 78 IGISYQMHGLVLVDKKGEPL-----------RKSIIWCDSRAVETGNKaFNEIGEEKCASHL-----LNSPANFTAsKLK 141
Cdd:COG1069 82 IGVDATGCTPVPVDADGTPLallpefaenphAMVILWKDHTAQEEAER-INELAKARGEDYLryvggIISSEWFWP-KIL 159
|
170 180
....*....|....*....|....*.
gi 1199785844 142 WVQENEPDIYSQIHKFMLPGDYIAYK 167
Cdd:COG1069 160 HLLREDPEVYEAADSFVELCDWITWQ 185
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
39-470 |
6.35e-14 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 73.97 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 39 FAQ---KNGWAEQKPNDWW--LHIC--NAITKLK-KEYNISrTQIKGIGISYQMHGLVLVDKK-GEPLRKSIIWCDSRAV 109
Cdd:PLN02295 31 FTQiypQAGWVEHDPMEILesVLTCiaKALEKAAaKGHNVD-SGLKAIGITNQRETTVAWSKStGRPLYNAIVWMDSRTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 110 ETGNKAFNEIGE------EKCAshlLNSPANFTASKLKWVQENEPDIYSQIHKfmlpGD--------YIAYKFSNKIN-- 173
Cdd:PLN02295 110 SICRRLEKELSGgrkhfvETCG---LPISTYFSATKLLWLLENVDAVKEAVKS----GDalfgtidsWLIWNLTGGASgg 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 174 ---TTISGLSEGIFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDEKGEeecglAAGTPIFYRAGDQpNNALSL 250
Cdd:PLN02295 183 vhvTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIGTIAKGWP-----LAGVPIAGCLGDQ-HAAMLG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 251 NVFNPGEVAATGGTS----------------GVVYAVTDSLSAKessrvnnfAHVNYQ-KGAAArigkllcINGAGIQyr 313
Cdd:PLN02295 257 QRCRPGEAKSTYGTGcfillntgeevvpskhGLLTTVAYKLGPD--------APTNYAlEGSVA-------IAGAAVQ-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 314 WLLNNLAV-SSYEEMNNLASEIPvGSDGVCLIPFGNG--AERMLNNkeigTRIVNMNLNN-HHKGHMCRAALEGIAF--- 386
Cdd:PLN02295 320 WLRDNLGIiKSASEIEALAATVD-DTGGVYFVPAFSGlfAPRWRDD----ARGVCVGITRfTNKAHIARAVLESMCFqvk 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 387 ----SFVYGMEILKSDGiKPSVIR----AGNDNL---FRSEIFANTVATLIEQEieiyntTGAIGAARAANLHKG---DF 452
Cdd:PLN02295 395 dvldAMRKDAGEEKSHK-GLFLLRvdggATANNLlmqIQADLLGSPVVRPADIE------TTALGAAYAAGLAVGlwtEE 467
|
490
....*....|....*...
gi 1199785844 453 ETFGKVIMDNDhvMTFMP 470
Cdd:PLN02295 468 EIFASEKWKNT--TTFRP 483
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
69-399 |
5.65e-10 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 61.20 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 69 NISRTQIKGIGIS-YQMHGlVLVDKKGEPLRKSIIWCDSRAVETGNKAFNEIGEEKCasHLLNSPANF---TASKLKWVQ 144
Cdd:PRK10331 66 ELTECHIRGITVTtFGVDG-ALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQL--QQISGVGAFsfnTLYKLVWLK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 145 ENEPDIYSQIHKFMLPGDYIAYKFSNKINT--TISGLSEgiFWDFKNDSVADFLLEYYGINKDLVPDIVDTFSVQSLVDE 222
Cdd:PRK10331 143 ENHPQLLEQAHAWLFISSLINHRLTGEFTTdiTMAGTSQ--MLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 223 KGEEECGLAAGTPIFyRAGDQPNNALslnvFNPG----EVAATGGTSGVVYAvtdslsakESSRVNNFAHVNYQkGAAAR 298
Cdd:PRK10331 221 SAAALLGLPVGIPVI-SAGHDTQFAL----FGSGagqnQPVLSSGTWEILMV--------RSAQVDTSLLSQYA-GSTCE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 299 IGKLLCINGAGIQY------RWLLNNL--AVSSYEEMNNLASEIPVGSDGVCLIPfgngaeRMLNNKEIGTRIVNMNLNn 370
Cdd:PRK10331 287 LDSQSGLYNPGMQWlasgvlEWVRKLFwtAETPYQTMIEEARAIPPGADGVKMQC------DLLACQNAGWQGVTLNTT- 359
|
330 340
....*....|....*....|....*....
gi 1199785844 371 hhKGHMCRAALEGIAFSFVYGMEILKSDG 399
Cdd:PRK10331 360 --RGHFYRAALEGLTAQLKRNLQVLEKIG 386
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-450 |
1.62e-09 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 59.84 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEvETGKSLGVVQ-EpeeemgmFAQ---KNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKG 77
Cdd:PRK00047 6 YILALDQGTTSSRAIIFD-HDGNIVSVAQkE-------FTQifpQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 78 IGISYQMHGLVLVDKK-GEPLRKSIIWCDSR----AVETGNKAFNEIGEEKcASHLLNspANFTASKLKWVQENEPDIYS 152
Cdd:PRK00047 78 IGITNQRETTVVWDKEtGRPIYNAIVWQDRRtadiCEELKRDGYEDYIREK-TGLVID--PYFSGTKIKWILDNVEGARE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 153 QIHKfmlpGDYIA--------YKFSN-KINTT-ISGLS-------EGIFWDfkndsvaDFLLEYYGINKDLVPDIVDTFS 215
Cdd:PRK00047 155 RAEK----GELLFgtidtwlvWKLTGgKVHVTdYTNASrtmlfniHTLDWD-------DELLELLDIPRSMLPEVRPSSE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 216 VQSLVDEKGeeecGLAAGTPIFYRAGDQpNNALSLNV-FNPGEVAATGGTSGVVYAVTDSlSAKESSrvNNF-------- 286
Cdd:PRK00047 224 VYGKTNPYG----FFGGEVPIAGIAGDQ-QAALFGQLcFEPGMAKNTYGTGCFMLMNTGE-KAVKSE--NGLlttiawgi 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 287 -AHVNYQ-KGAAArigkllcINGAGIQyrWLLNNLA-VSSYEEMNNLASEIPvGSDGVCLIP-F-GNGA------ERmln 355
Cdd:PRK00047 296 dGKVVYAlEGSIF-------VAGSAIQ--WLRDGLKiISDASDSEALARKVE-DNDGVYVVPaFtGLGApywdsdAR--- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 356 nkeiGTrIVNMNLNNhHKGHMCRAALEGIAFS---FVYGMEilKSDGIKPSVIR-----AGNDNL--FRSEIFANTVATL 425
Cdd:PRK00047 363 ----GA-IFGLTRGT-TKEHIIRATLESIAYQtrdVLDAMQ--ADSGIRLKELRvdggaVANNFLmqFQADILGVPVERP 434
|
490 500
....*....|....*....|....*
gi 1199785844 426 IEQEieiynTTgAIGAARAANLHKG 450
Cdd:PRK00047 435 VVAE-----TT-ALGAAYLAGLAVG 453
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
2-170 |
3.55e-07 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 52.54 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 2 YYLGLDIGSSSIKAALVEVETGKSLG--VVQEPEEEMGMFAQ-KNGWAEQKPNDWWLHICNAITKLKKEYNISRTQIKGI 78
Cdd:PRK04123 4 YVIGLDFGTDSVRALLVDCATGEELAtaVVEYPHWVKGRYLDlPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAVVGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 79 GISYQMHGLVLVDKKGEPLRKS-----------IIWCDSRAVETGNkAFNEIGEEKCASHLLN------SPANFTASKLK 141
Cdd:PRK04123 84 GVDFTGSTPAPVDADGTPLALLpefaenphamvKLWKDHTAQEEAE-EINRLAHERGEADLSRyiggiySSEWFWAKILH 162
|
170 180
....*....|....*....|....*....
gi 1199785844 142 WVQENePDIYSQIHKFMLPGDYIAYKFSN 170
Cdd:PRK04123 163 VLRED-PAVYEAAASWVEACDWVVALLTG 190
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-88 |
8.09e-06 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 47.58 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 1 MYYLGLDIGSSSIKAALVEvETGKslgVVQEPEEEMGMFAQKNGWAEQkpndwwlhICNAITKLKKEYNISRTQIKGIGI 80
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVD-LDGE---VLARERIPTPAGAGPEAVLEA--------IAELIEELLAEAGISRGRILGIGI 72
|
....*...
gi 1199785844 81 SyqMHGLV 88
Cdd:COG1940 73 G--VPGPV 78
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
258-446 |
2.23e-05 |
|
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: 45.39 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 258 VAATGGTSGVVYAVTDSLSAKESSRVNNFAHVNYQKGAAARIGkllcINGAGIQYRWLLNNLAVSSYEE--------MNN 329
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEMLPGYWGLEGG----QSAAGSLLAWLLQFHGLREELRdagnveslAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 330 LASEIPVGSDGVCLIPFGNGAERMLNNKEIGTRIVNMNlNNHHKGHMCRAALEGIAFSFVYGMEIL-KSDGIKPSVIRA- 407
Cdd:pfam02782 77 AALAAVAPAGGLLFYPDFSGNRAPGADPGARGSITGLS-SPTTLAHLYRAILESLALQLRQILEALtKQEGHPIDTIHVs 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199785844 408 -GndnLFRSEIFANTVATLIEQEIEI--YNTTGAIGAARAAN 446
Cdd:pfam02782 156 gG---GSRNPLLLQLLADALGLPVVVpgPDEATALGAALLAA 194
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
3-200 |
2.36e-04 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 43.55 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 3 YLGLDIGSSSIKAALVEVETGkslgVVQEPEEEMGMF--AQKNGWAEQKPNDWWlhicNAITKLKKEYNI--SRTQIKGI 78
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGT----LLATSERPISYKqdPKDLWFVTQSSTEIW----KAIKTALKELIEelSDYIVSGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199785844 79 GIS------------YQMHgLV---LVDKKGEPLRKSIIWCDSRAVETGNKaFNEIGEEKCASHLLNSpanFTAS----K 139
Cdd:cd07778 74 GVSatcsmvvmqrdsDTSY-LVpynVIHEKSNPDQDIIFWMDHRASEETQW-LNNILPDDILDYLGGG---FIPEmaipK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199785844 140 LKWVQENEPDIYSQIHKFMLPGDYIAYKFS-NKINTTISGLSEGIFWDFKND-SVADFLLEYY 200
Cdd:cd07778 149 LKYLIDLIKEDTFKKLEVFDLHDWISYMLAtNLGHSNIVPVNAPPSIGIGIDgSLKGWSKDFY 211
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
1-79 |
4.24e-03 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 38.93 E-value: 4.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199785844 1 MYYLGLDIGSSSIKAALVEvETGKSLGVVQEPeeemgmfaqkNGWaeqKPNDwwlHICNAITKLKKEYNISRTQIKGIG 79
Cdd:COG1924 3 MIYLGIDIGSTTTKAVLLD-EDGEILASAYLP----------TGG---DPLE---AAKEALKELLEEAGLKREDIAGVV 64
|
|
| |
