|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
2-437 |
1.02e-173 |
|
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: 495.92 E-value: 1.02e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAESGKTLVRTQYPdreMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAETGRVVASGSAP---HENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQKALAHLLNSPGNFTASKLRWVQENEPELYRRIKHFMLPG 161
Cdd:cd07809 78 GQMHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 162 DYIALKMTGEtcsTISGLSE--GIFWDFLEQKPADLVFQDYG----IDPALMPALQPTFGIQGALRAEAAAELGLVAGIP 235
Cdd:cd07809 158 DYLNWKLTGE---KVTGLGDasGTFPIDPRTRDYDAELLAAIdpsrDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 236 VAYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFAHVNYtlehpsiGVLMCINGAGITYSWLR 315
Cdd:cd07809 235 VAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDSTG-------GMLPLINTTNCLTAWTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 316 QNMGAAGVSYPELEERAAQVPIGADGLSILPFGNsAERILNNVDLGAQIQGLNFNRHGQAHLIRAGLEGIAFAFVYGMSI 395
Cdd:cd07809 308 LFRELLGVSYEELDELAAQAPPGAGGLLLLPFLN-GERTPNLPHGRASLVGLTLSNFTRANLARAALEGATFGLRYGLDI 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 503531638 396 LQEMGLDLKVMR-VGndNLFQSRIFAETIATLCNSHIEMLDTT 437
Cdd:cd07809 387 LRELGVEIDEIRlIG--GGSKSPVWRQILADVFGVPVVVPETG 427
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-492 |
1.35e-146 |
|
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: 428.87 E-value: 1.35e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAEsGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDAD-GEVVASAS---AEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQKALAHLLNSPG-NFTASKLRWVQENEPELYRRIKHFMLP 160
Cdd:COG1070 78 GQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHpGFTAPKLLWLKENEPEIFARIAKVLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 161 GDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVAYRA 240
Cdd:COG1070 158 KDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 241 GDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFAHV---NYTlehpsigVLMCINGAGITYSWLRQN 317
Cdd:COG1070 238 GDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAvpgRWL-------PMGATNNGGSALRWFRDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 318 MGAAGV-SYPELEERAAQVPIGADGLSILPFGNSAERILNNVDLGAQIQGLNFNrHGQAHLIRAGLEGIAFAFVYGMSIL 396
Cdd:COG1070 311 FADGELdDYEELNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLS-HTRAHLARAVLEGVAFALRDGLEAL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 397 QEMGLDLKVMRVGnDNLFQSRIFAETIATLCNSHIEMLDTTGAVGA--AKGAGFGAGVYSSLREALGSTPKVGA-YEP-L 472
Cdd:COG1070 390 EEAGVKIDRIRAT-GGGARSPLWRQILADVLGRPVEVPEAEEGGALgaALLAAVGLGLYDDLEEAAAAMVRVGEtIEPdP 468
|
490 500
....*....|....*....|
gi 503531638 473 SNADAHTAAYSVWLNQLHKL 492
Cdd:COG1070 469 ENVAAYDELYERYRELYPAL 488
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
2-437 |
2.68e-109 |
|
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: 332.97 E-value: 2.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVD-EDGRVLASAS---AEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGqQKALAHLLN--SPGnFTASKLRWVQENEPELYRRIKHFML 159
Cdd:cd07808 77 GQMHGLVLLDKNGRPLRPAILWNDQRSAAECEELEARLG-DEILIITGNppLPG-FTLPKLLWLKENEPEIFARIRKILL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 160 PGDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVAYR 239
Cdd:cd07808 155 PKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 240 AGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFAHVNYTLEHpSIGVlmcINGAGITYSWLRQNMG 319
Cdd:cd07808 235 AGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWY-AMGV---TLSAGLSLRWLRDLFG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 320 AAGVSYPELEERAAQVPIGADGLSILPFgNSAER-ILNNVDL-GAQIqGLNFnRHGQAHLIRAGLEGIAFAFVYGMSILQ 397
Cdd:cd07808 311 PDRESFDELDAEAAKVPPGSEGLLFLPY-LSGERtPYWDPNArGSFF-GLSL-SHTRAHLARAVLEGVAFSLRDSLEVLK 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 503531638 398 EMGLDLKVMRV---GNdnlfQSRIFAETIATLCNSHIEMLDTT 437
Cdd:cd07808 388 ELGIKVKEIRLiggGA----KSPLWRQILADVLGVPVVVPAEE 426
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
4-400 |
2.84e-100 |
|
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: 309.63 E-value: 2.84e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 4 IGYDIGSSSVKAALVDaESGKTLVRTQYPdreMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGISYQ 83
Cdd:TIGR01312 1 LGIDLGTSGVKALLVD-EQGEVIASGSAP---HTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 84 MHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQKALAHLLNS--PGnFTASKLRWVQENEPELYRRIKHFMLPG 161
Cdd:TIGR01312 77 MHGLVLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLalPG-FTAPKLLWVRKHEPEVFARIAKVMLPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 162 DYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVAYRAG 241
Cdd:TIGR01312 156 DYLRYRLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 242 DQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFAHVNYTLEHPsigvLMCINGAGITYSWLRQNMGAa 321
Cdd:TIGR01312 236 DNAAGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGWLP----MGVTLSATSSLEWFRELFGK- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 322 gVSYPELEERAAQVPIGADGLSILPFGNsAERILNNV-DLGAQIQGLNFNrHGQAHLIRAGLEGIAFAFVYGMSILQEMG 400
Cdd:TIGR01312 311 -EDVEALNELAEQSPPGAEGVTFLPYLN-GERTPHLDpQARGSFIGLTHN-TTRADLTRAVLEGVTFALRDSLDILREAG 387
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
2-410 |
6.01e-84 |
|
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: 266.31 E-value: 6.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVD-EDGKVLASAS---IEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 yQMHG-LVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQKalahLLNSPGN-----FTASKLRWVQENEPELYRRIK 155
Cdd:cd07804 77 -GLVPaLVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDR----IFEITGNpldsqSVGPKLLWIKRNEPEVFKKTR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 156 HFMLPGDYIALKMTGE-TCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGI 234
Cdd:cd07804 152 KFLGAYDYIVYKLTGEyVIDYSSAGNEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 235 PVAYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPlsrvnGFAHVNYTLEHPSIgVLMCINGAGITYSWL 314
Cdd:cd07804 232 PVVAGTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDP-----RLWLDYHDIPGTYV-LNGGMATSGSLLRWF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 315 RQNMG--------AAGVS-YPELEERAAQVPIGADGLSILPFgNSAER-ILNNVDLGAQIQGLNFNrHGQAHLIRAGLEG 384
Cdd:cd07804 306 RDEFAgeeveaekSGGDSaYDLLDEEAEKIPPGSDGLIVLPY-FMGERtPIWDPDARGVIFGLTLS-HTRAHLYRALLEG 383
|
410 420
....*....|....*....|....*.
gi 503531638 385 IAFAFVYGMSILQEMGLDLKVMRVGN 410
Cdd:cd07804 384 VAYGLRHHLEVIREAGLPIKRLVAVG 409
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
2-408 |
4.30e-80 |
|
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: 257.45 E-value: 4.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQYPdreMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07805 1 YILAIDLGTSGVKAALVD-LDGELVASAFAP---YPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQKALAHLLNSP--GNFTASKLRWVQENEPELYRRIKHFML 159
Cdd:cd07805 77 GQMQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPpsGKDPLAKILWLKENEPEIYAKTHKFLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 160 PGDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVAYR 239
Cdd:cd07805 157 AKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 240 AGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFAHVNYTLEHPsIGVLMCingAGITYSWLRQNMG 319
Cdd:cd07805 237 GGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASADPGRYLL-AAEQET---AGGALEWARDNLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 320 AAGV----SYPELEERAAQVPIGADGLSILP--FGnsaER-ILNNVDLGAQIQGLNfNRHGQAHLIRAGLEGIAFAFVYG 392
Cdd:cd07805 313 GDEDlgadDYELLDELAAEAPPGSNGLLFLPwlNG---ERsPVEDPNARGAFIGLS-LEHTRADLARAVLEGVAFNLRWL 388
|
410
....*....|....*.
gi 503531638 393 MSILQEMGLDLKVMRV 408
Cdd:cd07805 389 LEALEKLTRKIDELRL 404
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
2-408 |
2.66e-78 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 249.79 E-value: 2.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAESgkTLVRTQYpdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDG--NLVASAS--REYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAvdigaaaferigqqkalahllnspgnftasklrwvqenepelyrrikHFMLPG 161
Cdd:cd00366 77 GQMPGVVLVDADGNPLRPAIIWLDRRA-----------------------------------------------KFLQPN 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 162 DYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVAYRAG 241
Cdd:cd00366 110 DYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 242 DQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPlSRVNGFAHV--NYTLehpsigVLMCINGAGITYSWLRQNMG 319
Cdd:cd00366 190 DTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPD-PRLLNRCHVvpGLWL------LEGAINTGGASLRWFRDEFG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 320 AAG---VSYPELEERAAQVPIGADGLSILPFGNSAERILNNVDLGAQIQGLNFNrHGQAHLIRAGLEGIAFAFVYGMSIL 396
Cdd:cd00366 263 EEEdsdAEYEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLS-HTRAHLIRAVLEGVAYALRDNLEIL 341
|
410
....*....|..
gi 503531638 397 QEMGLDLKVMRV 408
Cdd:cd00366 342 EELGVKIKEIRV 353
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
2-424 |
1.63e-70 |
|
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: 232.06 E-value: 1.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAEsGKTL--VRTQYPdremdMQAPRAGWAEQHPDQWWEGIVQATQRLLKShsFNPQSVKAIG 79
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDED-GRVVasSSAEYP-----LIRPEPGWAEQDPEEILEAVLEALKEVLAK--LGGGEVDAIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 80 ISYQMHGLVLVDAADQVLRPSIIWCDGRAvdigAAAFERIGQQKALAHLLNSPG-----NFTASKLRWVQENEPELYRRI 154
Cdd:cd07770 73 FSSAMHSLLGVDEDGEPLTPVITWADTRA----AEEAERLRKEGDGSELYRRTGcpihpMYPLAKLLWLKEERPELFAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 155 KHFMLPGDYIALKMTGETC---STISGLseGIF------WDfleqkpADLVfqDY-GIDPALMPALQPTFGIQGALRAEA 224
Cdd:cd07770 149 AKFVSIKEYLLYRLTGELVtdySTASGT--GLLnihtldWD------EEAL--ELlGIDEEQLPELVDPTEVLPGLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 225 AAELGLVAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVngFAHVnYTLEHPSIGvlMCI 304
Cdd:cd07770 219 AERLGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGTSGAIRVVSDRPVLDPPGRL--WCYR-LDENRWLVG--GAI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 305 NGAGITYSWLRQNMGAAGVSYPELEERAAQVPIGADGLSILPF--GnsaERILN-NVDLGAQIQGLNFNrHGQAHLIRAG 381
Cdd:cd07770 294 NNGGNVLDWLRDTLLLSGDDYEELDKLAEAVPPGSHGLIFLPYlaG---ERAPGwNPDARGAFFGLTLN-HTRADILRAV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 503531638 382 LEGIAFAFVYGMSILQEMGLDLKVMRVGNdNLFQSRIFAETIA 424
Cdd:cd07770 370 LEGVAFNLKSIYEALEELAGPVKEIRASG-GFLRSPLWLQILA 411
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
2-437 |
1.02e-66 |
|
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: 221.27 E-value: 1.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFD-LDGREIAVAS---RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAVDI---------GAAAFERIGQqkalaHLLnsPGNfTASKLRWVQENEPELYR 152
Cdd:cd07802 77 GHGNGLYLVDKDGKPVRNAILSNDSRAADIvdrweedgtLEKVYPLTGQ-----PLW--PGQ-PVALLRWLKENEPERYD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 153 RIKHFMLPGDYIALKMTGETCSTISGLSEGiFWDFLEQKPADLVFQDYGIDPA--LMPALQPTFGIQGALRAEAAAELGL 230
Cdd:cd07802 149 RIRTVLFCKDWIRYRLTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGIEELkdKLPPLVPSTEIAGRVTAEAAALTGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 231 VAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNG-FAHVNYTLEHPSIGvlmciNGAGi 309
Cdd:cd07802 228 PEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSlHADPGLYLIVEASP-----TSAS- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 310 TYSWLRQNMGAA-----GVSYPELEERAAQVPIGADGLSILPF--GNSAerilnNVDLGAQIQGLNfNRHGQAHLIRAGL 382
Cdd:cd07802 302 NLDWFLDTLLGEekeagGSDYDELDELIAAVPPGSSGVIFLPYlyGSGA-----NPNARGGFFGLT-AWHTRAHLLRAVY 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 383 EGIAFAFVYGMSilqemglDLKVMRVGNDNLF-----QSRIFAETIATLCNSHIEMLDTT 437
Cdd:cd07802 376 EGIAFSHRDHLE-------RLLVARKPETIRLtgggaRSPVWAQIFADVLGLPVEVPDGE 428
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
2-408 |
1.64e-64 |
|
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: 215.53 E-value: 1.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKtLVRTQYpdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHsfNPQSVKAIGIS 81
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFD-EDGR-ILASAS--RETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA--GPDPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQK--ALAHLLNSPgNFTASKLRWVQENEPELYRRIKHFML 159
Cdd:cd07773 75 SQGESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEElyRITGLPPSP-MYSLAKLLWLREHEPEIFAKAAKWLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 160 PGDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVAyr 239
Cdd:cd07773 154 VADYIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVV-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 240 AG--DQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFahvnyTLEHPSIGVLMCING---AGITYSWL 314
Cdd:cd07773 232 VGghDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGL-----SYGHHVPGGYYYLAGslpGGALLEWF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 315 RQNMGAAGVSYPELEERAAQVPIGADGLSILPFGNSAERILNNVDLGAQIQGLNFNrHGQAHLIRAGLEGIAFAFVYGMS 394
Cdd:cd07773 307 RDLFGGDESDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLG-TTRADLLRAILEGLAFELRLNLE 385
|
410
....*....|....
gi 503531638 395 ILQEMGLDLKVMRV 408
Cdd:cd07773 386 ALEKAGIPIDEIRA 399
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
2-428 |
6.73e-64 |
|
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: 213.53 E-value: 6.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAEsGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLD-GNIVASGY---REYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAvdigaaaferigqqkalahllnspgnftasklrwvqenepelyrriKHFMLPG 161
Cdd:cd07779 77 SQRSTFVPVDEDGRPLRPAISWQDKRT----------------------------------------------AKFLTVQ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 162 DYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVAYRAG 241
Cdd:cd07779 111 DYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 242 DQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFAHV---NYTLEhpsigvlMCINGAGITYSWLRQNM 318
Cdd:cd07779 191 DQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAvpgKWVLE-------GSINTGGSAVRWFRDEF 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 319 GAAGV--------SYPELEERAAQVPIGADGLSILPFGNSAERILNNVDLGAQIQGLNFnRHGQAHLIRAGLEGIAFAFV 390
Cdd:cd07779 264 GQDEVaekelgvsPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTL-SHTRAHLARAILEGIAFELR 342
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 503531638 391 YGMSILQEMGLDLKVMRV--GndnLFQSRIFAETIATLCN 428
Cdd:cd07779 343 DNLEAMEKAGVPIEEIRVsgG---GSKSDLWNQIIADVFG 379
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
1-401 |
2.97e-63 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 213.29 E-value: 2.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 1 MYlIGYDIGSSSVKAALVDaESGKTLVrTQypDREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFnpQSVKAIGI 80
Cdd:PRK15027 1 MY-IGIDLGTSGVKVILLN-EQGEVVA-SQ--TEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 81 SYQMHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQKALAHLLNSPGnFTASKLRWVQENEPELYRRIKHFMLP 160
Cdd:PRK15027 74 AGQMHGATLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPG-FTAPKLLWVQRHEPEIFRQIDKVLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 161 GDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAgIPVAYRA 240
Cdd:PRK15027 153 KDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 241 GDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFAHVnytleHPSIGVLMCIN-GAGITYSWLRQNMG 319
Cdd:PRK15027 232 GDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHA-----LPQRWHLMSVMlSAASCLDWAAKLTG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 320 AAGVsyPELEERAAQVPIGADGLSILPFgNSAERILNNvdlGAQIQGLNF---NRHGQAHLIRAGLEGIAFAFVYGMSIL 396
Cdd:PRK15027 307 LSNV--PALIAAAQQADESAEPVWFLPY-LSGERTPHN---NPQAKGVFFgltHQHGPNELARAVLEGVGYALADGMDVV 380
|
....*
gi 503531638 397 QEMGL 401
Cdd:PRK15027 381 HACGI 385
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
2-387 |
4.10e-54 |
|
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: 189.28 E-value: 4.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAESGKTLVR--TQYPDREMDmqaPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIG 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLADGEELASavVPYPTGYIP---PRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 80 ISYQMHGLVLVDAADQVLRPSIIWCDGRAVDiGAAAFERIGQQKALAHLLNSPGNFTA----SKLRWVQENEPELYRRIK 155
Cdd:cd07781 78 VDTTSSTVVPVDEDGNPLAPAILWMDHRAQE-EAAEINETAHPALEYYLAYYGGVYSSewmwPKALWLKRNAPEVYDAAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 156 HFMLPGDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDygIDPAL------MPA-LQPTFGIQGALRAEAAAEL 228
Cdd:cd07781 157 TIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAA--LDPGLlklrekLPGeVVPVGEPAGTLTAEAAERL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 229 GLVAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDP--LSRVNGFAHVN-YTLEhpsigvlmcin 305
Cdd:cd07781 235 GLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDIPgiCGPVPDAVVPGlYGLE----------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 306 gAGIT-----YSWLRQNMG-----AAGVSYPELEERAAQVPIGADGLSILPF--GNsaeR-ILNNVDLGAQIQGLNFNrH 372
Cdd:cd07781 304 -AGQSavgdiFAWFVRLFVppaeeRGDSIYALLSEEAAKLPPGESGLVALDWfnGN---RtPLVDPRLRGAIVGLTLG-T 378
|
410
....*....|....*
gi 503531638 373 GQAHLIRAGLEGIAF 387
Cdd:cd07781 379 TPAHIYRALLEATAF 393
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
2-243 |
6.73e-54 |
|
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: 181.38 E-value: 6.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQ---LENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQK--ALAHLLNSPGnFTASKLRWVQENEPELYRRIKHFML 159
Cdd:pfam00370 77 NQGHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKlyEITGLPIWPG-FTLSKLRWIKENEPEVFEKIHKFLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 160 PGDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVAYR 239
Cdd:pfam00370 156 IHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGG 235
|
....
gi 503531638 240 AGDQ 243
Cdd:pfam00370 236 GGDQ 239
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
2-428 |
1.12e-52 |
|
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: 184.35 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAEsGKTLVRTQypdREMDMQAP-RAGWA-EQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIG 79
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSE-GKIVAIAY---REWEYYTDdDYPDAkEFDPEELWEKICEAIREALKKAGISPEDISAVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 80 ISYQMHGLVLVDAADQVLR--PSIiwcDGRAVDIGAAAFERIGQQKALAHLLNSPGNFTASKLRWVQENEPELYRRIKHF 157
Cdd:cd07798 77 STSQREGIVFLDKDGRELYagPNI---DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAARLLWFKENRPEIFERIATV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 158 MLPGDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAGIPVA 237
Cdd:cd07798 154 LSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 238 YRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVNGFAHV---NYTLEhPSIGVlmcingAGITYSWL 314
Cdd:cd07798 234 VGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLvpgKWVLE-SNAGV------TGLNYQWL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 315 RQNM-GAAGVSYPELEERAAQVPIGADG----LSILPFgnsaerilnNVDLGAQIQG-------LNFNRHGQAHLIRAGL 382
Cdd:cd07798 307 KELLyGDPEDSYEVLEEEASEIPPGANGvlafLGPQIF---------DARLSGLKNGgflfptpLSASELTRGDFARAIL 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 503531638 383 EGIAFAFVYGMSILQEM-GLDLKVMRVGNdNLFQSRIFAETIATLCN 428
Cdd:cd07798 378 ENIAFAIRANLEQLEEVsGREIPYIILCG-GGSRSALLCQILADVLG 423
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
2-400 |
6.66e-52 |
|
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: 181.65 E-value: 6.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTL--VRTQYPdremdMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPqsVKAIG 79
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVD-EDGTVLasASEPYP-----TSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRR--VVAIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 80 ISYQMHGLVLVDAADQVLRPSIIWCDGRAVDIGAAAFERIGQQKALAHLLNSPgNFTASKLRWVQENEPELYRRIKHFML 159
Cdd:cd07783 73 VDGTSGTLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSP-SSSLAKLLWLKRHEPEVLAKTAKFLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 160 PGDYIALKMTG------ETCSTISGlsegifWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLVAG 233
Cdd:cd07783 152 QADWLAGRLTGdrgvtdYNNALKLG------YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 234 IPVAyrAG--DQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSRVngfahvnYTleHPSIGVLMCINGAGity 311
Cdd:cd07783 226 TPVV--AGttDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGGGV-------YS--HRHGDGYWLVGGAS--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 312 swlrqNMGAA-------GVSYPELEERAAqvPIGADGLSILPFGNSAERI-LNNVDLGAQIQGLNfnrHGQAHLIRAGLE 383
Cdd:cd07783 292 -----NTGGAvlrwffsDDELAELSAQAD--PPGPSGLIYYPLPLRGERFpFWDPDARGFLLPRP---HDRAEFLRALLE 361
|
410
....*....|....*..
gi 503531638 384 GIAFAFVYGMSILQEMG 400
Cdd:cd07783 362 GIAFIERLGYERLEELG 378
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
2-388 |
2.85e-45 |
|
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: 164.33 E-value: 2.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFD-LDGRELAVAA---RRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQVLRPSIIWCDGRAVD---------IGAAAFERIGQqkalahLLNsPGNFtASKLRWVQENEPELYR 152
Cdd:cd24121 77 GQGDGTWLVDEDGRPVRDAILWLDGRAADiverwqadgIAEAVFEITGT------GLF-PGSQ-AAQLAWLKENEPERLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 153 RIKHFMLPGDYIALKMTGETCSTISGLSEgIFWDFLEQKPADLVFQDYGIDP--ALMPALQPTFGIQGALRAEAAAELGL 230
Cdd:cd24121 149 RARTALHCKDWLFYKLTGEIATDPSDASL-TFLDFRTRQYDDEVLDLLGLEElrHLLPPIRPGTEVIGPLTPEAAAATGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 231 VAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDPLSrvngfahVNYTLEHPSIGV---LMCINGA 307
Cdd:cd24121 228 PAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEG-------VGYTICLGVPGRwlrAMANMAG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 308 GITYSWLRQNMGAAGVS---------YPELEERAAQVPIGADGLSILPFGNSA-ERI-LNNVDLGAQIQGLNFNrHGQAH 376
Cdd:cd24121 301 TPNLDWFLRELGEVLKEgaepagsdlFQDLEELAASSPPGAEGVLYHPYLSPAgERApFVNPNARAQFTGLSLE-HTRAD 379
|
410
....*....|..
gi 503531638 377 LIRAGLEGIAFA 388
Cdd:cd24121 380 LLRAVYEGVALA 391
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
2-418 |
4.60e-23 |
|
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: 101.77 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07769 1 YILAIDQGTTSTRAILFD-EDGNIVASAQ---KEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAAD-QVLRPSIIWCDGRAVDI----GAAAFERIGQQKAlaHLLNSPgNFTASKLRWVQENEPELYRRIKH 156
Cdd:cd07769 77 NQRETTVVWDKKTgKPLYNAIVWQDRRTADIceelKAKGLEERIREKT--GLPLDP-YFSATKIKWILDNVPGARERAER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 157 fmlpGD--------YIALKMT-GETCST------------ISGLSegifWDfleqkpaDLVFQDYGIDPALMPALQPTFG 215
Cdd:cd07769 154 ----GEllfgtidtWLIWKLTgGKVHVTdvtnasrtmlfnIHTLE----WD-------DELLELFGIPRSMLPEVRPSSE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 216 IQGALRAEaaaelGLVAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAIT-DQAVYDPlsrvNGF-------- 286
Cdd:cd07769 219 VFGYTDPE-----GLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTgEKPVPSK----NGLlttiawqi 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 287 -AHVNYTLEHpSIGvlmcINGAGITysWLRQNMGAAGvSYPELEERAAQVPiGADGLSILP-FgnsaerilnnVDLGA-- 362
Cdd:cd07769 290 gGKVTYALEG-SIF----IAGAAIQ--WLRDNLGLIE-DAAETEELARSVE-DNGGVYFVPaF----------SGLGApy 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503531638 363 -------QIQGLNFNrHGQAHLIRAGLEGIAFaFVYgmSILQEM----GLDLKVMRVG-----NDNL--FQSRI 418
Cdd:cd07769 351 wdpdargAIVGLTRG-TTKAHIVRAALESIAY-QTR--DVLEAMekdsGIKLKELRVDggataNNFLmqFQADI 420
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
2-342 |
2.33e-21 |
|
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: 96.63 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVD------AESGKTLVRTQYPDRE--MDMQAPRAgwaeqhpdqwWEGIVQATQRLLKSHSFNPQ 73
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDlegnqiAVAQREWRHKEVPDVPgsMDFDTEKN----------WKLICECIREALKKAGIAPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 74 SVKAIGISYQMHGLVLVDAADQVlrpsiIW-C---DGRAVD-----------IGAAAFERIGQQKALAHLlnspgnftaS 138
Cdd:cd07775 71 SIAAISTTSMREGIVLYDNEGEE-----IWaCanvDARAAEevselkelyntLEEEVYRISGQTFALGAI---------P 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 139 KLRWVQENEPELYRRIKHFMLPGDYIALKMTGETCSTIS-GLSEGIF------WDfleqkpaDLVFQDYGIDPALMPALQ 211
Cdd:cd07775 137 RLLWLKNNRPEIYRKAAKITMLSDWIAYKLSGELAVEPSnGSTTGLFdlktrdWD-------PEILEMAGLKADILPPVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 212 PTFGIQGALRAEAAAELGLVAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQAVYDP--LSRVNgfAHV 289
Cdd:cd07775 210 ESGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPamNIRVN--CHV 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503531638 290 NYTL-EHPSIGVLmcingAGITYSWLRQNMGA--------AGVS-YPELEERAAQVPIGADGL 342
Cdd:cd07775 288 IPDMwQAEGISFF-----PGLVMRWFRDAFCAeekeiaerLGIDaYDLLEEMAKDVPPGSYGI 345
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
2-435 |
2.39e-21 |
|
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: 96.14 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAESGKTLVRTQYPDREmDMQAPRAGWAEQHPdqwwEGIVQATQRLLKS-HSFNPQSVKAIGI 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVSRPTPA-PISSDDPGRSEQDP----EKILEAVRNLIDElPREYLSDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 81 SYQMHGLVLVDAADQVLRPSIIWCDGRA--------VDIGAAAFERIGQQkaLAhllnsPGnFTASKLRWVQENEPELYR 152
Cdd:cd07777 76 TGQMHGIVLWDEDGNPVSPLITWQDQRCseeflgglSTYGEELLPKSGMR--LK-----PG-YGLATLFWLLRNGPLPSK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 153 RiKHFMLPGDYIALKMTGET---CSTISGLSEGiFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEaaaelg 229
Cdd:cd07777 148 A-DRAGTIGDYIVARLTGLPkpvMHPTNAASWG-LFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSA------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 230 LVAGIPVaYRA-GDQ----------PNNALSLNVldpgevaatgGTSGVVYAITDQAVYDPLSRVNGFAHVNYtlehpsI 298
Cdd:cd07777 220 LPKGIPV-YVAlGDNqasvlgsglnEENDAVLNI----------GTGAQLSFLTPKFELSGSVEIRPFFDGRY------L 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 299 GVLMCINGaGITYSWL----RQNMGAAGVSYPELE-----ERAAQvPIGADGLSILP--FGnsaERIlnNVDLGAQIQGL 367
Cdd:cd07777 283 LVAASLPG-GRALAVLvdflREWLRELGGSLSDDEiweklDELAE-SEESSDLSVDPtfFG---ERH--DPEGRGSITNI 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503531638 368 ---NFNrhgqahliragLEGIAFAFVYGM-----SILQEMGLDLKVMR--VGNDNLFQ-SRIFAETIATLCNSHIEMLD 435
Cdd:cd07777 356 gesNFT-----------LGNLFRALCRGIaenlhEMLPRLDLDLSGIEriVGSGGALRkNPVLRRIIEKRFGLPVVLSE 423
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
2-432 |
4.13e-21 |
|
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: 96.09 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKtlVRTQYPDREMDMQaPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07793 1 YILAVDVGTTNIRCHIFD-KKGK--IIGSSSEKVEVLY-PEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDA-ADQVLRPSIIWCDGRAVDI--------------GAAA----FERIGQQKALAHLLNSPGnFTASKLRW 142
Cdd:cd07793 77 TQRNTFLTWDKkTGKPLHNFITWQDLRAAELceswnrslllkalrGGSKflhfLTRNKRFLAASVLKFSTA-HVSIRLLW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 143 VQENEPELYRRIKHfmlpGD--------YIALKMTGE-------TCSTISGLsegifWDFLEQKPADLVFQDYGIDPALM 207
Cdd:cd07793 156 ILQNNPELKEAAEK----GEllfgtidtWLLWKLTGGkvhatdySNASATGL-----FDPFTLEWSPILLSLFGIPSSIL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 208 PALQPTFGIQGalraeAAAELGLVAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGTSGVV--------YAiTDQAVYdP 279
Cdd:cd07793 227 PEVKDTSGDFG-----STDPSIFGAEIPITAVVADQQAALFGECCFDKGDVKITMGTGTFIdintgskpHA-SVKGLY-P 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 280 LS--RVNGfaHVNYTLEhpsiGVlmcINGAGITYSWLRQNMGAAGVSypELEERAAQVPIgADGLSILPFGNSAERILNN 357
Cdd:cd07793 300 LVgwKIGG--EITYLAE----GN---ASDTGTVIDWAKSIGLFDDPS--ETEDIAESVED-TNGVYFVPAFSGLQAPYND 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 358 VDLGAQIQGLNFNRHgQAHLIRAGLEGIAFAF--VYGMsILQEMGLDLKVMRV-G----NDNLFQsrifaeTIATLCNSH 430
Cdd:cd07793 368 PTACAGFIGLTPSTT-KAHLVRAILESIAFRVkqLLET-MEKETSIKISSIRVdGgvsnNDFILQ------LIADLLGKP 439
|
..
gi 503531638 431 IE 432
Cdd:cd07793 440 VE 441
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
2-418 |
1.28e-20 |
|
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: 94.48 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAEsGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHD-GNIVAVAQ---REFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAAD-QVLRPSIIWCDGRAVDI----GAAAFERIGQQKAlaHLLNSPgNFTASKLRWVQENEPELYRRIKh 156
Cdd:cd07786 77 NQRETTVVWDRETgKPVYNAIVWQDRRTADIceelKAEGHEEMIREKT--GLVLDP-YFSATKIRWILDNVPGARERAE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 157 fmlPGD--------YIALKMTGETC-ST------------ISGLSegifWD--FLEQkpadlvfqdYGIDPALMPALQPT 213
Cdd:cd07786 153 ---RGElafgtidsWLIWKLTGGKVhATdvtnasrtmlfnIHTLE----WDdeLLEL---------FGIPASMLPEVKPS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 214 FGIQGALRAEaaaelGLVAGIPVAYRAGDQpNNAL-SLNVLDPGEVAATGGTSGVVYAIT-DQAVYDP---LS----RVN 284
Cdd:cd07786 217 SEVFGYTDPD-----LLGAEIPIAGIAGDQ-QAALfGQACFEPGMAKNTYGTGCFMLMNTgEKPVRSKnglLTtiawQLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 285 GfaHVNYTLEhpsiGVLMcINGAGItySWLRQNMGAAGVSyPELEERAAQVPiGADGLSILP-FgnsaerilnnVDLGA- 362
Cdd:cd07786 291 G--KVTYALE----GSIF-IAGAAV--QWLRDGLGLIESA-AETEALARSVP-DNGGVYFVPaF----------TGLGAp 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503531638 363 --------QIQGLNFNRhGQAHLIRAGLEGIAFAFVygmSILQEM----GLDLKVMRV-----GNDNL--FQSRI 418
Cdd:cd07786 350 ywdpdargAIFGLTRGT-TRAHIARAALESIAYQTR---DLLEAMeadsGIPLKELRVdggasANDFLmqFQADI 420
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
2-418 |
2.27e-19 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 90.89 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:COG0554 4 YILAIDQGTTSTRAILFD-RDGNIVAVAQ---REFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAAD-QVLRPSIIWCDGRAVDIgAAAFERIGQQKALAH---LLNSPgNFTASKLRWVQENEPELYRRIKHf 157
Cdd:COG0554 80 NQRETTVVWDRKTgKPLYNAIVWQDRRTADI-CEELKADGLEDLIREktgLVLDP-YFSATKIKWILDNVPGARERAEA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 158 mlpGD--------YIALKMTG-------------------ETCStisglsegifWDfleqkpADLVfQDYGIDPALMPAL 210
Cdd:COG0554 157 ---GEllfgtidsWLIWKLTGgkvhvtdvtnasrtmlfniHTLD----------WD------DELL-ELFGIPRSMLPEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 211 QPTFGIQGalraeAAAELGLVAGIPVAYRAGDQpNNALslnV----LDPGEVAATGGTSGVVYAIT-DQAVYDP---LS- 281
Cdd:COG0554 217 RPSSEVFG-----ETDPDLFGAEIPIAGIAGDQ-QAAL---FgqacFEPGMAKNTYGTGCFLLMNTgDEPVRSKnglLTt 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 282 ---RVNGfaHVNYTLEhpsiG-VLMCinGAGITysWLRQNMGAAGvSYPELEERAAQVPiGADGLSILP-Fgnsaeriln 356
Cdd:COG0554 288 iawGLGG--KVTYALE----GsIFVA--GAAVQ--WLRDGLGLID-SAAESEALARSVE-DNGGVYFVPaF--------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 357 nVDLGAQ---------IQGLNFNrHGQAHLIRAGLEGIAFafvYGMSILQEM----GLDLKVMRV-----GNDNL--FQS 416
Cdd:COG0554 347 -TGLGAPywdpdargaIFGLTRG-TTRAHIARAALESIAY---QTRDVLDAMeadsGIPLKELRVdggasANDLLmqFQA 421
|
..
gi 503531638 417 RI 418
Cdd:COG0554 422 DI 423
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
7-437 |
4.58e-19 |
|
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: 89.89 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 7 DIGSSSVKAALVDaESGKTLVRTQYpdrEMDMQAPRAGWAEQHPDQWWEGI---VQATQRLLKSHSFNPQSVKAIGISYQ 83
Cdd:cd07792 7 DQGTTSTRFIVFD-STGELVASHQV---EHKQIYPKPGWVEHDPMEILESVyecIEEAVEKLKALGISPSDIKAIGITNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 84 MHGLVLVDAA-DQVLRPSIIWCDGRAVDIGAAAFERIGQQK-ALAHLLNSPGN--FTASKLRWVQENEPElyrrIKHFML 159
Cdd:cd07792 83 RETTVVWDKStGKPLYNAIVWLDTRTSDTVEELSAKTPGGKdHFRKKTGLPIStyFSAVKLRWLLDNVPE----VKKAVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 160 PGD--------YIALKMTGetcstisGLSEGIF-------------------WDfleqkpaDLVFQDYGIDPALMPALQP 212
Cdd:cd07792 159 DGRllfgtvdsWLIWNLTG-------GKNGGVHvtdvtnasrtmlmnlrtlqWD-------PELCEFFGIPMSILPEIRS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 213 TFGIQGalraeaAAELGLVAGIPVAYRAGDQpNNALslnV----LDPGEVAATGGTsGV--VYAITDQAVYDP---LSRV 283
Cdd:cd07792 225 SSEVYG------KIASGPLAGVPISGCLGDQ-QAAL---VgqgcFKPGEAKNTYGT-GCflLYNTGEEPVFSKhglLTTV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 284 nGF-----AHVNYTLEHpSIGvlmcINGAGItySWLRQNMGAAGvSYPELEERAAQVPiGADGLSILP-FG--------N 349
Cdd:cd07792 294 -AYklgpdAPPVYALEG-SIA----IAGAAV--QWLRDNLGIIS-SASEVETLAASVP-DTGGVYFVPaFSglfapywrP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 350 SAERIlnnvdlgaqIQGLNF--NRhgqAHLIRAGLEGIAF---AFVYGMSilQEMGLDLKVMRV--GndnLFQSRIFAET 422
Cdd:cd07792 364 DARGT---------IVGLTQftTK---AHIARAALEAVCFqtrEILDAMN--KDSGIPLTSLRVdgG---MTKNNLLMQI 426
|
490
....*....|....*...
gi 503531638 423 IATLCNSHIE---MLDTT 437
Cdd:cd07792 427 QADILGIPVErpsMVETT 444
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
2-437 |
2.34e-18 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 87.72 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQYPDREMdmqAPRAGWAEQHPDQWWEGIVQATQRLLK-SHSFNPQ-SVKAIG 79
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFD-EKGNVVSSHQIPHEQI---TPHPGWLEHDPEEILRNVYKCMNEAIKkLREKGPSfKIKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 80 ISYQMHGLVLVDAA-DQVLRPSIIWCDGRAVDIGAAAFERIGQQKALAHLLNSPGN--FTASKLRWVQENEPELYRRIKH 156
Cdd:PTZ00294 79 ITNQRETVVAWDKVtGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQKITGLPIStyFSAFKIRWMLENVPAVKDAVKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 157 ----FMLPGDYIALKMTGETC--STISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPT---FGIqgalraEAAAE 227
Cdd:PTZ00294 159 gtllFGTIDTWLIWNLTGGKShvTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSsenFGT------ISGEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 228 LGLVAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGTSG-VVYAITDQAVYDP---LSRV----NGFAHVNYTLEhPSIG 299
Cdd:PTZ00294 233 VPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCfLLMNTGTEIVFSKhglLTTVcyqlGPNGPTVYALE-GSIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 300 VlmcingAGITYSWLRQNMGAAGvSYPELEERAAQVPiGADGLSILP-F-GNSAERILNnvDLGAQIQGLNFNRhGQAHL 377
Cdd:PTZ00294 312 V------AGAGVEWLRDNMGLIS-HPSEIEKLARSVK-DTGGVVFVPaFsGLFAPYWRP--DARGTIVGMTLKT-TRAHI 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503531638 378 IRAGLEGIAF---AFVYGMSilQEMGLDLKVMRVgNDNLFQSRIFAETIATLCNSHI---EMLDTT 437
Cdd:PTZ00294 381 VRAALEAIALqtnDVIESME--KDAGIELNSLRV-DGGLTKNKLLMQFQADILGKDIvvpEMAETT 443
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
2-346 |
2.56e-16 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 81.59 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDaESGKTLVRTQypdREMDMQA-PR-AGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIG 79
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFD-LNGNQIAVGQ---AEWRHLAvPDvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 80 ISYQMHGLVLVDAADQVlrpsiIW-C---DGRAV-----------DIGAAAFERIGQQKALAHLlnspgnftaSKLRWVQ 144
Cdd:PRK10939 80 ATSMREGIVLYDRNGTE-----IWaCanvDARASrevselkelhnNFEEEVYRCSGQTLALGAL---------PRLLWLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 145 ENEPELYRRIKHFMLPGDYIALKMTGETCSTIS-GLSEGIFwDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAE 223
Cdd:PRK10939 146 HHRPDIYRQAHTITMISDWIAYMLSGELAVDPSnAGTTGLL-DLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 224 AAAELGLVAGIPVAYRAGDQPNNALSLNVLDPGEVAATGGT--SGVVYaiTDQAVYDPLS--RVNgfAHVnytlehpsig 299
Cdd:PRK10939 225 AAAETGLRAGTPVVMGGGDVQLGCLGLGVVRPGQTAVLGGTfwQQVVN--LPAPVTDPNMniRIN--PHV---------- 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503531638 300 vlmcING----------AGITYSWLRQNMGA--------AGVS-YPELEERAAQVPIGADGlsILP 346
Cdd:PRK10939 291 ----IPGmvqaesisffTGLTMRWFRDAFCAeekllaerLGIDaYSLLEEMASRVPVGSHG--IIP 350
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
2-279 |
1.95e-15 |
|
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: 78.73 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAEsGKTLVRTQYPDRemdMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGI- 80
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLD-GRLLATASQPIT---TWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 81 ---SyqmhgLVLVDAADQVLRPS---------IIWCDGRAVDigaAAfERIGQQKAlaHLLNSPGNfTAS------KLRW 142
Cdd:cd07782 77 atcS-----LVVLDAEGKPVSVSpsgddernvILWMDHRAVE---EA-ERINATGH--EVLKYVGG-KISpemeppKLLW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 143 VQENEPELYRRIKHFM-LPgDYIALKMTGET----CST--------ISGLSEGifWD--FLEQ-KPADLVFQDYG-IDPA 205
Cdd:cd07782 145 LKENLPETWAKAGHFFdLP-DFLTWKATGSLtrslCSLvckwtylaHEGSEGG--WDddFFKEiGLEDLVEDNFAkIGSV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 206 LMPALQPtfgIQGALRAEAAAELGLVAGIPV------AY---------RAGDQPNNALSLnvldPGEVAATGGTSGVVYA 270
Cdd:cd07782 222 VLPPGEP---VGGGLTAEAAKELGLPEGTPVgvslidAHagglgtlgaDVGGLPCEADPL----TRRLALICGTSSCHMA 294
|
....*....
gi 503531638 271 ITDQAVYDP 279
Cdd:cd07782 295 VSPEPVFVP 303
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
2-387 |
3.57e-15 |
|
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: 78.05 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAESGKTLVRTQYPDREMdmQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYAGLEMAQEPVPYYQD--SSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMhGLVLVDAADQVLRPS---------IIWCDGRAVDigaaAFERIGQQKALAHLLNSPGNFTA----SKLRWVQENEP 148
Cdd:cd07768 79 ATC-SLAIFDREGTPLMALipypnednvIFWMDHSAVN----EAQWINMQCPQQLLDYLGGKISPemgvPKLKYFLDEYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 149 ELYRRIKHFMLPGDYIALKMTGETCSTISGLSEGIFWDFLEQKPADLVFQDygIDPALM--------PALQPTFGIQGAL 220
Cdd:cd07768 154 HLRDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKN--IDPRLEhltttknlPSNVPIGTTSGVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 221 RAEAAAELGLVAGIPVAYRAGDQPNNALSLNVLD-PGEVAATGGTSGVVYAITDQAvydplSRVNGFAHVNYTLEHPSIG 299
Cdd:cd07768 232 LPEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHlETSLFMIAGTSSCHMYGTTIS-----DRIPGVWGPFDTIIDPDYS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 300 VLMCINGA-GITYSWLRQNMGAA---------GVS-YPELEERAAQV---PIGADGLSILPFGNSAERILNNVDLGAQIQ 365
Cdd:cd07768 307 VYEAGQSAtGKLIEHLFESHPCArkfdealkkGADiYQVLEQTIRQIeknNGLSIHILTLDMFFGNRSEFADPRLKGSFI 386
|
410 420
....*....|....*....|....
gi 503531638 366 GLNFNRHGQ--AHLIRAGLEGIAF 387
Cdd:cd07768 387 GESLDTSMLnlTYKYIAILEALAF 410
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-400 |
5.91e-14 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 73.91 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 1 MYLIGYDIGSSSVKAALVDAEsGKTLVRTQYPDR-EMDMQAPRagWAEQHPDQWWEGIVQATQRLLKShsFNPQSVKAIG 79
Cdd:PRK10331 2 DVILVLDCGATNVRAIAVDRQ-GKIVARASTPNAsDIAAENSD--WHQWSLDAILQRFADCCRQINSE--LTECHIRGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 80 IS-YQMHGlVLVDAADQVLRPSIIWCDGRAvdigAAAFERIGQQKALAHL--LNSPGNF---TASKLRWVQENEPELYRR 153
Cdd:PRK10331 77 VTtFGVDG-ALVDKQGNLLYPIISWKCPRT----AAVMENIERYISAQQLqqISGVGAFsfnTLYKLVWLKENHPQLLEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 154 IKHFMLPGDYIALKMTGE--TCSTISGLSEgiFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAAAELGLV 231
Cdd:PRK10331 152 AHAWLFISSLINHRLTGEftTDITMAGTSQ--MLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 232 AGIPVaYRAGDQPNNALSLNVLDPGEVAATGGTSGVVYAITDQA------VYDPL-----SRVNGFahvNYTLEHPSIGV 300
Cdd:PRK10331 230 VGIPV-ISAGHDTQFALFGSGAGQNQPVLSSGTWEILMVRSAQVdtsllsQYAGStceldSQSGLY---NPGMQWLASGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 301 LmcingagitySWLRQNMGAAGVSYPELEERAAQVPIGADGLSILP-FGNSAErilnnvdlgAQIQGLNFNRhGQAHLIR 379
Cdd:PRK10331 306 L----------EWVRKLFWTAETPYQTMIEEARAIPPGADGVKMQCdLLACQN---------AGWQGVTLNT-TRGHFYR 365
|
410 420
....*....|....*....|.
gi 503531638 380 AGLEGIAFAFVYGMSILQEMG 400
Cdd:PRK10331 366 AALEGLTAQLKRNLQVLEKIG 386
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
2-387 |
6.52e-14 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 74.11 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAESGKTLVR--TQYPDREMDMQAPRAG-WAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAI 78
Cdd:PRK04123 4 YVIGLDFGTDSVRALLVDCATGEELATavVEYPHWVKGRYLDLPPnQALQHPLDYIESLEAAIPAVLKEAGVDPAAVVGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 79 GISYQMHGLVLVDAADQVL--RPS---------IIWCDGRAVDiGAAAFERIGQQKALAHLLNSPGN------FTASKLR 141
Cdd:PRK04123 84 GVDFTGSTPAPVDADGTPLalLPEfaenphamvKLWKDHTAQE-EAEEINRLAHERGEADLSRYIGGiyssewFWAKILH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 142 WVQENePELYRRIKHFMLPGDYIALKMTGETcsTISGLSEGI-------FW----------DFLEqkpadlvfqdyGIDP 204
Cdd:PRK04123 163 VLRED-PAVYEAAASWVEACDWVVALLTGTT--DPQDIVRSRcaaghkaLWheswgglpsaDFFD-----------ALDP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 205 ALMPALQ-----PTFGIQ---GALRAEAAAELGLVAGIPVAYRAGDQPNNALSLNVlDPGEVAATGGTSGVVYAITDQAV 276
Cdd:PRK04123 229 LLARGLRdklftETWTAGepaGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGA-EPGTLVKVMGTSTCDILLADKQR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 277 YDP--LSRVNGFAHVNYT-LEHPSIGVlmcingaGITYSWLRQNMGAA----------GVSYPELEERAAQVPIGADGLS 343
Cdd:PRK04123 308 AVPgiCGQVDGSIVPGLIgYEAGQSAV-------GDIFAWFARLLVPPeykdeaeargKQLLELLTEAAAKQPPGEHGLV 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 503531638 344 ILPFGNSAERILNNVDLGAQIQGLNFnRHGQAHLIRAGLEGIAF 387
Cdd:PRK04123 381 ALDWFNGRRTPLADQRLKGVITGLTL-GTDAPDIYRALIEATAF 423
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-418 |
3.91e-09 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 58.68 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVDAEsGKTLVRTQypdREMDMQAPRAGWAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGIS 81
Cdd:PRK00047 6 YILALDQGTTSSRAIIFDHD-GNIVSVAQ---KEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVLVDAADQvlRP---SIIWCDGRAVDIgAAAFERIGQQ---KALAHLLNSPgNFTASKLRWVQENEPELYRRIK 155
Cdd:PRK00047 82 NQRETTVVWDKETG--RPiynAIVWQDRRTADI-CEELKRDGYEdyiREKTGLVIDP-YFSGTKIKWILDNVEGARERAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 156 HfmlpGDYIA--------LKMTGETC--STISGLSEGIFWDFLEQKPADLVFQDYGIDPALMPALQPTFGIQGALRAEAa 225
Cdd:PRK00047 158 K----GELLFgtidtwlvWKLTGGKVhvTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNPYG- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 226 aelGLVAGIPVAYRAGDQpNNALSLNV-LDPGEVAATGGTSGVVYAIT-DQAVydpLSRvNGF---------AHVNYTLE 294
Cdd:PRK00047 233 ---FFGGEVPIAGIAGDQ-QAALFGQLcFEPGMAKNTYGTGCFMLMNTgEKAV---KSE-NGLlttiawgidGKVVYALE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 295 HpSIGVlmcingAGITYSWLRQNMGAAGVSyPELEERAAQVPiGADGLSILP-FgnsaerilnnVDLGA---------QI 364
Cdd:PRK00047 305 G-SIFV------AGSAIQWLRDGLKIISDA-SDSEALARKVE-DNDGVYVVPaF----------TGLGApywdsdargAI 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503531638 365 QGLN-FNrhGQAHLIRAGLEGIAFA---FVYGMSilQEMGLDLKVMRV-----GNDNL--FQSRI 418
Cdd:PRK00047 366 FGLTrGT--TKEHIIRATLESIAYQtrdVLDAMQ--ADSGIRLKELRVdggavANNFLmqFQADI 426
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
258-428 |
5.51e-08 |
|
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: 53.10 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 258 VAATGGTSGVVYAITDqavyDPLSRVNGFAHvNYTLEH--PSIGVLMCINGAGITYSWLRQNMGAAGV--------SYPE 327
Cdd:pfam02782 1 LAISAGTSSFVLVETP----EPVLSVHGVWG-PYTNEMlpGYWGLEGGQSAAGSLLAWLLQFHGLREElrdagnveSLAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 328 LEERAAQVPigADGLSILPF--GNSAEriLNNVDLGAQIQGLNfNRHGQAHLIRAGLEGIAFAFVYGMSILQEM-GLDLK 404
Cdd:pfam02782 76 LAALAAVAP--AGGLLFYPDfsGNRAP--GADPGARGSITGLS-SPTTLAHLYRAILESLALQLRQILEALTKQeGHPID 150
|
170 180
....*....|....*....|....*.
gi 503531638 405 VMRV--GndnLFQSRIFAETIATLCN 428
Cdd:pfam02782 151 TIHVsgG---GSRNPLLLQLLADALG 173
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
2-428 |
1.32e-07 |
|
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: 53.69 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 2 YLIGYDIGSSSVKAALVdaesgktlvrtQYPDREMDMQapragwaEQH--PDQ---------W-----WEGIVQATQRLL 65
Cdd:cd07771 1 NYLAVDLGASSGRVILG-----------SLDGGKLELE-------EIHrfPNRpveinghlyWdidrlFDEIKEGLKKAA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 66 KSHSfNPQSVkAI---GISYqmhglVLVDAADQVLRPsiIWC--DGRAVDIGAAAFERIGQQKALAH--LLNSPGNfTAS 138
Cdd:cd07771 63 EQGG-DIDSI-GIdtwGVDF-----GLLDKNGELLGN--PVHyrDPRTEGMMEELFEKISKEELYERtgIQFQPIN-TLY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 139 KLRWVQENEPELYRRIKHFMLPGDYIALKMTGETCS--TISGLSEgiFWDFLEQKPADLVFQDYGIDPALMPALQPTFGI 216
Cdd:cd07771 133 QLYALKKEGPELLERADKLLMLPDLLNYLLTGEKVAeyTIASTTQ--LLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 217 QGALRAEAAAELGLvAGIPVAYRAG-----------DQPNNA--LSLnvldpgevaatgGTSGVVYAITDQAVYDPLSRV 283
Cdd:cd07771 211 LGTLKPEVAEELGL-KGIPVIAVAShdtasavaavpAEDEDAafISS------------GTWSLIGVELDEPVITEEAFE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 284 NGF---AHVNYTlehpsigVLMCINGAGItysWL----RQNMGAAGV--SYPELEERAAQVPigadglsilPFGN----S 350
Cdd:cd07771 278 AGFtneGGADGT-------IRLLKNITGL---WLlqecRREWEEEGKdySYDELVALAEEAP---------PFGAfidpD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 351 AERILNNVDLGAQIQGLnFNRHGQ------AHLIRAGLEGIAFAFVYGMSILQEM-GLDLKVMRV---GNdnlfQSRIFA 420
Cdd:cd07771 339 DPRFLNPGDMPEAIRAY-CRETGQpvpespGEIARCIYESLALKYAKTIEELEELtGKRIDRIHIvggGS----RNALLC 413
|
....*...
gi 503531638 421 ETIATLCN 428
Cdd:cd07771 414 QLTADATG 421
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-236 |
4.43e-07 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 52.26 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 7 DIGSSSVKAALVDaESGKTLVRTQYPDREmdmqAPRAGWAEQHPDQWWEGIVQATQRLLKSHSfnpqsVKAIGISyqMHG 86
Cdd:cd07772 6 DIGKTNKKLLLFD-ENGEVLAERSTPNPE----IEEDGYPCEDVEAIWEWLLDSLAELAKRHR-----IDAINFT--THG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 87 --LVLVDAADQVLRP--SIIWcdgravDIG---AAAFERIGQQKALAHLLNSPGNFTASK-LRWVQENEPELYRRIKHFM 158
Cdd:cd07772 74 atFALLDENGELALPvyDYEK------PIPdeiNEAYYAERGPFEETGSPPLPGGLNLGKqLYWLKREKPELFARAKTIL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 159 LPGDYIALKMTGETCSTISGLseGI---FWDFLEQKPADLVfQDYGIDpALMPALQPTFGIQGALRAEAAAELGLVAGIP 235
Cdd:cd07772 148 PLPQYWAWRLTGKAASEITSL--GChtdLWDFEKNEYSSLV-KKEGWD-KLFPPLRKAWEVLGPLRPDLARRTGLPKDIP 223
|
.
gi 503531638 236 V 236
Cdd:cd07772 224 V 224
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-88 |
5.62e-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: 48.35 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 1 MYLIGYDIGSSSVKAALVDaESGKTLVRTQYPDRemdmqapragwAEQHPDQWWEGIVQATQRLLKSHSFNPQSVKAIGI 80
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVD-LDGEVLARERIPTP-----------AGAGPEAVLEAIAELIEELLAEAGISRGRILGIGI 72
|
....*...
gi 503531638 81 SyqMHGLV 88
Cdd:COG1940 73 G--VPGPV 78
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
3-173 |
4.49e-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: 42.78 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 3 LIGYDIGSSSVKAALVDaESGKTLVRTQYP-DREMDMQAPraGWAEQHPDQWWEGIVQATQRLLKshSFNPQSVKAIGIS 81
Cdd:cd07778 2 GIGIDVGSTSVRIGIFD-YHGTLLATSERPiSYKQDPKDL--WFVTQSSTEIWKAIKTALKELIE--ELSDYIVSGIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 82 YQMHGLVL-VDAADQVLRP------------SII-WCDGRAVDIgAAAFERIGQQKALAHLlnsPGNFTAS----KLRWV 143
Cdd:cd07778 77 ATCSMVVMqRDSDTSYLVPynviheksnpdqDIIfWMDHRASEE-TQWLNNILPDDILDYL---GGGFIPEmaipKLKYL 152
|
170 180 190
....*....|....*....|....*....|
gi 503531638 144 QENEPELYRRIKHFMLPGDYIALKMTGETC 173
Cdd:cd07778 153 IDLIKEDTFKKLEVFDLHDWISYMLATNLG 182
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
4-120 |
2.61e-03 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 39.37 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503531638 4 IGYDIGSSSVKAALVDaESGKTLVRTQYPDRemdmqapragwAEQHPDQWWEGIVQATQRLLKSHSFNPQsVKAIGISyq 83
Cdd:cd23763 1 IGIDIGGTKIRAALVD-LDGEILARERVPTP-----------AEEGPEAVLDRIAELIEELLAEAGVRER-ILGIGIG-- 65
|
90 100 110
....*....|....*....|....*....|....*....
gi 503531638 84 MHGlvLVDAADQVLR--PSIIWCDGraVDIGAAAFERIG 120
Cdd:cd23763 66 VPG--PVDPETGIVLfaPNLPWWKN--VPLRELLEERLG 100
|
|
| |
