|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
12-545 |
0e+00 |
|
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: 996.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 89
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 169
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 170 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:cd07782 160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:cd07782 240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 403
Cdd:cd07782 318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 404 TLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 483
Cdd:cd07782 398 TLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEP 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555144 484 ESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVEHQKEY 545
Cdd:cd07782 478 EAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREY 539
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
12-545 |
0e+00 |
|
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.
Pssm-ID: 273552 [Multi-domain] Cd Length: 541 Bit Score: 673.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDATCS 89
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 169
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 170 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 401
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 402 DLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQ 481
Cdd:TIGR01315 396 DPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPY 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555144 482 EVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFP-EHADKKYYDKKYQVFLRMVEHQKEY 545
Cdd:TIGR01315 476 VNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPrGDPAKKLHDRKYEIFLQLARTQQEY 540
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
10-547 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 587.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 10 SRYYVGIDVGTGSVRAALVDQR-GLLLAFAEQPIKKWEP---------QFnhhEQSSEDIWAACCLVTKEVVQ--GIDAH 77
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 78 RIRGLGFDAT-CSLVVLDKEFHPLPVNHE--GDSSRNVIMWLDHRAVSQVHRINE----TKHRVLQYVGGVMSVEMQAPK 150
Cdd:COG1069 78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 151 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIG--LEDLIDdnysKIGN 226
Cdd:COG1069 158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDplLDGLAD----RLGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 227 LVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLAVICGTSSCHMGISKD 306
Cdd:COG1069 233 EIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LVKVMGTSTCHMLVSPE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 307 PVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVD 386
Cdd:COG1069 299 ERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 387 LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLF 465
Cdd:COG1069 373 LHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 466 VQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKV-GKVVFPEHADKKYYDKKYQVFLRMVEHQKE 544
Cdd:COG1069 450 MQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYFGR 529
|
...
gi 167555144 545 YSA 547
Cdd:COG1069 530 GRN 532
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
12-535 |
2.37e-154 |
|
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: 451.69 E-value: 2.37e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE-PQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDAT 87
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNirEGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 88 CSLVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 167 GHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDLiDDNYSKIGNLVLLPGAALGIGLtPEAAR 245
Cdd:cd07768 160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGhgltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:cd07768 238 KMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQaKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTL 405
Cdd:cd07768 306 SVYEAGQSATGKLIEHLFESHPCARKFD-EALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 406 KGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVES 485
Cdd:cd07768 382 KGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 167555144 486 VLVGAAILGACASGDFT---SVQEAMARMSKVGKVVFPE-HADKKYYDKKYQVF 535
Cdd:cd07768 462 GILGAAVLAKVAAGKKQladSITEADISNDRKSETFEPLaYRLGADYILLYKLL 515
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
12-538 |
5.77e-150 |
|
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: 440.05 E-value: 5.77e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--PQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA 86
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAeaGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 87 TCS-LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRV----LQYVGGVMSVEMQAPKLLWLKENLREI 161
Cdd:cd07781 81 TSStVVPVDEDGNPL---------APAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 162 cWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDLidDNYSKIGNLVLLPGAALGiGLT 240
Cdd:cd07781 152 -YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGLL--KLREKLPGEVVPVGEPAG-TLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 241 PEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSA 320
Cdd:cd07781 228 AEAAERLGLPAGIPVAQGGIDAHMG---AIGAGVVEPG----------TLALIMGTSTCHLMVSPKPVDIPGICGPVPDA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 321 MVPGFWLNEGGQSVTGKLIDhmvqghpAFPELQAKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNR 397
Cdd:cd07781 295 VVPGLYGLEAGQSAVGDIFA-------WFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 398 SPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQMHADITGMP 476
Cdd:cd07781 360 TPLVDPRLRGAIVGLTLGTTP---AHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555144 477 VVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRM 538
Cdd:cd07781 437 IKVPKSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
11-544 |
8.87e-103 |
|
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: 318.31 E-value: 8.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 11 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT- 87
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAkaGVDPEEIAAIGVSGQm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 88 CSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 165
Cdd:COG1070 81 HGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 166 AGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGLEDLIddnyskignL--VLLPGAALGiG 238
Cdd:COG1070 151 IAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIDREL---------LpeLVPPGEVAG-T 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 239 LTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYY 318
Cdd:COG1070 217 LTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 319 SAMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKAtarcQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDF 393
Cdd:COG1070 284 CHAVPGRWLPMGATNNGGSALRWFRD------LFADGE----LDDYEELN---ALAAEV-PPGadgllFL-------PYL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 394 HGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADIT 473
Cdd:COG1070 343 SGERTPHWDPNARGAFFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVL 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167555144 474 GMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVEHQKE 544
Cdd:COG1070 420 GRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYPALKP 490
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
13-536 |
7.04e-88 |
|
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: 281.22 E-value: 7.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 13 YVGIDVGTGSVRAALVDQRGLLLAFAEQPI--KKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATCSL 90
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATCSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 91 VVLDKE-----FHPLPVNHE-GDSSRNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICW 163
Cdd:cd07778 82 VVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 164 DKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDLIDDNYSKIGNLVL 229
Cdd:cd07778 162 KKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNVGNTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 230 LPGAALGIG-LTPEAARELGLPSGIAVAASLIDAHAGGLGVIgadvrghgltCEGQPVTSRLAVICGTSSCHMGISKDPV 308
Cdd:cd07778 233 LPYAGIPIGkVNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 309 --FVPGVWGPYySAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATarcqSIYAYLNSHLDLI--KKAQPVGFLT 384
Cdd:cd07778 303 vgPIPGIWGPF-DQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYLT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 385 VDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPL 464
Cdd:cd07778 378 RHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNAR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 465 FVQMHADITGMPVV---LSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADK-----------KYYDK 530
Cdd:cd07778 458 LLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAFLHNQSIEERLISLKNEDQISICASASIvklvsdetklaIILRA 537
|
....*.
gi 167555144 531 KYQVFL 536
Cdd:cd07778 538 KYQIMN 543
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
12-549 |
8.91e-88 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 281.35 E-value: 8.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKW---------EPQFNHHEQSSEDIWAAcclVTKEVVQ--GIDAHRI 79
Cdd:PRK04123 4 YVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 80 RGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR-----VLQYVGGVMSVEMQAPKL 151
Cdd:PRK04123 81 VGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 152 LWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDLIDDnys 222
Cdd:PRK04123 161 LHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 223 KIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMG 302
Cdd:PRK04123 237 KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTLV----------KVM-GTSTCDIL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 303 ISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA- 377
Cdd:PRK04123 302 LADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLLELLT------EAAa 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 378 -QPVG---FLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTL 453
Cdd:PRK04123 371 kQPPGehgLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 454 FLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARM-SKVGKVVFPEHADKKYYDKK 531
Cdd:PRK04123 443 IAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQL 522
|
570
....*....|....*....
gi 167555144 532 YQVFLRMVE-HQKEYSAIM 549
Cdd:PRK04123 523 YQEYKQLHDyFGRGGNAVM 541
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
12-536 |
3.31e-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: 259.37 E-value: 3.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksGIDPSDIAAIAFSGQmQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQY---VGGVMSVEMQAPKLLWLKENLREIcWDK 165
Cdd:cd07805 81 GVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEI-YAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 166 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLE-DLIDDnyskignlvLLPGAALgIG-LTPE 242
Cdd:cd07805 151 THKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDpDKLPE---------LVPSTEV-VGeLTPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 243 AARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrlAVIC-GTSS---CHmgiSKDPVFVPGvwGPYY 318
Cdd:cd07805 221 AAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGD-------------AHIYlGTSGwvaAH---VPKPKTDPD--HGIF 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 319 S--AMVPGFWLNEGGQSVTGKLIDHMVqghpafpELQAKATARCQSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPD 392
Cdd:cd07805 282 TlaSADPGRYLLAAEQETAGGALEWAR-------DNLGGDEDLGADDYELLD---ELAAEAPPgsngLLFL-------PW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 393 FHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADI 472
Cdd:cd07805 345 LNGERSPVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADV 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555144 473 TGMPV-VLSQEVESVLVGAAILGACASGDFTSVQEAmARMSKVGKVVFPEHADKKYYDKKYQVFL 536
Cdd:cd07805 422 LGRPVeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
12-538 |
1.77e-79 |
|
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: 257.47 E-value: 1.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDA-TC 88
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLakAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 167
Cdd:cd07808 81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 168 HFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdliddnyskIGNL--VLLPGAALG 236
Cdd:cd07808 151 KIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD---------PSILppIVESTEIVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 237 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPV----TSrlAVICGTSSCHMGISKDPVF--- 309
Cdd:cd07808 214 -TLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfp 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 310 --VPGVWgpYYSAMVPGF-----WLNE--GGQSVTGKLIDHMVQGHPAfpelqakatarcqsiyaylnshldlikKAQPV 380
Cdd:cd07808 283 haVPGKW--YAMGVTLSAglslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSEGL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 381 GFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS 460
Cdd:cd07808 334 LFL-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGA 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167555144 461 KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRM 538
Cdd:cd07808 404 KSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
12-528 |
8.03e-76 |
|
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: 246.66 E-value: 8.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkaGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 168
Cdd:cd07779 81 TFVPVDEDGRPL---------RPAISWQDKRTA----------------------------------------------K 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 169 FFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDliddnySKIGNLVLlPGAALGiGLTPEAAREL 247
Cdd:cd07779 106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGIDR------DKLPELVP-PGTVIG-TLTKEAAEET 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 248 GLPSGIAVAASlidAHAGGLGVIGAdvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWL 327
Cdd:cd07779 178 GLPEGTPVVAG---GGDQQCAALGA-----GVLEPGT-----ASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 328 NEGGQSVTGKLIDHMVQghpAFPELQAKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNRSPLADLTLKG 407
Cdd:cd07779 245 LEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAGTPYWNPEARG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 408 MVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVL 487
Cdd:cd07779 316 AFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATA 392
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 167555144 488 VGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYY 528
Cdd:cd07779 393 LGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
12-494 |
9.02e-69 |
|
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: 226.68 E-value: 9.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkaGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAvsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 168
Cdd:cd00366 81 GVVLVDADGNPL---------RPAIIWLDRRA-----------------------------------------------K 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 169 FFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGLEDliddnySKIGNLVLlPGAALGiGLTPEAARE 246
Cdd:cd00366 105 FLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIPR------EKLPPIVE-SGEVVG-RVTPEAAEE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 247 LGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVtsrlaVICGTSSCHMGISKDPVFVPGVWGPYYSAmVPGFW 326
Cdd:cd00366 176 TGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLW 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 327 LNEGGQSVTGKLIDHMvqghpafpelqAKATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLAD 402
Cdd:cd00366 242 LLEGAINTGGASLRWF-----------RDEFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGERSPIWD 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 403 LTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQE 482
Cdd:cd00366 304 PAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEV 380
|
490
....*....|..
gi 167555144 483 VESVLVGAAILG 494
Cdd:cd00366 381 AEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
12-495 |
1.07e-68 |
|
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: 227.88 E-value: 1.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 90
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 91 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFF 170
Cdd:cd07783 81 VLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 171 DLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGL-EDLIddnyskigNLVLLPGAALGIgLTPEAARELG 248
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIpPDLL--------PRVVAPGTVIGT-LTAEAAEELG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 249 LPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFVPGvwGPYYSAMVP-GFWL 327
Cdd:cd07783 222 LPAGTPVVAGTTDSIAAFLAS-GAVRPGDAVT------------SLGTTLVLKLLSDKRVPDPG--GGVYSHRHGdGYWL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 328 NEGGQSVTGKLIDHMVQGHPaFPELQAKATARCQSiyaylnshldlikkaqpvgfltvDLHVWP-DFHGNRSPLADLTLK 406
Cdd:cd07783 287 VGGASNTGGAVLRWFFSDDE-LAELSAQADPPGPS-----------------------GLIYYPlPLRGERFPFWDPDAR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 407 GMVTGLTlsqdlDDLAILYLATVQAIAFGTRFIIETMEAAGHS-LSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVES 485
Cdd:cd07783 343 GFLLPRP-----HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
|
490
....*....|
gi 167555144 486 VLvGAAILGA 495
Cdd:cd07783 418 AL-GAALLAA 426
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-499 |
2.40e-65 |
|
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: 219.38 E-value: 2.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFdAT--CS 89
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISV-SSqgES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 90 LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 167
Cdd:cd07773 80 GVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 168 HFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSfwkmigLEDLIDDNYSKIGNLVlLPGAALGIgLTPEAAR 245
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEE------LLEAAGIDASLLPELV-PSGTVIGT-VTPEAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 246 ELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYS---AMV 322
Cdd:cd07773 221 ELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 323 PGFWLNEGGQSvTGKLIDHMVQghpafpELQAKATARCQSIYAYLNShldlIKKAQPVGFLtvdlhvwPDFHGNRSPLAD 402
Cdd:cd07773 288 GGYYYLAGSLP-GGALLEWFRD------LFGGDESDLAAADELAEAA----PPGPTGLLFL-------PHLSGSGTPDFD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 403 LTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQE 482
Cdd:cd07773 350 PDARGAFLGLTLGTTRAD---LLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426
|
490
....*....|....*..
gi 167555144 483 VESVLVGAAILGACASG 499
Cdd:cd07773 427 PEATALGAALLAGVGAG 443
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
12-545 |
5.02e-65 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 220.95 E-value: 5.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--------------PQFNHHEQSSEDIWAAcclVTKEVVQ--GI 74
Cdd:TIGR01234 2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWVkgqflpktgaklpnDQALQHPADYIEVLEA---AIPTVLAelGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 75 DAHRIRGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR----VLQYVGGVMSVEMQ 147
Cdd:TIGR01234 79 DPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEFAENPHayFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 148 APKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDLIDDNYSK- 223
Cdd:TIGR01234 159 WAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 224 IGNLvllpGAALGiGLTPEAARELGLPSGIAVAASLIDAHaggLGVIGADVrghgltceGQPvtSRLAVICGTSSCHMGI 303
Cdd:TIGR01234 238 IWTA----GEPAG-TLTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 304 SKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQgHPAFPELQAKATARCQSiyayLNSHLDLIKKAQPV--- 380
Cdd:TIGR01234 300 GDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgeh 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 381 GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS 460
Cdd:TIGR01234 375 GLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 461 -KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVF---PEHADKkyYDKKYQVFL 536
Cdd:TIGR01234 447 rKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLtpcSENAQR--YEQLYARYQ 524
|
....*....
gi 167555144 537 RMVEHQKEY 545
Cdd:TIGR01234 525 ELAMSFGQY 533
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-499 |
8.98e-63 |
|
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: 212.41 E-value: 8.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksGVDPSDIAGVGVTGHgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:cd07802 81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 167 GHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDLIDdnysKIGNLVllPGAALGIGL 239
Cdd:cd07802 151 RTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEELKD----KLPPLV--PSTEIAGRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 240 TPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGpYYS 319
Cdd:cd07802 218 TAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 320 AMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKATARCQSIYAYLNshlDLIKKAQPVG----FLtvdlhvwPDFHG 395
Cdd:cd07802 284 HADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PYLYG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 396 NRsplADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHsLSTLFLCGGLSKNPLFVQMHADITGM 475
Cdd:cd07802 348 SG---ANPNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLGL 420
|
490 500
....*....|....*....|....
gi 167555144 476 PVVLSQEVESVLVGAAILGACASG 499
Cdd:cd07802 421 PVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-499 |
4.22e-62 |
|
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: 210.85 E-value: 4.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFA--EQPIKKwePQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA- 86
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASAsiEHDLLT--PKPGWAEHDPEVWWGAVCEIIRELLAkaGISPKEIAAIGVSGl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 87 TCSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWD 164
Cdd:cd07804 79 VPALVPVDENGKPL---------RPAILYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPEV-FK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 165 KAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGL-EDLIDDNYSkignlvllPGAALG 236
Cdd:cd07804 149 KTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGIdPDLLPELVP--------STEIVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 237 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGP 316
Cdd:cd07804 216 -EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 317 YYSamVPGFWLNEGGQSVTGKLIDHMVQGhpAFPELQAKATARCQSIYAYLNshldliKKAQ--PVGfltVD-LHVWPDF 393
Cdd:cd07804 282 YHD--IPGTYVLNGGMATSGSLLRWFRDE--FAGEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIVLPYF 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 394 HGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADIT 473
Cdd:cd07804 349 MGERTPIWDPDARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVT 425
|
490 500
....*....|....*....|....*.
gi 167555144 474 GMPVVLSQEVESVLVGAAILGACASG 499
Cdd:cd07804 426 GVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
12-539 |
2.13e-61 |
|
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: 209.72 E-value: 2.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 90
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMhSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 91 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRI--NETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGH 168
Cdd:cd07770 81 LGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 169 FFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEDlidDNYSKignlvLLPGAALGIGLTPEA 243
Cdd:cd07770 151 FVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGIDE---EQLPE-----LVDPTEVLPGLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 244 ARELGLPSGIAVAASLIDAHAGGLGViGADVRGhgltcegqpvtsRLAVICGTSschmG----ISKDPVFVP--GVWgPY 317
Cdd:cd07770 219 AERLGLLAGTPVVLGASDGALANLGS-GALDPG------------RAALTVGTS----GairvVSDRPVLDPpgRLW-CY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 318 YSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHPAFPELQAKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPD 392
Cdd:cd07770 281 RLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 393 FHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADI 472
Cdd:cd07770 337 LAGERAPGWNPDARGAFFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555144 473 TGMPVVLSQEVESVLVGAAILGACASGDFTSVQEamARMSKVGKVVFPEHADKKYYDKKYQVFLRMV 539
Cdd:cd07770 414 LGRPVLVPEEEEASALGAALLALEALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKLY 478
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
290-497 |
1.84e-60 |
|
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: 198.32 E-value: 1.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 290 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAkaTARCQSIYAYLN 368
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRD--AGNVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 369 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEA-AG 447
Cdd:pfam02782 79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 167555144 448 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACA 497
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
12-499 |
4.92e-44 |
|
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: 162.01 E-value: 4.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHH--EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgfdAT 87
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREALKkaGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 88 CS----LVVLDKEFHPL---PvNHegdssrnvimwlDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAP-KLLWLKENLR 159
Cdd:cd07798 78 TSqregIVFLDKDGRELyagP-NI------------DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 160 EIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDLIddnyskignL--VL 229
Cdd:cd07798 145 EI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPPEI---------LpeIV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 230 LPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrLAVICGTSSCHMGISKDPVF 309
Cdd:cd07798 208 PSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS-GAIEPGD------------IGIVAGTTTPVQMVTDEPII 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 310 VP--GVW-GPYysaMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQakatarcqsiYAYLNSHLDLIKKAQP--VGFLT 384
Cdd:cd07798 274 DPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 385 VDLhvwpdFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNP 463
Cdd:cd07798 341 PQI-----FDARLSGLKNGGFLFPTPLSASELTRGDFAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSA 412
|
490 500 510
....*....|....*....|....*....|....*.
gi 167555144 464 LFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 499
Cdd:cd07798 413 LLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
12-499 |
4.96e-43 |
|
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: 159.25 E-value: 4.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPikkWEPQFNHH---EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD 85
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAP---HENILIDPgwaEQDPEDWWDALQAAFAQLLKdaGAELRDVAAIGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 86 ATC-SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcW 163
Cdd:cd07809 78 GQMhGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-Y 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 164 DKAgHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDLIDDNYSKIGNlVLLPGAAL 235
Cdd:cd07809 148 ARI-AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLPE-VLPAGEVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 236 GiGLTPEAARELGLPSGIAVAASLIDAHAG--GLGVIGadvrghgltcEGQPVTSrlaviCGTSSCHMGISKDPVFVPgv 313
Cdd:cd07809 217 G-RLTPEGAEELGLPAGIPVAPGEGDNMTGalGTGVVN----------PGTVAVS-----LGTSGTAYGVSDKPVSDP-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 314 wgpyySAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYlnshldlikkaqpvgf 382
Cdd:cd07809 279 -----HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLL---------------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 383 ltvdlhvwPDFHGNRSP-LADLTlkGMVTGLTLSQdlDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSK 461
Cdd:cd07809 338 --------PFLNGERTPnLPHGR--ASLVGLTLSN--FTRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSK 405
|
490 500 510
....*....|....*....|....*....|....*...
gi 167555144 462 NPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 499
Cdd:cd07809 406 SPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-499 |
4.30e-41 |
|
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: 153.93 E-value: 4.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGID--AHRIRGLGFDAT-- 87
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDvlPDRVAAIGVTGQgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 88 -CSLVvlDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICwD 164
Cdd:cd24121 81 gTWLV--DEDGRPV---------RDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 165 KAGHFFDLPDFLSWKATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDLIDdnyskignlvLLPGAALGIG--- 238
Cdd:cd24121 149 RARTALHCKDWLFYKLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH----------LLPPIRPGTEvig 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 239 -LTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFvpgvwGPY 317
Cdd:cd24121 216 pLTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDACS------------ILGTTGVHEVVVDEPDL-----EPE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 318 YSAM-----VPGFWLNEGGqSVTGKL-IDHMVQghPAFPELQAKATARCQSIYAYLNSHLdlikKAQPVGFLTVDLHVWP 391
Cdd:cd24121 278 GVGYticlgVPGRWLRAMA-NMAGTPnLDWFLR--ELGEVLKEGAEPAGSDLFQDLEELA----ASSPPGAEGVLYHPYL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 392 DFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRfiiETMEAAGHSLSTLFLCGGLSKNPLFVQMHAD 471
Cdd:cd24121 351 SPAGERAPFVNPNARAQFTGLSLEHTRADLL---RAVYEGVALAMR---DCYEHMGEDPGELRLSGGGARSDTWCQILAD 424
|
490 500
....*....|....*....|....*...
gi 167555144 472 ITGMPVVLSQEVESVLVGAAILGACASG 499
Cdd:cd24121 425 ALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
12-533 |
1.92e-29 |
|
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: 121.67 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKWEPQFNHHEQSSEDI-----WAACCLVTKEVVQ--GIDAHRIRGLgf 84
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQ---REWRHKEVPDVPGSMDFdteknWKLICECIREALKkaGIAPKSIAAI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 85 dATCS----LVVLDKEFHPLPVNHegdssrNVimwlDHRAVSQVHRINETKH---RVLQYVGGVMSVEMQAPKLLWLKEN 157
Cdd:cd07775 76 -STTSmregIVLYDNEGEEIWACA------NV----DARAAEEVSELKELYNtleEEVYRISGQTFALGAIPRLLWLKNN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 158 LREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDLIDDNyskignlVLLPGAAL 235
Cdd:cd07775 145 RPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKADILPP-------VVESGTVI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 236 GIgLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrlAVICGTSSCHMGI-SKDPVFVPGVW 314
Cdd:cd07775 216 GK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 315 GPYYSAMVPGFWLNEGGQSVTGKLIDHMVQghpAF-PELQAKATARCQSIYAYLNshldliKKAQ--PVGF-----LTVD 386
Cdd:cd07775 281 IRVNCHVIPDMWQAEGISFFPGLVMRWFRD---AFcAEEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpIFSD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 387 L-------HVWPDFhgnrspladltlkgmvTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAA-GHSLSTLFLCGG 458
Cdd:cd07775 352 VmnyknwrHAAPSF----------------LNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGG 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555144 459 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQ 533
Cdd:cd07775 416 ASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-268 |
4.98e-26 |
|
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: 106.65 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATC- 88
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlGISLKQIKGIGISNQGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:pfam00370 81 GTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 167 GHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdliDDNYSKignlvLLPGAALGIG 238
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP---RDHLPP-----LVESSEIYGE 215
|
250 260 270
....*....|....*....|....*....|
gi 167555144 239 LTPEAARELGLPSGIAVAASLIDAHAGGLG 268
Cdd:pfam00370 216 LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
12-540 |
8.73e-22 |
|
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: 98.31 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdaTC- 88
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAkaGISASDIAAIGI--TNq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 89 --SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---LREI 161
Cdd:cd07769 79 reTTVVWDK--------KTGKPLYNAIVWQDRRTADICEELKAKGLeeRIREKTGLPLDPYFSATKIKWILDNvpgARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 162 CwdKAGHF-FDLPD-FLSWKATG----VT-----ARSLcsLvckwtYSAEKG-WDDSfwkmigLEDLIDdnyskignlvl 229
Cdd:cd07769 151 A--ERGELlFGTIDtWLIWKLTGgkvhVTdvtnaSRTM--L-----FNIHTLeWDDE------LLELFG----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 230 LPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEGQpvtsrlaVIC--GT-S 297
Cdd:cd07769 205 IPRSML-----PEvrpssevfgYTDPEGLGAGIPIAGILGDQQA-------ALF-GQGCFEPGM-------AKNtyGTgC 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 298 SCHMGISKDPVFV-PGV-----WG----PYYSAmvpgfwlnEGGQSVTGKLIDHMVQGhpafpelqakatarcqsiyayl 367
Cdd:cd07769 265 FLLMNTGEKPVPSkNGLlttiaWQiggkVTYAL--------EGSIFIAGAAIQWLRDN---------------------- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 368 nshLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIE 441
Cdd:cd07769 315 ---LGLIEDAAETEELarSVEdnggVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 442 TMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEaMARMSKVGKVVFP 520
Cdd:cd07769 389 AMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDE-LASLWQVDKRFEP 467
|
570 580
....*....|....*....|
gi 167555144 521 EhADKKYYDKKYQVFLRMVE 540
Cdd:cd07769 468 S-MDEEERERLYRGWKKAVE 486
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
10-540 |
7.50e-21 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 95.51 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 10 SRYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD-- 85
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAkaGISAEDIAAIGITnq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 86 -ATCslVVLDKEF-HPLpvnHegdssrNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---L 158
Cdd:COG0554 82 rETT--VVWDRKTgKPL---Y------NAIVWQDRRTADICEELKADGLedLIREKTGLVLDPYFSATKIKWILDNvpgA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 159 REicwdKA--GH-FFDLPD-FLSWKATG----VT-----ARSLCslvckwtYSAEKG-WDDSFWKMIGLedliddnyski 224
Cdd:COG0554 151 RE----RAeaGElLFGTIDsWLIWKLTGgkvhVTdvtnaSRTML-------FNIHTLdWDDELLELFGI----------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 225 gnlvllPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEG------------ 283
Cdd:COG0554 209 ------PRSML-----PEvrpssevfgETDPDLFGAEIPIAGIAGDQQA-------ALF-GQACFEPGmakntygtgcfl 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 284 ------QPVTSR---LAVICgtsschmgiskdpvfvpgvWG----PYYsAMvpgfwlnEGGQSVTGKLIDhmvqghpafp 350
Cdd:COG0554 270 lmntgdEPVRSKnglLTTIA-------------------WGlggkVTY-AL-------EGSIFVAGAAVQ---------- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 351 elqakatarcqsiyaYLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAil 424
Cdd:COG0554 313 ---------------WLRDGLGLIDSAAESEALarSVEdnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA-- 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 425 yLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTS 503
Cdd:COG0554 376 -RAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKS 454
|
570 580 590
....*....|....*....|....*....|....*..
gi 167555144 504 VQEaMARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 540
Cdd:COG0554 455 LEE-LAALWKVDRRFEPQ-MDEEERERLYAGWKKAVE 489
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
13-538 |
6.70e-20 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 92.72 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 13 YVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC-----CLVTKEVVQGIDAHRIRGLGFDAT 87
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATdramkALGDQHSLQDVKALGIAGQMHGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 88 cslvVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAG 167
Cdd:PRK15027 82 ----LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 168 HFfdLP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDLIDDNYSkignlVLLPGAALGIGLTPEAAR 245
Cdd:PRK15027 149 VL--LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 246 ELGLPSgIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVTSrlaviCGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:PRK15027 219 AWGMAT-VPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 326 WlneggqsvtgKLIDHMVQGHPAFpELQAKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTL 405
Cdd:PRK15027 285 W----------HLMSVMLSAASCL-DWAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 406 KGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQ--EV 483
Cdd:PRK15027 346 KGVFFGLTHQHGPNELA---RAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTggDV 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 167555144 484 ESVLvGAAILGACASGDFTSVQEAMARMSkVGKVVFPEHADKKYYDKKYQVFLRM 538
Cdd:PRK15027 423 GPAL-GAARLAQIAANPEKSLIELLPQLP-LEQSHLPDAQRYAAYQPRRETFRRL 475
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
12-540 |
9.48e-19 |
|
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: 89.16 E-value: 9.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdAT-- 87
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKnaGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 88 CSLVVLDKE----FHplpvnhegdssrNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVM-----------------SVE 145
Cdd:cd07793 80 NTFLTWDKKtgkpLH------------NFITWQDLRAAELCESWNRsLLLKALRGGSKFLhfltrnkrflaasvlkfSTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 146 MQAPKLLWLKENLREICWDKAGH---FFDLPDFLSWKATG----VTARSLCSLVckwtysaekgwddsfwkmiGLEDLID 218
Cdd:cd07793 148 HVSIRLLWILQNNPELKEAAEKGellFGTIDTWLLWKLTGgkvhATDYSNASAT-------------------GLFDPFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 219 DNYSK-IGNLVLLPGAALgigltPEaarelglpsgiavaaslIDAHAGGLGVIGADVRGHGLtcegqPVTSrlavICGTS 297
Cdd:cd07793 209 LEWSPiLLSLFGIPSSIL-----PE-----------------VKDTSGDFGSTDPSIFGAEI-----PITA----VVADQ 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 298 SCHMgiskdpvFVPGVWGPYYSAMVPG---FW-LNEGGQ---SVTG--KLIDHMVQGHPAF-PELQAKATARC----QSI 363
Cdd:cd07793 258 QAAL-------FGECCFDKGDVKITMGtgtFIdINTGSKphaSVKGlyPLVGWKIGGEITYlAEGNASDTGTVidwaKSI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 364 yAYLNSHLDLIKKAQPVGfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETM 443
Cdd:cd07793 331 -GLFDDPSETEDIAESVE-DTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETM 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 444 EA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVqEAMARMSKVGKVVFPEh 522
Cdd:cd07793 406 EKeTSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK- 483
|
570
....*....|....*...
gi 167555144 523 ADKKYYDKKYQVFLRMVE 540
Cdd:cd07793 484 MDNEKREELYKNWKKAVK 501
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-520 |
4.94e-17 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 83.92 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 17 DVGTGSVRAALVDQRGLLLAFAEQP----IKKWEPQFnhHEQSSEDIW---AACClvtKEVVQGIDAHRIRGL-----GF 84
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnasdIAAENSDW--HQWSLDAILqrfADCC---RQINSELTECHIRGItvttfGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 85 DATcslvvldkefhplPVNHEGDSSRNVIMWLDHRAVSQVHRI-NETKHRVLQYVGGVMSVEMQAP-KLLWLKENLREIc 162
Cdd:PRK10331 83 DGA-------------LVDKQGNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVGAFSFNTLyKLVWLKENHPQL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 163 WDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGL-EDL---IDDNYSKIGNLvllpgaalg 236
Cdd:PRK10331 149 LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLsRRLfprLVEAGEQIGTL--------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 237 iglTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrGHGLtceGQPV-----------------TSRLAVICGtSSC 299
Cdd:PRK10331 219 ---QPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvdTSLLSQYAG-STC 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 300 HMGiSKDPVFVPGVWgpyysamvpgfWLNEGGQSVTGKLIdhmvqghpaFPELQAKATarcqsiyaylnshldLIKKAQP 379
Cdd:PRK10331 286 ELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLF---------WTAETPYQT---------------MIEEARA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 380 VGFLTVDLHVWPDFHGNRspladltlKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGH-SLSTLFLCGG 458
Cdd:PRK10331 330 IPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHF---YRAALEGLTAQLKRNLQVLEKIGHfKASELLLVGG 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555144 459 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFP 520
Cdd:PRK10331 399 GSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYP 460
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
12-540 |
6.55e-17 |
|
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: 83.31 E-value: 6.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD---A 86
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAkaGIRASDIAAIGITnqrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 87 TCslVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---LREI 161
Cdd:cd07786 81 TT--VVWDRE--------TGKPVYNAIVWQDRRTADICEELKAEGHeeMIREKTGLVLDPYFSATKIRWILDNvpgARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 162 cwDKAGH-FFDLPD-FLSWKATG----VT-----ARSLcslvckwTYSAEKG-WDDsfwkmiGLEDLIDdnyskignlvl 229
Cdd:cd07786 151 --AERGElAFGTIDsWLIWKLTGgkvhATdvtnaSRTM-------LFNIHTLeWDD------ELLELFG----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 230 LPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEGQ---------------- 284
Cdd:cd07786 205 IPASML-----PEvkpssevfgYTDPDLLGAEIPIAGIAGDQQA-------ALF-GQACFEPGMakntygtgcfmlmntg 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 285 --PVTSR---LAVICGtsschmGISKDP-------VFVPGvwgpyysAMVPgfWLNEGGqsvtgKLIDHmvqghpafpel 352
Cdd:cd07786 272 ekPVRSKnglLTTIAW------QLGGKVtyalegsIFIAG-------AAVQ--WLRDGL-----GLIES----------- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 353 qAKATArcqsiyaylnshlDLIKKAQPVGfltvDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAI 432
Cdd:cd07786 321 -AAETE-------------ALARSVPDNG----GVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA---RAALESI 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 433 AFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAmARM 511
Cdd:cd07786 380 AYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDEL-AKL 458
|
570 580
....*....|....*....|....*....
gi 167555144 512 SKVGKVVFPEhADKKYYDKKYQVFLRMVE 540
Cdd:cd07786 459 WQVDRRFEPS-MSEEEREALYAGWKKAVK 486
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
12-542 |
7.59e-17 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 83.52 E-value: 7.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKW----EPQF-NHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgf 84
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWrhlaVPDVpGSMEFDLEKNWQLACQCIRQALQkaGIPASDIAAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 85 dATCSL----VVLDKEFHPLpvnhegdssrnvimW----LDHRAVSQV----HRINETKHRVLQYVGGVMSVEmQAPKLL 152
Cdd:PRK10939 79 -SATSMregiVLYDRNGTEI--------------WacanVDARASREVselkELHNNFEEEVYRCSGQTLALG-ALPRLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 153 WLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKMIGledLIDDNYSKi 224
Cdd:PRK10939 143 WLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEMAG---LRADILPP- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 225 gnlVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGT-------- 296
Cdd:PRK10939 211 ---VKETGTVLG-HVTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnl 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 297 ----SSCHMGISKDPvfvpgvwgpyysAMVPGFWLNEGGQSVTGkLIdhMVQGHPAF-PELQAKATARCQSIYAYLNshl 371
Cdd:PRK10939 274 papvTDPNMNIRINP------------HVIPGMVQAESISFFTG-LT--MRWFRDAFcAEEKLLAERLGIDAYSLLE--- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 372 dliKKAQ--PVGFLTVdLHVWPD-------FHGNRSPLadltlkgmvtGLTLSQDLDDLAILYLATVQAIAFGTRFIIET 442
Cdd:PRK10939 336 ---EMASrvPVGSHGI-IPIFSDvmrfkswYHAAPSFI----------NLSIDPEKCNKATLFRALEENAAIVSACNLQQ 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 443 MEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPE 521
Cdd:PRK10939 402 IAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPN 481
|
570 580
....*....|....*....|.
gi 167555144 522 HADKKYYDKKYQVFLRMVEHQ 542
Cdd:PRK10939 482 PENHELYQEAKEKWQAVYADQ 502
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
13-540 |
2.40e-16 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 81.80 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 13 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC--CL---VTKEVVQGIDAHRIRGLGFda 86
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVyeCIeeaVEKLKALGISPSDIKAIGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 87 TC---SLVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHR----INETKHRVLQYVGGVMSVEMQAPKLLWLKENLR 159
Cdd:cd07792 80 TNqreTTVVWDKS--------TGKPLYNAIVWLDTRTSDTVEElsakTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 160 EI---------------CWdkaghffdlpdfLSWKATG----------VTARSLCSLV----CKWtysaekgwDDSFWKM 210
Cdd:cd07792 152 EVkkavddgrllfgtvdSW------------LIWNLTGgknggvhvtdVTNASRTMLMnlrtLQW--------DPELCEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 211 IGLedliddnyskignlvllPGAALgigltPE---AARELGLPS-----GIAVAASLIDAHAgglgvigADVrGHGLTCE 282
Cdd:cd07792 212 FGI-----------------PMSIL-----PEirsSSEVYGKIAsgplaGVPISGCLGDQQA-------ALV-GQGCFKP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 283 GQ------------------PVTSRlaviCG--TSSCH-MGISKDPVFvpgvwgpyysAMvpgfwlnEGGQSVTGKLIDh 341
Cdd:cd07792 262 GEakntygtgcfllyntgeePVFSK----HGllTTVAYkLGPDAPPVY----------AL-------EGSIAIAGAAVQ- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 342 mvqghpafpelqakatarcqsiyaYLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLS 415
Cdd:cd07792 320 ------------------------WLRDNLGIISSASEVETLaaSVPdtggVYFVPAFSGLFAPYWRPDARGTIVGLTQF 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 416 QDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILG 494
Cdd:cd07792 376 TTKAHIA---RAALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAA 452
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 167555144 495 ACASGDFTSVQEaMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVE 540
Cdd:cd07792 453 GLAVGVWKSLDE-LKSLNEGGRTVFEPQISEEERERRYKRWKKAVE 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
13-532 |
3.73e-15 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 78.09 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 13 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIdahRIRGLGFDATC--- 88
Cdd:PTZ00294 3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKL---REKGPSFKIKAigi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 89 -----SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINET--KHRVLQYVGG-VMSVEMQAPKLLWLKENLRE 160
Cdd:PTZ00294 80 tnqreTVVAWDK--------VTGKPLYNAIVWLDTRTYDIVNELTKKygGSNFFQKITGlPISTYFSAFKIRWMLENVPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 161 IcwDKAGH-----FFDLPDFLSWKATG-------VTARSLCSLVCKWTYSaekgWDDSFWKMIGL--EDL--IDDNYSKI 224
Cdd:PTZ00294 152 V--KDAVKegtllFGTIDTWLIWNLTGgkshvtdVTNASRTFLMNIKTLK----WDEELLNKFGIpkETLpeIKSSSENF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 225 GNLVLLPGAALgigltpeaarelglpSGIAVAASLIDAHAGGLGvigadvrgHGLTCEGQPVTSRlavicGTSsCH--MG 302
Cdd:PTZ00294 226 GTISGEAVPLL---------------EGVPITGCIGDQQAALIG--------HGCFEKGDAKNTY-----GTG-CFllMN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 303 ISKDPVFVP-GVWGpyysamVPGFWLNEGGQSVtgklidHMVQGhpafpelqakATARCQSIYAYLNSHLDLIKKAQPVG 381
Cdd:PTZ00294 277 TGTEIVFSKhGLLT------TVCYQLGPNGPTV------YALEG----------SIAVAGAGVEWLRDNMGLISHPSEIE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 382 FL------TVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETME-AAGHSLSTLF 454
Cdd:PTZ00294 335 KLarsvkdTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIV---RAALEAIALQTNDVIESMEkDAGIELNSLR 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167555144 455 LCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPeHADKKYYDKKY 532
Cdd:PTZ00294 412 VDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSNSTFSP-QMSAEERKAIY 488
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
12-493 |
3.76e-15 |
|
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: 77.65 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWEPQ--FNHHEQSSEDIWAAcclvTKEVVQGIDAH---RIRGLGFd 85
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPREylsDVTGIGI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 86 aTC---SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGV-MSVEMQAPKLLWLKENLREI 161
Cdd:cd07777 76 -TGqmhGIVLWDEDGNPV---------SPLITWQDQRCSEEFLGGLSTYGEELLPKSGMrLKPGYGLATLFWLLRNGPLP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 162 cwDKAGHFFDLPDFLSWKATGvTARSLCSLVCK--WTY--SAEKGWDDSFWKMIGLEDLIddnYSKIGNlvllPGAALGi 237
Cdd:cd07777 146 --SKADRAGTIGDYIVARLTG-LPKPVMHPTNAasWGLfdLETGTWNKDLLEALGLPVIL---LPEIVP----SGEIVG- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 238 GLTPEaarelgLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRLAVICGTSScHMGISKDPVFVPGVWG-- 315
Cdd:cd07777 215 TLSSA------LPKGIPVYVALGDNQAS---VLGSGLNEEN----------DAVLNIGTGA-QLSFLTPKFELSGSVEir 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 316 PYYSamvpGFWLNeggqSVT----GKLIDHMVQghpAFPELQAKATARC--QSIYAYLNShLDLIKKAQPvgfLTVDlhv 389
Cdd:cd07777 275 PFFD----GRYLL----VAAslpgGRALAVLVD---FLREWLRELGGSLsdDEIWEKLDE-LAESEESSD---LSVD--- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 390 wPDFHGNRSplaDLTLKGMVTGLTLsqdlDDLAI--LYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGG-LSKNPLFV 466
Cdd:cd07777 337 -PTFFGERH---DPEGRGSITNIGE----SNFTLgnLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLR 408
|
490 500
....*....|....*....|....*..
gi 167555144 467 QMHADITGMPVVLSQEVESVLVGAAIL 493
Cdd:cd07777 409 RIIEKRFGLPVVLSEGSEEAAVGAALL 435
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
388-541 |
4.49e-12 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 68.31 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 388 HVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFV 466
Cdd:PRK00047 344 YVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHII---RATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLM 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555144 467 QMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEaMARMSKVGKVVFPEHADKKyYDKKYQVFLRMVEH 541
Cdd:PRK00047 421 QFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDE-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
13-527 |
1.60e-10 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 63.56 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 13 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAcclVTKEVVQGIDAHRIRGLGFDATCSLV 91
Cdd:PLN02295 1 FVGaIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILES---VLTCIAKALEKAAAKGHNVDSGLKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 92 VL--DKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKH----RVLQYVGGVMSVEMQAPKLLWLKENLREICWD- 164
Cdd:PLN02295 78 GItnQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSggrkHFVETCGLPISTYFSATKLLWLLENVDAVKEAv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 165 KAGH--FFDLPDFLSWKATGVTARSL----CSLVCKWTYSAEKG--WDDSFWKMIGL--EDL--IDDNYSKIGnlvllpG 232
Cdd:PLN02295 158 KSGDalFGTIDSWLIWNLTGGASGGVhvtdVTNASRTMLMNLKTldWDKPTLEALGIpaEILpkIVSNSEVIG------T 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 233 AALGIGLtpeaarelglpSGIAVAASLIDAHAGGLGvigadvrghgltcegqpvtsrlavicgtSSCHMGISKDpVFVPG 312
Cdd:PLN02295 232 IAKGWPL-----------AGVPIAGCLGDQHAAMLG----------------------------QRCRPGEAKS-TYGTG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 313 VWgpyysaMVpgfwLNEGGQSVTGKlidHMVQGHPAFpELQAKATARcqsiYA-------------YLNSHLDLIKKAQP 379
Cdd:PLN02295 272 CF------IL----LNTGEEVVPSK---HGLLTTVAY-KLGPDAPTN----YAlegsvaiagaavqWLRDNLGIIKSASE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 380 VGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETM------EAAG 447
Cdd:PLN02295 334 IEALaaTVDdtggVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIA---RAVLESMCFQVKDVLDAMrkdageEKSH 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 448 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFP----EHA 523
Cdd:PLN02295 411 KGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPkldeEER 490
|
....
gi 167555144 524 DKKY 527
Cdd:PLN02295 491 AKRY 494
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
16-493 |
2.41e-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: 53.03 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 16 IDVGTGSVRAALVDQRGLLLAFAEQPIK-KWEPQFNHHEqsSEDIWAACCLVTKEVVQGidaHRIRGLGFdaTC---SLV 91
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPeIEEDGYPCED--VEAIWEWLLDSLAELAKR---HRIDAINF--TThgaTFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 92 VLDKEFHP-LPV---NHEGDSSrnvimwldhravsqvhrINEtkhrvlQY--------------VGGVMSVEMQapkLLW 153
Cdd:cd07772 78 LLDENGELaLPVydyEKPIPDE-----------------INE------AYyaergpfeetgsppLPGGLNLGKQ---LYW 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 154 LKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledliddnys 222
Cdd:cd07772 132 LKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 223 kignlvLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAgglgvigadvrghgltcegqpvtSRLAvicgtsscHMG 302
Cdd:cd07772 199 ------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP--------YLA 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 303 ISKDPvFV---PGVWgpyYSAMVPGFWLNEGGQSVTGKLIDHM-VQGHPA----FP-----ELQAKataRCQSIYAYLNS 369
Cdd:cd07772 241 AGKEP-FTllsTGTW---CIAMNPGNDLPLTELDLARDCLYNLdVFGRPVktarFMggreyERLVE---RIAKSFPQLPS 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 370 HLDLIKkaqpvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAfgtrfiietMEAAGHS 449
Cdd:cd07772 314 LADLAK------LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYA---------LDLLGSG 378
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 167555144 450 LSTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAIL 493
Cdd:cd07772 379 VGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
432-507 |
2.57e-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: 53.30 E-value: 2.57e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555144 432 IAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAILGACASGDFTSVQEA 507
Cdd:cd07771 378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
447-530 |
8.58e-04 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 42.16 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555144 447 GHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKV----GKVVFPEH 522
Cdd:cd07776 423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502
|
....*...
gi 167555144 523 ADKKYYDK 530
Cdd:cd07776 503 EAAEVYDK 510
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
11-84 |
3.98e-03 |
|
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: 39.49 E-value: 3.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167555144 11 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIkkwepqfnHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGF 84
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPT--------PAGAGPEAVLEAIAELIEELLAeaGISRGRILGIGI 72
|
|
| |
