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Conserved domains on  [gi|498326674|ref|WP_010640830|]
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MULTISPECIES: ROK family transcriptional regulator [Streptomyces]

Protein Classification

ROK family transcriptional regulator( domain architecture ID 11448795)

NagC/ROK (Repressor, ORF, Kinase) family transcriptional regulator is involved in carbohydrate-dependent transcriptional control; contains a MarR family winged helix-turn-helix domain

CATH:  1.10.10.10
Gene Ontology:  GO:0003700|GO:0006355
SCOP:  4000330

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
77-384 6.42e-94

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: 283.71  E-value: 6.42e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:COG1940    7 VIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELlaEAGISRGRILGIGIGVPGPVDPETGVVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:COG1940   87 NAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGEI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGR--SAELAARLEAggrlsaadvaaaasgGDTAALELIRRG 312
Cdd:COG1940  167 GHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGGAEKltAEELFAAARA---------------GDPLALEVLDEA 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498326674 313 GRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:COG1940  232 ARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAAL 303
Lrp super family cl34293
DNA-binding transcriptional regulator, Lrp family [Transcription];
12-52 7.04e-03

DNA-binding transcriptional regulator, Lrp family [Transcription];


The actual alignment was detected with superfamily member COG1522:

Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 36.68  E-value: 7.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 498326674  12 RLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLV 52
Cdd:COG1522    9 RILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVI 49
 
Name Accession Description Interval E-value
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
77-384 6.42e-94

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: 283.71  E-value: 6.42e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:COG1940    7 VIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELlaEAGISRGRILGIGIGVPGPVDPETGVVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:COG1940   87 NAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGEI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGR--SAELAARLEAggrlsaadvaaaasgGDTAALELIRRG 312
Cdd:COG1940  167 GHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGGAEKltAEELFAAARA---------------GDPLALEVLDEA 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498326674 313 GRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:COG1940  232 ARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAAL 303
ASKHA_ATPase_ROK_BsXylR-like cd24076
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ...
75-388 1.24e-71

ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Bacillus subtilis xylose repressor (BsXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. BsXylR acts as transcriptional repressor of xylose-utilizing enzymes.


Pssm-ID: 466926 [Multi-domain]  Cd Length: 303  Bit Score: 226.29  E-value: 1.24e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  75 LRFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGI 152
Cdd:cd24076    1 GAVIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREAlaAAPDSPLGILGIGVGVPGLVDSEDGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24076   81 VLLAPNL-GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPDGLPCACGNQGCLEAHFSGSALAR---DAEQVAREGRSAELAARLEAggrlsaadvaaaasgGDTAALELI 309
Cdd:cd24076  160 EIGHMTVDPDGPPCSCGNRGCWETYASERALLRaagRLGAGGEPLSLAELVEAARA---------------GDPAALAAL 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498326674 310 RRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDH 388
Cdd:cd24076  225 EEVGEYLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAAALAIDH 303
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
78-392 1.38e-59

ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]


Pssm-ID: 273246 [Multi-domain]  Cd Length: 318  Bit Score: 195.89  E-value: 1.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674   78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAV-----FEQVLDMAEKLKASGLaegfdGAGIGVPGPVRFPEGI 152
Cdd:TIGR00744   1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDaiasaVDSFIQHIAKVGHEIV-----AIGIGAPGPVNRQRGT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  153 PVAPPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:TIGR00744  76 VYFAVNL-DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  233 DIGHIQVEPDG-LPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRR 311
Cdd:TIGR00744 155 EIGHIRMVPDGrLLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYRE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  312 GGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLFS 391
Cdd:TIGR00744 235 VARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGAADLARTYIIE 314

                  .
gi 498326674  392 P 392
Cdd:TIGR00744 315 P 315
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
78-384 5.63e-56

ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.


Pssm-ID: 395384 [Multi-domain]  Cd Length: 292  Bit Score: 185.62  E-value: 5.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674   78 LGVDIGATSVDVAVTNAELEVLGHI---TQPMDVREGPVAVFEQVLDMAEklkasGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:pfam00480   1 IGIDIGGTKIAAALFDEEGEILARErvpTPTTTTEETLVDAIAFFVDSAQ-----RKFGELIAVGIGSPGLISPKYGYIT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  155 APPiMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:pfam00480  76 NTP-NIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAR--EGRSAELAARLeaggrlsaadvaaaasgGDTAALELIRRG 312
Cdd:pfam00480 155 GHIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQKGEdlEGKDIIVLAEQ-----------------GDEVAEEAVERL 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498326674  313 GRHTGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAAIRTQVYRQSL-PLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:pfam00480 218 ARYLAKAIANLINLFDPQAIVLGGGV-SNADGLLEAIRSLVKKYLNgYLPVPPVIIVAASLGDNAGALGAAAL 289
PRK09698 PRK09698
D-allose kinase; Provisional
76-393 8.66e-29

D-allose kinase; Provisional


Pssm-ID: 182034 [Multi-domain]  Cd Length: 302  Bit Score: 113.92  E-value: 8.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  76 RFLGVDIGATSVDVAVTNAELEVLGHITQP-MDVREGPVA------VFEQVLDMAEKLKasglaegfdGAGIGVPGPVRF 148
Cdd:PRK09698   5 VVLGIDMGGTHIRFCLVDAEGEILHCEKKRtAEVIAPDLVsglgemIDEYLRRFNARCH---------GIVMGFPALVSK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 149 PEGIPVAPPIMP--GWDGFPVREALSQELGCPVMVDNDVNLMAMGE--QHAGVARTArdfLCVKIGTGIGCGIVVGSTVY 224
Cdd:PRK09698  76 DRRTVISTPNLPltALDLYDLADKLENTLNCPVFFSRDVNLQLLWDvkENNLTQQLV---LGAYLGTGMGFAVWMNGAPW 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 225 RGTTGSAGDIGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVARegrsaelaarleaggrlsaadvaaaasggDTA 304
Cdd:PRK09698 153 TGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQQPR-----------------------------DYP 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 305 ALELIRRGGRH---------TGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSL-PLATGNLPIVLGELGP 374
Cdd:PRK09698 204 LSDLFVHAGDHpfiqsllenLARAIATSINLFDPDAIILGGGVMDMPAFPRETLIAMIQKYLRkPLPYEVVRFIYASSSD 283
                        330
                 ....*....|....*....
gi 498326674 375 AAGVIGGARLISDHLFSPA 393
Cdd:PRK09698 284 FNGAQGAAILAHQRFLPQS 302
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
12-52 7.04e-03

DNA-binding transcriptional regulator, Lrp family [Transcription];


Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 36.68  E-value: 7.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 498326674  12 RLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLV 52
Cdd:COG1522    9 RILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVI 49
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
12-52 8.59e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 33.95  E-value: 8.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 498326674   12 RLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLV 52
Cdd:pfam13412   5 KILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
 
Name Accession Description Interval E-value
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
77-384 6.42e-94

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: 283.71  E-value: 6.42e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:COG1940    7 VIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELlaEAGISRGRILGIGIGVPGPVDPETGVVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:COG1940   87 NAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGEI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGR--SAELAARLEAggrlsaadvaaaasgGDTAALELIRRG 312
Cdd:COG1940  167 GHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGGAEKltAEELFAAARA---------------GDPLALEVLDEA 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498326674 313 GRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:COG1940  232 ARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAAL 303
ASKHA_ATPase_ROK_BsXylR-like cd24076
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ...
75-388 1.24e-71

ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Bacillus subtilis xylose repressor (BsXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. BsXylR acts as transcriptional repressor of xylose-utilizing enzymes.


Pssm-ID: 466926 [Multi-domain]  Cd Length: 303  Bit Score: 226.29  E-value: 1.24e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  75 LRFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGI 152
Cdd:cd24076    1 GAVIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREAlaAAPDSPLGILGIGVGVPGLVDSEDGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24076   81 VLLAPNL-GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPDGLPCACGNQGCLEAHFSGSALAR---DAEQVAREGRSAELAARLEAggrlsaadvaaaasgGDTAALELI 309
Cdd:cd24076  160 EIGHMTVDPDGPPCSCGNRGCWETYASERALLRaagRLGAGGEPLSLAELVEAARA---------------GDPAALAAL 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498326674 310 RRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDH 388
Cdd:cd24076  225 EEVGEYLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAAALAIDH 303
ASKHA_ATPase_ROK cd23763
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ...
78-384 3.85e-70

ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466849 [Multi-domain]  Cd Length: 239  Bit Score: 220.41  E-value: 3.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL-KASGLAEGFDGAGIGVPGPVRFPEGIPVAP 156
Cdd:cd23763    1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELlAEAGVRERILGIGIGVPGPVDPETGIVLFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd23763   81 PNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVepdglpcacgnqgcleahfsgsalardaeqvaregrsaelaarleaggrlsaadvaaaasggdtaalelIRRGGRHT 316
Cdd:cd23763  161 ITV---------------------------------------------------------------------LEEAARYL 171
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd23763  172 GIGLANLINLLNPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLLGAAAL 239
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
77-384 9.82e-70

nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and similar proteins; The family includes Fusobacterium nucleatum N-acetylmannosamine kinase (NanK; EC 2.7.1.60) and beta-glucoside kinase (BglK; EC 2.7.1.85) from Klebsiella pneumoniae and Listeria innocua. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. BglK catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. It may have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. The subfamily belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.


Pssm-ID: 466918 [Multi-domain]  Cd Length: 294  Bit Score: 221.28  E-value: 9.82e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKLKASGLAEGfdgAGIGVPGPVRFPEGIPV-A 155
Cdd:cd24068    2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEG---IGISSAGQVDPKTGEVIyA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24068   79 TDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQV--AREGRSAELAARLEAggrlsaadvaaaasgGDTAALELIRRGG 313
Cdd:cd24068  159 HMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEAlgEPGIDGREIFDLADA---------------GDPLAKEVVEEFA 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498326674 314 RHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd24068  224 EDLATGLANLVHIFDPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAYL 294
ASKHA_NBD_ROK_BsGLK-like cd24062
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ...
76-384 2.57e-65

nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466912 [Multi-domain]  Cd Length: 311  Bit Score: 210.61  E-value: 2.57e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  76 RFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEG-I 152
Cdd:cd24062    1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIITDIAESIQQLleELGYSKEDLIGIGVGVPGPVDVETGtV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPImpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24062   81 EVAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPD-GLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRR 311
Cdd:cd24062  159 EIGHITVNPEgGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAVVDT 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498326674 312 GGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd24062  239 VARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAAWL 311
ASKHA_NBD_ROK_TM1224-like cd24059
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ...
78-391 1.52e-64

nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to N-acetylglucosamine kinase (Tm1224; EC 2.7.1.59) from Thermotoga maritima, which belongs to kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Tm1224 lacks the cysteine-rich zinc-binding motif, which presents in other family members.


Pssm-ID: 466909 [Multi-domain]  Cd Length: 305  Bit Score: 208.21  E-value: 1.52e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEK-LKASGLAEGFDGAGIGVPGPVRFPEGIPVAP 156
Cdd:cd24059    4 IGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRlLEKENIKSKILGIGIGAPGPLDVEKGIILNP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd24059   84 PNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEIGH 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAggrlsaadvaaaaSGGDTAALELIRRGGRHT 316
Cdd:cd24059  164 TSIDINGPRCSCGNRGCLELYASIPAIEKKARSALGSGRSFQLDIVEAL-------------QKGDPIADEVIEEAAKYL 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLFS 391
Cdd:cd24059  231 GIGLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAAALVLNKYFE 305
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
77-390 3.46e-63

ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; CYANR acts as transcriptional repressor of cyclobis-(1-6)-alpha-nigerosyl (CNN) degrading enzymes. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466923 [Multi-domain]  Cd Length: 304  Bit Score: 204.71  E-value: 3.46e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREgPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:cd24073    3 VVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGD-PEAVAEAIAEAVAELlaQAGLSPDRLLGIGVGLPGLVDAETGICR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:cd24073   82 WSPLL-GWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAggrlsaadvaaaASGGDTAALELIRRGGR 314
Cdd:cd24073  161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGLRGEPLTIEDLLAA------------ARAGDPAARAILRRAGR 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498326674 315 HTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLF 390
Cdd:cd24073  229 ALGLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFPGLASDLELVIHPWGDEAWARGAAALALQEFF 304
ASKHA_NBD_ROK_SgGLK-like cd24061
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ...
78-384 4.11e-60

nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466911 [Multi-domain]  Cd Length: 306  Bit Score: 196.81  E-value: 4.11e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVreGPVAVFEQVLDMAEklkasGLAEGFD--GAGIGVPGPVRFPEGIPVA 155
Cdd:cd24061    2 IGVDIGGTKIAAGVVDEEGEILATERVPTPP--TADGIVDAIVEAVE-----ELREGHDvsAVGVAAAGFVDADRATVLF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPgWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24061   75 APNIA-WRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVARE-GRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRRGGR 314
Cdd:cd24061  154 HIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANAtPEGAAVLLADGSVDGITGKHISEAARAGDPVALDALRELAR 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498326674 315 HTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTqVYRQSLPlATGNLP---IVLGELGPAAGVIGGARL 384
Cdd:cd24061  234 WLGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIRE-AFERWLP-GRGWRPiprLRTAQLGNDAGLIGAADL 304
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
78-392 1.38e-59

ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]


Pssm-ID: 273246 [Multi-domain]  Cd Length: 318  Bit Score: 195.89  E-value: 1.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674   78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAV-----FEQVLDMAEKLKASGLaegfdGAGIGVPGPVRFPEGI 152
Cdd:TIGR00744   1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDaiasaVDSFIQHIAKVGHEIV-----AIGIGAPGPVNRQRGT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  153 PVAPPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:TIGR00744  76 VYFAVNL-DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  233 DIGHIQVEPDG-LPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRR 311
Cdd:TIGR00744 155 EIGHIRMVPDGrLLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYRE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  312 GGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLFS 391
Cdd:TIGR00744 235 VARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGAADLARTYIIE 314

                  .
gi 498326674  392 P 392
Cdd:TIGR00744 315 P 315
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
78-384 5.63e-56

ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.


Pssm-ID: 395384 [Multi-domain]  Cd Length: 292  Bit Score: 185.62  E-value: 5.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674   78 LGVDIGATSVDVAVTNAELEVLGHI---TQPMDVREGPVAVFEQVLDMAEklkasGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:pfam00480   1 IGIDIGGTKIAAALFDEEGEILARErvpTPTTTTEETLVDAIAFFVDSAQ-----RKFGELIAVGIGSPGLISPKYGYIT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  155 APPiMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:pfam00480  76 NTP-NIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAR--EGRSAELAARLeaggrlsaadvaaaasgGDTAALELIRRG 312
Cdd:pfam00480 155 GHIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQKGEdlEGKDIIVLAEQ-----------------GDEVAEEAVERL 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498326674  313 GRHTGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAAIRTQVYRQSL-PLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:pfam00480 218 ARYLAKAIANLINLFDPQAIVLGGGV-SNADGLLEAIRSLVKKYLNgYLPVPPVIIVAASLGDNAGALGAAAL 289
ASKHA_NBD_ROK_TtHK-like cd24065
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ...
78-382 9.57e-56

nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; HK (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). Thermus thermophilus HK possesses significant enzymatic activity against glucose and mannose. However, it shows little catalytic capacity for galactose and fructose. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466915 [Multi-domain]  Cd Length: 289  Bit Score: 184.84  E-value: 9.57e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAElEVLGHITQPMDvREGPVAVFEQVLDMAEKLKASglAEGFDGAGIGVPGPVRFPEGIPVAPP 157
Cdd:cd24065    3 IGLDLGGTKIAAGVVDGG-RILSRLVVPTP-REGGEAVLDALARAVEALQAE--APGVEAVGLGVPGPLDFRRGRVRFAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 158 IMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGHI 237
Cdd:cd24065   79 NIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 238 QVEPDGLPCACGNQGCLEAHFSGSALARDAEQV-AREGRSAELAARLEAggrlsaadvaaaasgGDTAALELIRRGGRHT 316
Cdd:cd24065  159 TVLPGGPMCGCGLVGCLEALASGRALARDASFAyGRPMSTAELFELAQQ---------------GEPKALRIVEQAAAHL 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGnlPIVLGELGPAAGVIGGA 382
Cdd:cd24065  224 GIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARRYTEGWHAP--PLRLAHLGTDAGVIGAA 287
ASKHA_ATPase_ROK_Lmo0178-like cd24071
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ...
77-390 3.52e-55

ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Listeria monocytogenes Lmo0178 protein, which is a predicted transcription repressor belonging to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466921 [Multi-domain]  Cd Length: 312  Bit Score: 184.03  E-value: 3.52e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL-KASGLAEGFDGAGIGVPGPVRFPEGIPVA 155
Cdd:cd24071    3 IIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIKKLiKNKHVEKKLLGIGIAVSGLVDSKKGIVIR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24071   83 STIL-GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAElaarLEAGGRLSAADVAAAASGGDTAALELIRRGGRH 315
Cdd:cd24071  162 HMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLSL----LKELEDFEIEKVREAAEEGDSVATELFKKAGEY 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 316 TGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLF 390
Cdd:cd24071  238 LGIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALLVIDHLF 312
ASKHA_NBD_ROK_TmGLK-like cd24064
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ...
78-382 1.58e-49

nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466914 [Multi-domain]  Cd Length: 301  Bit Score: 169.21  E-value: 1.58e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVldmAEKLKASGLAEGFDGAGIGVPGPVRFPEGIPVAPP 157
Cdd:cd24064    2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRI---AETVNELIEEMELLGIGIGSPGSIDRENGIVRFSP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 158 IMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGHI 237
Cdd:cd24064   79 NFPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 238 QVEPDGLPCACGNQGCLEAHFSGSALARdaeqVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRRGGRHTG 317
Cdd:cd24064  159 IVEPNGPICGCGNRGCVEAFASATAIIR----YARESRKRYPDSLAGESEKINAKHVFDAARKNDPLATMVFRRVVDALA 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 318 QVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGA 382
Cdd:cd24064  235 IAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVEDAGILGAA 299
ASKHA_NBD_ROK_ApGLK-like cd24063
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ...
76-384 7.85e-46

nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466913 [Multi-domain]  Cd Length: 308  Bit Score: 159.81  E-value: 7.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  76 RFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKLKASGLAEGFDGAGIGVPGPVRFPEGIPVA 155
Cdd:cd24063    1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIETLLSKAGKDSIEGIGVSSAGPLDLRKGTIVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPGWDgFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24063   81 SPNIKGKE-IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPD-GLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGR-LSAADVAAAASGGDTAALELIRRGG 313
Cdd:cd24063  160 HLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTSLKLRNPGGEgITAKEVFSAARKGDPLALKIIEKLA 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498326674 314 RHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSlplATGNLP-IVLGELGPAAGVIGGARL 384
Cdd:cd24063  240 RYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEKNP---AISKGPeIVLSELGDDVGLIGALAL 308
ASKHA_NBD_ROK_AlsK cd24070
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ...
76-382 5.70e-42

nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1.55), also called allokinase, catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. It has also low level glucokinase activity in vitro. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466920 [Multi-domain]  Cd Length: 293  Bit Score: 148.85  E-value: 5.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  76 RFLGVDIGATSVDVAVTNAELEVLG---HITQPMDVREGPVAVFEQVLDmaEKLKASGLAegFDGAGIGVPGPVRFPEGI 152
Cdd:cd24070    2 YVLGIDIGGTNIRIGLVDEDGKLLDfekVPSKDLLRAGDPVEVLADLIR--EYIEEAGLK--PAAIVIGVPGTVDKDRRT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24070   78 VISTPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARleaggrlsaadvaaaasGGDTAAL-ELIrr 311
Cdd:cd24070  158 ELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEEHYPDTPILDIFVD-----------------HGDEPELdEFV-- 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 312 ggRHTGQVIAGLVSFFNPGLVVIGGGVTGLG----HTLLAAIRTQVyRQSLPLatGNLPIVLGELGPAAGVIGGA 382
Cdd:cd24070  219 --EDLALAIATEINILDPDAVILGGGVIDMKgfprETLEEYIRKHL-RKPYPA--DNLKIIYAELGPEAGVIGAA 288
ASKHA_ATPase_ROK_YphH-like cd24072
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ...
78-353 1.06e-41

ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YphH that belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466922 [Multi-domain]  Cd Length: 308  Bit Score: 148.72  E-value: 1.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLD-MAEKLKASglAEGFDGAGIGVPGPVRFPEGIPVAP 156
Cdd:cd24072    4 LGIVVSPNSLRAQVGNACGELLGEFEYRVITLETPEALIDEIIDcIDRLLKLW--KDRVKGIALAIQGLVDSHKGVSLWS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPgWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd24072   82 PGAP-WRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVaaaasgGDTAALELIRRGGRHT 316
Cdd:cd24072  161 TKVNPDGARCDCGRRGCLETVASNSALKRNARVTLKLGPVSADPEKLTMEQLIEALEE------GEPIATQIFDRAANAI 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQV 353
Cdd:cd24072  235 GRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAI 271
ASKHA_ATPase_ROK_NagC cd24075
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ...
75-374 2.66e-41

ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as a repressor of the nagEBACD operon involved in the uptake and degradation of the amino sugars, N-acetyl-D-glucosamine (GlcNAc) and glucosamine (GlcN). It acts both as an activator and a repressor for the transcription of the glmSU operon, encoding proteins necessary for the synthesis of GlcN (glmS) and the formation of UDP-GlcNAc (glmU). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466925 [Multi-domain]  Cd Length: 315  Bit Score: 147.90  E-value: 2.66e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  75 LRFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREgPVAVFEQVLDMAEKLKASGLAEGFDGAGIGV--PGPVRFPEGI 152
Cdd:cd24075    1 FHILAVRLGRHDLTLGLYDLSGELLAEHTVPLTALN-QEALLSQLIEEIAQFLKSHRRKTQRLIAISItlPGLINPKTGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPIMPGWDgFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24075   80 VHYMPHIQVKS-WPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARleaggRLSAADVAAAASGGDTAALELIRRG 312
Cdd:cd24075  159 EIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQGYASQLTLQ-----DCTIKDICQAALNGDQLAQDVIKRA 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498326674 313 GRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGP 374
Cdd:cd24075  234 GRYLGKVIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQALPDFRQELKIVASQLDH 295
ASKHA_NBD_ROK_GNE cd24060
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ...
78-384 7.24e-41

nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.


Pssm-ID: 466910 [Multi-domain]  Cd Length: 305  Bit Score: 146.41  E-value: 7.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVLGHITQPM-DVREGPVAVFEQVLDMAEKlKASGLAEGFDGAGIGVPGPVRFPEGIPV-A 155
Cdd:cd24060    3 LAVDLGGTNLRVAIVSMKGEIVKKYTQPNpKTYEERIDLILQMCVEAAS-EAVKLNCRILGVGISTGGRVNPREGIVLhS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24060   82 TKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRRGGRH 315
Cdd:cd24060  162 HIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGTA 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498326674 316 TGQVIAGLVSFFNPGLVVIGGGVTGLGhtlLAAIRTQVYRQSLPlATGNLPIVLGELGPAAgVIGGARL 384
Cdd:cd24060  242 LGLGIVNILHTLNPSLVILSGVLASHY---ENIVKDVIAQRALP-SVQNVDVVVSDLVDPA-LLGAASM 305
ASKHA_ATPase_ROK_Mlc cd24074
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ...
159-391 7.91e-37

ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466924 [Multi-domain]  Cd Length: 322  Bit Score: 136.29  E-value: 7.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 159 MPGWD--GFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd24074   84 LPFYDikNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGH 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARleaggRLSAADVAAAASGGDTAALELIRRGGRHT 316
Cdd:cd24074  164 TQIDPYGKRCYCGNHGCLETVASIPAILEQANQLLEQSPDSMLHGQ-----PISIESLCQAALAGDPLAQDIIIQVGRHL 238
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGpAAGVIGGARLISDHLFS 391
Cdd:cd24074  239 GRILAILVNLFNPEKILIGSPLNNAAEILFPALSQSIRQQSLPAYSQHLQIESTKFY-NDGTMPGAALIKDALYD 312
ASKHA_ATPase_ROK_SaXylR-like cd24077
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ...
77-370 1.35e-29

ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Staphylococcus aureus xylose repressor (SaXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. SaXylR acts as a transcriptional repressor of xylose-utilizing enzymes. It lacks the cysteine-rich zinc-binding motif, which presents in other family members.


Pssm-ID: 466927 [Multi-domain]  Cd Length: 295  Bit Score: 116.10  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREgPVAVFEQVLDMAEKLKAS------GLAegfdGAGIGVPGPVrFPE 150
Cdd:cd24077    3 SIGIDLGYNYISLMLTYLDGEIISSKQIKLLDIS-FENILEILKSIIQELISQapktpyGLV----GIGIGIHGIV-DEN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 151 GIPVAPPIMpgWDGFPVREALSQELGCPVMVDNDVNLMAMGEQhaGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGS 230
Cdd:cd24077   77 EIIFTPYYD--LEDIDLKEKLEEKFNVPVYLENEANLSALAER--TFSEDYDNLISISIHSGIGAGIIINNQLYRGYNGF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 231 AGDIGHIQVEPDGLPCACGNQGCLEAHFSGSALARD-AEQVAREG-RSAELAARLEAggrlsaadvaaaasgGDTAALEL 308
Cdd:cd24077  153 AGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKElSEKKGLETlTFDDLIQLYNE---------------GDPEALEL 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498326674 309 IRRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQV------YRQSLPLATGNLPIVLG 370
Cdd:cd24077  218 IDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELLEKIKEQLsssfnkYVEILISTLGKNATLLG 285
ASKHA_NBD_ROK_NAGK cd24057
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
79-384 1.39e-29

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called GlcNAc kinase, catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466907 [Multi-domain]  Cd Length: 298  Bit Score: 115.79  E-value: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  79 GVDIGATSVDVAVTNAELEVLGHITQPMDVREGPvAVFEQVLDMAEKLKASGLAEGfdGAGIGVPGPVRFPEGIPVAPPI 158
Cdd:cd24057    4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYA-AFLAAIAELVAEADARFGVKG--PVGIGIPGVIDPEDGTLITANI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 159 mPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH-- 236
Cdd:cd24057   81 -PAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHgp 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 ----IQVEPDGLP---CACGNQGCLEAHFSGSALARDAEQVAREGRSA-ELAARLEAggrlsaadvaaaasgGDTAALEL 308
Cdd:cd24057  160 lpadALLLGYDLPvlrCGCGQTGCLETYLSGRGLERLYAHLYGEELDApEIIAAWAA---------------GDPQAVAH 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498326674 309 IRRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGhTLLAAIRTQVYRQSLPLATgnLP-IVLGELGPAAGVIGGARL 384
Cdd:cd24057  225 VDRWLDLLAGCLANILTALDPDVVVLGGGLSNFP-ALIAELPAALPAHLLSGAR--TPrIVPARHGDAGGVRGAAFL 298
ASKHA_NBD_ROK_EcNanK-like cd24069
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ...
78-384 1.54e-29

nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar proteins; N-acetylmannosamine kinase (NanK; EC 2.7.1.60), also called ManNAc kinase, or N-acetyl-D-mannosamine kinase, catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. It has also low level glucokinase activity in vitro. This subfamily also contains Brucella melitensis bifunctional enzyme NanE/NanK (EC 5.1.3.9/EC 2.7.1.60), which also converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466919 [Multi-domain]  Cd Length: 283  Bit Score: 115.46  E-value: 1.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVA-VTNAELEVLGHITQPmdvREGPVAVFEQVLdmaeKLKASGLAEGFDGAGIGVPGPVRFPEGIPVAP 156
Cdd:cd24069    1 LAIDIGGTKIAAAlIGNGQIIDRRQIPTP---RSGTPEALADAL----ASLLADYQGQFDRVAVASTGIIRDGVLTALNP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd24069   74 KNLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGH 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSA-ELAARleaggrlsaadvaaaASGGDTAALELIRRGGRH 315
Cdd:cd24069  154 TLADPPGPVCGCGRRGCVEAIASGTAIAAAASEILGEPVDAkDVFER---------------ARSGDEEAARLIDRAARA 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498326674 316 TGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAAIRTqvYRQSLPlATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd24069  219 LADLIADLKATLDLDCVVIGGSV-GLAEGFLERVEQ--YLADEP-AIFRVSLEPARLGQDAGLLGAALL 283
PRK09698 PRK09698
D-allose kinase; Provisional
76-393 8.66e-29

D-allose kinase; Provisional


Pssm-ID: 182034 [Multi-domain]  Cd Length: 302  Bit Score: 113.92  E-value: 8.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  76 RFLGVDIGATSVDVAVTNAELEVLGHITQP-MDVREGPVA------VFEQVLDMAEKLKasglaegfdGAGIGVPGPVRF 148
Cdd:PRK09698   5 VVLGIDMGGTHIRFCLVDAEGEILHCEKKRtAEVIAPDLVsglgemIDEYLRRFNARCH---------GIVMGFPALVSK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 149 PEGIPVAPPIMP--GWDGFPVREALSQELGCPVMVDNDVNLMAMGE--QHAGVARTArdfLCVKIGTGIGCGIVVGSTVY 224
Cdd:PRK09698  76 DRRTVISTPNLPltALDLYDLADKLENTLNCPVFFSRDVNLQLLWDvkENNLTQQLV---LGAYLGTGMGFAVWMNGAPW 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 225 RGTTGSAGDIGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVARegrsaelaarleaggrlsaadvaaaasggDTA 304
Cdd:PRK09698 153 TGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQQPR-----------------------------DYP 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 305 ALELIRRGGRH---------TGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSL-PLATGNLPIVLGELGP 374
Cdd:PRK09698 204 LSDLFVHAGDHpfiqsllenLARAIATSINLFDPDAIILGGGVMDMPAFPRETLIAMIQKYLRkPLPYEVVRFIYASSSD 283
                        330
                 ....*....|....*....
gi 498326674 375 AAGVIGGARLISDHLFSPA 393
Cdd:PRK09698 284 FNGAQGAAILAHQRFLPQS 302
ASKHA_NBD_ROK_EcFRK-like cd24066
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ...
78-384 5.01e-28

nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; Escherichia coli FRK (EC 2.7.1.4), also called D-fructose kinase, manno(fructo)kinase, or MAK, catalyzes the phosphorylation of fructose to fructose-6-phosphate. It has also low level glucokinase activity in vitro. It is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466916 [Multi-domain]  Cd Length: 294  Bit Score: 111.53  E-value: 5.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVLGHITQPMDvREGPVAVFEQVLDMAEKLKASGLAEGfdGAGIGVPGPVrfpegipvAPP 157
Cdd:cd24066    2 IGIDLGGTKIEGIALDRAGRELLRRRVPTP-RGDYEATLDAIADLVEEAEEELGAPA--TVGIGTPGSI--------SPR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 158 IMPGWD-------GFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGS 230
Cdd:cd24066   71 TGLVKNanstwlnGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 231 AGDIGHIQVEP------DGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSA-ELAARLEAggrlsaadvaaaasgGDT 303
Cdd:cd24066  151 AGEWGHNPLPWpdedelPGPPCYCGKRGCVETFLSGPALERDYARLTGKTLSAeEIVALARA---------------GDA 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 304 AALELIRRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHtLLAAIRTQVYRQ--SLPLATgnlPIVLGELGPAAGVIGG 381
Cdd:cd24066  216 AAVATLDRFLDRLGRALANVINILDPDVIVLGGGLSNIDE-LYTEGPAALARYvfSDEVET---PIVKNKHGDSSGVRGA 291

                 ...
gi 498326674 382 ARL 384
Cdd:cd24066  292 AWL 294
ASKHA_NBD_ROK_BsFRK-like cd24067
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ...
77-384 1.32e-23

nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; Bacillus subtilis FRK (EC 2.7.1.4), also called glucomannan utilization protein E, catalyzes the phosphorylation of fructose to fructose-6-P. It seems to be involved in the degradation of glucomannan. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466917 [Multi-domain]  Cd Length: 285  Bit Score: 99.16  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVregPVAVFEQVLDMAEKLKASglaegFDGAGIGVPGPVRFPEG----- 151
Cdd:cd24067    1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPTTT---PEETLQAVIDFFREQEEP-----IDAIGIASFGPIDLNPTsptyg 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 152 -IPVAPPimPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGS 230
Cdd:cd24067   73 yITTTPK--PGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLHP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 231 AGdiGHIQVEPDglPCACGNQG-------CLEAHFSGSALArdaeqvAREGRSAELAArleaggrlsaadvaaaasgGDT 303
Cdd:cd24067  151 EM--GHIRVPRH--PDDDGFPGvcpfhgdCLEGLASGPAIA------ARWGIPAEELP-------------------DDH 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 304 AALELIrrgGRHTGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAAIRTQVYRQ-----SLPLATGNLP--IVLGELGPAA 376
Cdd:cd24067  202 PAWDLE---AYYLAQACANLTLTLSPERIVLGGGV-MQRPGLFPRIREKFRKLlngylEVPRLLPDIDeyIVPPALGNDA 277

                 ....*...
gi 498326674 377 GVIGGARL 384
Cdd:cd24067  278 GILGALAL 285
PRK13310 PRK13310
N-acetyl-D-glucosamine kinase; Provisional
79-384 3.89e-22

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 183967 [Multi-domain]  Cd Length: 303  Bit Score: 95.44  E-value: 3.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  79 GVDIGATSVDVAVTNAELEVLGHITQPMdvregPVAVFEQVLDMAEKLKASGLAEgFDGAG---IGVPGPVRFPEGIPVA 155
Cdd:PRK13310   4 GFDIGGTKIELGVFNEKLELQWEERVPT-----PRDSYDAFLDAVCELVAEADQR-FGCKGsvgIGIPGMPETEDGTLYA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPImPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:PRK13310  78 ANV-PAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGL----------PCACGNQGCLEAHFSGSALARDAEQVAREGRSA-ELAARLEAggrlsaadvaaaasgGDTA 304
Cdd:PRK13310 157 HMRLPVDALtllgwdaplrRCGCGQKGCIENYLSGRGFEWLYQHYYGEPLQApEIIALYYQ---------------GDEQ 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 305 ALELIRRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTllaairTQVYRQSLP---LATGNLP-IVLGELGPAAGVIG 380
Cdd:PRK13310 222 AVAHVERYLDLLAICLGNILTIVDPHLVVLGGGLSNFDAI------YEQLPKRLPrhlLPVARVPrIEKARHGDAGGVRG 295

                 ....
gi 498326674 381 GARL 384
Cdd:PRK13310 296 AAFL 299
ASKHA_NBD_ROK-like cd24152
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ...
78-339 2.89e-21

nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This subfamily is composed of uncharacterized proteins belonging to the the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.


Pssm-ID: 466988 [Multi-domain]  Cd Length: 286  Bit Score: 92.63  E-value: 2.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVL--GHITQPMDVREgpvAVFEQVLDMAEKLKasglaEGFDGAGIGVPGPVRFPEGIPVA 155
Cdd:cd24152    3 LVFDIGGTFIKYALVDENGNIIkkGKIPTPKDSLE---EFLDYIKKIIKRYD-----EEIDGIAISAPGVIDPETGIIYG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24152   75 GGALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDglpcacGNQGCLEAHF-SGSALARDAEQVARE----GRsaELAARLEAggrlsaadvaaaasgGDTAALELIR 310
Cdd:cd24152  155 YLLTDDD------DKDLLFFSGLaSMFGLVKRYNKAKGLepldGE--EIFEKYAK---------------GDEAAKKILD 211
                        250       260
                 ....*....|....*....|....*....
gi 498326674 311 RGGRHTGQVIAGLVSFFNPGLVVIGGGVT 339
Cdd:cd24152  212 EYIRNLAKLIYNIQYILDPEVIVIGGGIS 240
PRK05082 PRK05082
N-acetylmannosamine kinase; Provisional
76-389 9.35e-21

N-acetylmannosamine kinase; Provisional


Pssm-ID: 235338 [Multi-domain]  Cd Length: 291  Bit Score: 91.51  E-value: 9.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  76 RFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKLKASglaegFDGAGIGVPGPVRfpEGIPVA 155
Cdd:PRK05082   2 TTLAIDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQAQ-----ADRVAVASTGIIN--DGILTA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 --PPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAgVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGD 233
Cdd:PRK05082  75 lnPHNLGGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQA-LPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGH 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 234 IGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAggrlsaadvaaaasgGDTAALELIRRGG 313
Cdd:PRK05082 154 IGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGWLAGCDAKTIFERAGQ---------------GDEQAQALINRSA 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498326674 314 RHTGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAaiRTQVYRQSLPLATgNLPIVLGELGPAAGVIGGARLISDHL 389
Cdd:PRK05082 219 QAIARLIADLKATLDCQCVVLGGSV-GLAEGYLE--LVQAYLAQEPAIY-HVPLLAAHYRHDAGLLGAALWAQGEK 290
PRK09557 PRK09557
fructokinase; Reviewed
78-339 2.20e-19

fructokinase; Reviewed


Pssm-ID: 236565 [Multi-domain]  Cd Length: 301  Bit Score: 87.77  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVL--GHITQPMDVREGPVAVFEQVLDMAEKlkasglAEGFDGA-GIGVPGPVRFPEGipV 154
Cdd:PRK09557   3 IGIDLGGTKIEVIALDDAGEELfrKRLPTPRDDYQQTIEAIATLVDMAEQ------ATGQRGTvGVGIPGSISPYTG--L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMPGW-DGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGD 233
Cdd:PRK09557  75 VKNANSTWlNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 234 IGHIQV---EPDGL------PCACGNQGCLEAHFSGSALARDAEQVAREGRS-AELAARLEAGGRLSaadvaaaasggdT 303
Cdd:PRK09557 155 WGHNPLpwmDEDELryrnevPCYCGKQGCIETFISGTGFATDYRRLSGKALKgSEIIRLVEEGDPVA------------E 222
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 498326674 304 AALE-LIRRGGRHTGQVIaglvSFFNPGLVVIGGGVT 339
Cdd:PRK09557 223 LAFRrYEDRLAKSLAHVI----NILDPDVIVLGGGMS 255
PRK13311 PRK13311
N-acetyl-D-glucosamine kinase; Provisional
77-260 7.48e-18

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 106271 [Multi-domain]  Cd Length: 256  Bit Score: 82.38  E-value: 7.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDvREGPVAVFEQVLDMAEKLKASGLAEGfdGAGIGVPGPVRFPEGIpVAP 156
Cdd:PRK13311   2 YYGFDMGGTKIELGVFDENLQRIWHKRVPTP-REDYPQLLQILRDLTEEADTYCGVQG--SVGIGIPGLPNADDGT-VFT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:PRK13311  78 ANVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGH 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 498326674 237 IQVEPDGL----------PCACGNQGCLEAHFSG 260
Cdd:PRK13311 158 FRLPVDALdilgadiprvPCGCGHRGCIENYISG 191
ASKHA_NBD_ROK_PPGK cd24058
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ...
78-384 8.47e-13

nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK (EC 2.7.1.63/EC 2.7.1.2), also called poly(P)/ATP-glucomannokinase (GMK), poly(P) glucokinase, ATP-dependent glucokinase, or polyphosphate--glucose phosphotransferase, catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in Mycobacterium tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor. PPGK belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this family lack the cysteine-rich zinc-binding motif, which presents in other ROK families.


Pssm-ID: 466908 [Multi-domain]  Cd Length: 239  Bit Score: 67.59  E-value: 8.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREG--PVAVFEQVLDMAEKLKAsglaegFDGAGIGVPGPVRfpEGI-PV 154
Cdd:cd24058    2 LGIDIGGSGIKGAIVDTDTGELLSERIRIPTPQPatPEAVADVVAELVAHFPW------FGPVGVGFPGVVR--RGVvRT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCV-KIGTGIGCGIVVGSTVYRGTtgsagD 233
Cdd:cd24058   74 AANLDKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVLVlTLGTGIGSALFVDGHLVPNT-----E 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 234 IGHIQVepDGlpcacgnqgcleahfsgsalaRDAEQVAregrSAELAARLEAGgrlsaadvaaaasggdtaalelIRRGG 313
Cdd:cd24058  149 LGHLEI--RG---------------------KDAEERA----SLGVRAREDLG----------------------WKRWA 179
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498326674 314 RHTGQVIAGLVSFFNPGLVVIGGGVTGLghtllaairtqvYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd24058  180 KRVNKYLQYLERLFNPDLFIIGGGNSKK------------ADKFLPLLDVKTPVVPAVLRNDAGIVGAALL 238
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
77-383 1.48e-05

BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 46.41  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGHIT----QPMDVreGPVAVFEQVLDMAEK-LKASGLAEGFDGAGIGVPGpVRFPEG 151
Cdd:COG2971    3 ILGVDGGGTKTRAVLVDADGEVLGRGRaggaNPQSV--GLEEALASLREALEEaLAAAGDPADIEAVGFGLAG-AGTPED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 152 IPVappimpgwdgfpVREALSQELG-CPVMVDNDVNLMAMG--EQHAGVArtardflCVkIGTG-IGCGIVVGSTVYR-- 225
Cdd:COG2971   80 AEA------------LEAALRELFPfARVVVVNDALAALAGalGGEDGIV-------VI-AGTGsIAAGRDGDGRTARvg 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 226 ------GTTGSAGDIG-----HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARL-----EAggrl 289
Cdd:COG2971  140 gwgyllGDEGSGAWLGrealrAALRALDGRGPPTALTEAVLAEFGLDDPEELIAWVYRGPAPPADLASLaplvfEA---- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 290 saadvaaaASGGDTAALELIRRGGRHTGQVIAGLVSfFNPGLVVIGGGVTGLGHTLLAAIRTQvyrqslpLATGNLPIVL 369
Cdd:COG2971  216 --------AEAGDPVARAILEEAADELAELARALLE-RGALPVVLAGGVAAAQPLLREALRAR-------LAAGGAEIVP 279
                        330
                 ....*....|....
gi 498326674 370 GELGPAAGVIGGAR 383
Cdd:COG2971  280 PAGDPVDGALLLAL 293
ASKHA_NBD_eukNAGK-like cd24007
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ...
77-376 6.65e-03

nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) 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: 466857 [Multi-domain]  Cd Length: 295  Bit Score: 38.05  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674  77 FLGVDIGATSVDVAVTNAELEVLGH-ITQPMDVREGPVAVFEQVLDMA--EKLKASGLAEGFDGAGIGvpgpvrfpegip 153
Cdd:cd24007    1 VLGVDGGGTKTRAVLADEDGKILGRgKGGPSNPASVGIEEAKENLKEAvrEALSQAGSLGEIDAICLG------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 154 vappiMPGWDGFPVREALSQEL-----GCPVMVDNDVNLMamgeqHAGVARTARDFLCVkIGTG-IGCGIVVGSTVYR-- 225
Cdd:cd24007   69 -----LAGIDSEEDRERLRSALkelflSGRIIIVNDAEIA-----LAAALGGGPGIVVI-AGTGsVAYGRNGDGEEARvg 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 226 ------GTTGSAGDIGH-----IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARL-----EAggrl 289
Cdd:cd24007  138 gwghllGDEGSGYWIGRralraALRALDGRGPKTPLLDAILKFLGLDSIEELITAIYRSSDRKKEIASLaplvfEA---- 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 290 saadvaaaASGGDTAALELIRRGGRHTGQVIAGLVS---FFNPGLVVIGGGVtGLGHTLLAAIRTQVYRQSLPLATGNLP 366
Cdd:cd24007  214 --------AEEGDPVAQAILKEAAEELAKLVVALAKlllLGEKLPLALSGGV-FKNNYYLAEFLEELLKKKKPNAKVVEP 284
                        330
                 ....*....|
gi 498326674 367 IVLGELGPAA 376
Cdd:cd24007  285 KGSPVVGALL 294
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
12-52 7.04e-03

DNA-binding transcriptional regulator, Lrp family [Transcription];


Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 36.68  E-value: 7.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 498326674  12 RLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLV 52
Cdd:COG1522    9 RILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVI 49
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
10-73 7.04e-03

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 36.49  E-value: 7.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498326674  10 QARLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLVVadgLAASRGGRRSHNIRLAP 73
Cdd:COG1846   40 QFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVE---REPDPEDRRAVLVRLTE 100
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
12-52 8.59e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 33.95  E-value: 8.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 498326674   12 RLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLV 52
Cdd:pfam13412   5 KILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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