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Conserved domains on  [gi|489106560|ref|WP_003016421|]
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ROK family protein [Francisella tularensis]

Protein Classification

ROK family protein( domain architecture ID 11449187)

ROK (Repressor, ORF, Kinase) family protein functions as a sugar kinase or may act as a transcriptional regulator involved in carbohydrate-dependent transcriptional control

CATH:  3.30.420.40
Gene Ontology:  GO:0005524
PubMed:  20512568|17979299
SCOP:  3000092|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 ...
12-289 2.48e-51

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: 170.85  E-value: 2.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRV--CGEnLLDSYlsKIPPDAEHNAQSVIDVVINTIAKVFT------SEVEGIGVGISSVADREKG 83
Cdd:COG1940    7 VIGIDIGGTKIKAALVdlDGE-VLARE--RIPTPAGAGPEAVLEAIAELIEELLAeagisrGRILGIGIGVPGPVDPETG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  84 IVYDVQNIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGA 163
Cdd:COG1940   84 VVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 164 GEFGMLPYLD----------GILEDYCSGQFFIKKIG-------VEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIM 226
Cdd:COG1940  164 GEIGHMPVDPdgplcgcgnrGCLETYASGPALLRRARelggaekLTAEELFAAARAGDPLALEVLDEAARYLGIGLANLI 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489106560 227 YTLDPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAAAVYLD 289
Cdd:COG1940  244 NLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALALE 306
 
Name Accession Description Interval E-value
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
12-289 2.48e-51

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: 170.85  E-value: 2.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRV--CGEnLLDSYlsKIPPDAEHNAQSVIDVVINTIAKVFT------SEVEGIGVGISSVADREKG 83
Cdd:COG1940    7 VIGIDIGGTKIKAALVdlDGE-VLARE--RIPTPAGAGPEAVLEAIAELIEELLAeagisrGRILGIGIGVPGPVDPETG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  84 IVYDVQNIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGA 163
Cdd:COG1940   84 VVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 164 GEFGMLPYLD----------GILEDYCSGQFFIKKIG-------VEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIM 226
Cdd:COG1940  164 GEIGHMPVDPdgplcgcgnrGCLETYASGPALLRRARelggaekLTAEELFAAARAGDPLALEVLDEAARYLGIGLANLI 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489106560 227 YTLDPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAAAVYLD 289
Cdd:COG1940  244 NLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALALE 306
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
12-233 7.87e-40

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: 140.77  E-value: 7.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRVCGENLLdSYLSKIPPDAEHNAQSVIDVVINTIAKVFTS-EVEGIGVGISSVADREKG-IVYDVQ 89
Cdd:cd24068    2 ILGIDIGGTKIKYGLVDADGEI-LEKDSVPTPASKGGDAILERLLEIIAELKEKyDIEGIGISSAGQVDPKTGeVIYATD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  90 NIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFGML 169
Cdd:cd24068   81 NLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 170 PYLD----------GILEDYCSG-------QFFIKKIGVEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIMYTLDPE 232
Cdd:cd24068  161 VVDPggrpcccggkGCLEQYASGtalvrrvAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPE 240

                 .
gi 489106560 233 V 233
Cdd:cd24068  241 V 241
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
13-233 7.19e-24

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: 98.18  E-value: 7.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560   13 VGVDIGGTKVNAGRVC--GENLLDSYLSKIPPDAEHNAQSVIDVVINTIAKVFtSEVEGIGVGISSVADREKGIVYDVQN 90
Cdd:pfam00480   1 IGIDIGGTKIAAALFDeeGEILARERVPTPTTTTEETLVDAIAFFVDSAQRKF-GELIAVGIGSPGLISPKYGYITNTPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560   91 IkSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFGMLP 170
Cdd:pfam00480  80 I-GWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489106560  171 YLD----------GILEDYCSGQFFIKKIG-----VEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIMYTLDPEV 233
Cdd:pfam00480 159 LDPngpkcgcgnhGCLETIASGRALEKRYQqkgedLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDPQA 236
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
13-231 1.17e-21

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: 92.66  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560   13 VGVDIGGTKVNAGrVCGENLLDSYLSKIPPDAEHNA-----QSVIDVVINTIAKVfTSEVEGIGVGISSVADREKGIVYD 87
Cdd:TIGR00744   1 IGVDIGGTTIKLG-VVDEEGNILSKWKVPTDTTPETivdaiASAVDSFIQHIAKV-GHEIVAIGIGAPGPVNRQRGTVYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560   88 VQNIkSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFG 167
Cdd:TIGR00744  79 AVNL-DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  168 ---MLPY--------LDGILEDYCSG-------QFFIKKI-------------GVEGVEILKRARNNDKDAINIYKQFGK 216
Cdd:TIGR00744 158 hirMVPDgrllcncgKQGCIETYASAtglvryaKRANAKPeraevllalgdgdGISAKHVFVAARQGDPVAVDSYREVAR 237
                         250
                  ....*....|....*
gi 489106560  217 HLGVAIKSIMYTLDP 231
Cdd:TIGR00744 238 WAGAGLADLASLFNP 252
PRK09698 PRK09698
D-allose kinase; Provisional
12-233 5.81e-10

D-allose kinase; Provisional


Pssm-ID: 182034 [Multi-domain]  Cd Length: 302  Bit Score: 58.84  E-value: 5.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVnagRVCgenLLDSYL----SKIPPDAEHNAQSV----IDVVINTIAKvFTSEVEGIGVGISSVADREKG 83
Cdd:PRK09698   6 VLGIDMGGTHI---RFC---LVDAEGeilhCEKKRTAEVIAPDLvsglGEMIDEYLRR-FNARCHGIVMGFPALVSKDRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  84 IVYDVQNIKSW-QDIH-LKEILEAEFKVPVFIDNDANCfaigQRLYgKGKQYE----NFVGITIGTGIGGGIINKGSLLK 157
Cdd:PRK09698  79 TVISTPNLPLTaLDLYdLADKLENTLNCPVFFSRDVNL----QLLW-DVKENNltqqLVLGAYLGTGMGFAVWMNGAPWT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 158 DSNCGAGEFGMLPYLD----------GILEDYCSGqFFIKKI--------GVEgvEILKRARNNDkdainIYKQFGKHLG 219
Cdd:PRK09698 154 GAHGVAGELGHIPLGDmtqhcgcgnpGCLETNCSG-MALRRWyeqqprdyPLS--DLFVHAGDHP-----FIQSLLENLA 225
                        250
                 ....*....|....
gi 489106560 220 VAIKSIMYTLDPEV 233
Cdd:PRK09698 226 RAIATSINLFDPDA 239
 
Name Accession Description Interval E-value
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
12-289 2.48e-51

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: 170.85  E-value: 2.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRV--CGEnLLDSYlsKIPPDAEHNAQSVIDVVINTIAKVFT------SEVEGIGVGISSVADREKG 83
Cdd:COG1940    7 VIGIDIGGTKIKAALVdlDGE-VLARE--RIPTPAGAGPEAVLEAIAELIEELLAeagisrGRILGIGIGVPGPVDPETG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  84 IVYDVQNIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGA 163
Cdd:COG1940   84 VVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 164 GEFGMLPYLD----------GILEDYCSGQFFIKKIG-------VEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIM 226
Cdd:COG1940  164 GEIGHMPVDPdgplcgcgnrGCLETYASGPALLRRARelggaekLTAEELFAAARAGDPLALEVLDEAARYLGIGLANLI 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489106560 227 YTLDPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAAAVYLD 289
Cdd:COG1940  244 NLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALALE 306
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
12-233 7.87e-40

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: 140.77  E-value: 7.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRVCGENLLdSYLSKIPPDAEHNAQSVIDVVINTIAKVFTS-EVEGIGVGISSVADREKG-IVYDVQ 89
Cdd:cd24068    2 ILGIDIGGTKIKYGLVDADGEI-LEKDSVPTPASKGGDAILERLLEIIAELKEKyDIEGIGISSAGQVDPKTGeVIYATD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  90 NIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFGML 169
Cdd:cd24068   81 NLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 170 PYLD----------GILEDYCSG-------QFFIKKIGVEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIMYTLDPE 232
Cdd:cd24068  161 VVDPggrpcccggkGCLEQYASGtalvrrvAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPE 240

                 .
gi 489106560 233 V 233
Cdd:cd24068  241 V 241
ASKHA_ATPase_ROK_Lmo0178-like cd24071
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ...
12-289 3.54e-36

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: 131.64  E-value: 3.54e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVnagRVCGENLLDSYLSK--IPPDAEHNAQSVIDVVINTIAKVFT-----SEVEGIGVGISSVADREKGI 84
Cdd:cd24071    3 IIGVKIEEGYL---VLALTDLKGKILEKtrIPFDHETDPEKVIELIAENIKKLIKnkhveKKLLGIGIAVSGLVDSKKGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  85 VYDvQNIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAG 164
Cdd:cd24071   80 VIR-STILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 165 EFG-MLPYLD---------GILEDYCSGQFFIKKI----------------GVEGVEILKRARNNDKDAINIYKQFGKHL 218
Cdd:cd24071  159 EIGhMTIQPDgrkcycgqkGCLEAYASFEALVNEIkeltesyplsllkeleDFEIEKVREAAEEGDSVATELFKKAGEYL 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489106560 219 GVAIKSIMYTLDPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAAAVYLD 289
Cdd:cd24071  239 GIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALLVID 309
ASKHA_NBD_ROK_TM1224-like cd24059
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ...
12-289 1.50e-33

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: 124.24  E-value: 1.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRVCGENLLDSYlSKIPPDAEHNAQSVIDVVINTIAKV-----FTSEVEGIGVGISSVADREKGIVY 86
Cdd:cd24059    3 VIGVEIGRDLLSAVLCDLSGNILAR-EKYPLDEKENPEEVLEKLYELIDRLlekenIKSKILGIGIGAPGPLDVEKGIIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  87 DVQNIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEF 166
Cdd:cd24059   82 NPPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 167 G-MLPYLDG---------ILEDYCSGQFFIKKI-------GVEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIMYTL 229
Cdd:cd24059  162 GhTSIDINGprcscgnrgCLELYASIPAIEKKArsalgsgRSFQLDIVEALQKGDPIADEVIEEAAKYLGIGLVNLINLL 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 230 DPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAAAVYLD 289
Cdd:cd24059  242 NPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAAALVLN 301
ASKHA_ATPase_ROK cd23763
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ...
13-286 2.61e-32

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: 119.49  E-value: 2.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  13 VGVDIGGTKVNAGRVCGE-NLLDSYlsKIPPDAEHNAQSVIDVVINTIAKV-----FTSEVEGIGVGISSVADREKGIVY 86
Cdd:cd23763    1 IGIDIGGTKIRAALVDLDgEILARE--RVPTPAEEGPEAVLDRIAELIEELlaeagVRERILGIGIGVPGPVDPETGIVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  87 DVQNIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENF-------------VGitigtgigggiinKG 153
Cdd:cd23763   79 FAPNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFvyitlgtgigggiII-------------DG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 154 SLLKDSNCGAGEFGMLPyldgiledycsgqffikkigvegveilkrarnndkdainIYKQFGKHLGVAIKSIMYTLDPEV 233
Cdd:cd23763  146 KLYRGANGAAGEIGHIT---------------------------------------VLEEAARYLGIGLANLINLLNPEL 186
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489106560 234 IIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAAAV 286
Cdd:cd23763  187 IVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLLGAAAL 239
ASKHA_ATPase_ROK_BsXylR-like cd24076
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ...
12-290 8.56e-28

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: 108.81  E-value: 8.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRV--CGENLLDSylsKIPPDAEHNAQSVIDVVINTIAKVFTSEVE------GIGVGISSVADREKG 83
Cdd:cd24076    3 VIGVELGVDYITVVVTdlAGEVLWRR---EVPLPASDDPDEVLAQLAALIREALAAAPDsplgilGIGVGVPGLVDSEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  84 IVYDVQNIKsWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGA 163
Cdd:cd24076   80 VVLLAPNLG-WRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 164 GEFG-MLPYLDGI---------LEDYCSGQFFIKKIGVEGV--------EILKRARNNDKDAINIYKQFGKHLGVAIKSI 225
Cdd:cd24076  159 GEIGhMTVDPDGPpcscgnrgcWETYASERALLRAAGRLGAggeplslaELVEAARAGDPAALAALEEVGEYLGIGLANL 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489106560 226 MYTLDPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAAAVYLDR 290
Cdd:cd24076  239 VNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAAALAIDH 303
ASKHA_NBD_ROK_SgGLK-like cd24061
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ...
13-232 7.27e-27

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: 106.67  E-value: 7.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  13 VGVDIGGTKVNAGRVCGE-NLLDSYLSKIPPDAEhnaqSVIDVVINTIAKVF-TSEVEGIGVGISSVADREKGIVYDVQN 90
Cdd:cd24061    2 IGVDIGGTKIAAGVVDEEgEILATERVPTPPTAD----GIVDAIVEAVEELReGHDVSAVGVAAAGFVDADRATVLFAPN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  91 IkSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFGMLP 170
Cdd:cd24061   78 I-AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 171 YL-DGIL---------EDYCSG-------------QFFIKKI--------GVEGVEILKRARNNDKDAINIYKQFGKHLG 219
Cdd:cd24061  157 VVpDGLLcgcgsrgcwEQYASGralvryakeaanaTPEGAAVlladgsvdGITGKHISEAARAGDPVALDALRELARWLG 236
                        250
                 ....*....|...
gi 489106560 220 VAIKSIMYTLDPE 232
Cdd:cd24061  237 AGLASLAALLDPE 249
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
44-290 2.59e-25

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: 102.25  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  44 AEHNAQSVIDVVINTI------AKVFTSEVEGIGVGISSVADREKGIVYDVQNIKsWQDIHLKEILEAEFKVPVFIDNDA 117
Cdd:cd24073   33 DSGDPEAVAEAIAEAVaellaqAGLSPDRLLGIGVGLPGLVDAETGICRWSPLLG-WRDVPLAELLEERLGLPVYVENDV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 118 NCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFGMLPyLD-----------GILEDYCSGQFFI 186
Cdd:cd24073  112 NALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGHTT-VDpdgppcrcgkrGCLEAYASDPAIL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 187 ---KKIGVEGV-----EILKRARNNDKDAINIYKQFGKHLGVAIKSIMYTLDPEVIIIAWSIISAREFFEKAMWDEIKTF 258
Cdd:cd24073  191 rqaREAGLRGEpltieDLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAH 270
                        250       260       270
                 ....*....|....*....|....*....|..
gi 489106560 259 AFTQSAKKIKIEWSETEGDFQVFSAAAVYLDR 290
Cdd:cd24073  271 VFPGLASDLELVIHPWGDEAWARGAAALALQE 302
ASKHA_NBD_ROK-like cd24152
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ...
11-233 4.80e-24

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: 98.41  E-value: 4.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  11 TVVGVDIGGTKVNAGRVCGE-NLLDSYLSKIPPDaehNAQSVIDVVINTIAKvFTSEVEGIGVGISSVADREKGIVYDVQ 89
Cdd:cd24152    1 KYLVFDIGGTFIKYALVDENgNIIKKGKIPTPKD---SLEEFLDYIKKIIKR-YDEEIDGIAISAPGVIDPETGIIYGGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  90 NIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFGML 169
Cdd:cd24152   77 ALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489106560 170 PYLDG-----ILEDYCSGQFFIK-------KIGVEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIMYTLDPEV 233
Cdd:cd24152  157 LTDDDdkdllFFSGLASMFGLVKrynkakgLEPLDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIYNIQYILDPEV 232
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
13-233 7.19e-24

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: 98.18  E-value: 7.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560   13 VGVDIGGTKVNAGRVC--GENLLDSYLSKIPPDAEHNAQSVIDVVINTIAKVFtSEVEGIGVGISSVADREKGIVYDVQN 90
Cdd:pfam00480   1 IGIDIGGTKIAAALFDeeGEILARERVPTPTTTTEETLVDAIAFFVDSAQRKF-GELIAVGIGSPGLISPKYGYITNTPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560   91 IkSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFGMLP 170
Cdd:pfam00480  80 I-GWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489106560  171 YLD----------GILEDYCSGQFFIKKIG-----VEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIMYTLDPEV 233
Cdd:pfam00480 159 LDPngpkcgcgnhGCLETIASGRALEKRYQqkgedLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDPQA 236
ASKHA_NBD_ROK_TmGLK-like cd24064
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ...
12-286 6.36e-22

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: 92.94  E-value: 6.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRVcGENLLDSYLSKIPPDAEHNAQSVIDVVINTIAKVF-TSEVEGIGVGISSVADREKGIVYDVQN 90
Cdd:cd24064    1 VIGIDLGGTDTKIGIV-DENGDILKKKTIDTKVENGKEDVINRIAETVNELIeEMELLGIGIGSPGSIDRENGIVRFSPN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  91 IKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSN---------- 160
Cdd:cd24064   80 FPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDgiaaelghvi 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 161 -------CGAGEFG----------MLPYLDGILEDYCSGQFFIKKiGVEGVEILKRARNNDKDAINIYKQFGKHLGVAIK 223
Cdd:cd24064  160 vepngpiCGCGNRGcveafasataIIRYARESRKRYPDSLAGESE-KINAKHVFDAARKNDPLATMVFRRVVDALAIAIG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489106560 224 SIMYTLDPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAAAV 286
Cdd:cd24064  239 GFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVEDAGILGAASI 301
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
13-231 1.17e-21

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: 92.66  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560   13 VGVDIGGTKVNAGrVCGENLLDSYLSKIPPDAEHNA-----QSVIDVVINTIAKVfTSEVEGIGVGISSVADREKGIVYD 87
Cdd:TIGR00744   1 IGVDIGGTTIKLG-VVDEEGNILSKWKVPTDTTPETivdaiASAVDSFIQHIAKV-GHEIVAIGIGAPGPVNRQRGTVYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560   88 VQNIkSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFG 167
Cdd:TIGR00744  79 AVNL-DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  168 ---MLPY--------LDGILEDYCSG-------QFFIKKI-------------GVEGVEILKRARNNDKDAINIYKQFGK 216
Cdd:TIGR00744 158 hirMVPDgrllcncgKQGCIETYASAtglvryaKRANAKPeraevllalgdgdGISAKHVFVAARQGDPVAVDSYREVAR 237
                         250
                  ....*....|....*
gi 489106560  217 HLGVAIKSIMYTLDP 231
Cdd:TIGR00744 238 WAGAGLADLASLFNP 252
ASKHA_NBD_ROK_ApGLK-like cd24063
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ...
11-233 3.53e-21

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: 91.25  E-value: 3.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  11 TVVGVDIGGTKVNAGrVCGENLLDSYLSKIPPDAEHNAQSVIDVVINTIAKVFTS----EVEGIGVGISSVADREKGIVY 86
Cdd:cd24063    1 YYVAVDIGGTWIRAG-LVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIETLLSKagkdSIEGIGVSSAGPLDLRKGTIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  87 DVQNIKSwQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEF 166
Cdd:cd24063   80 NSPNIKG-KEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 167 GMLpYLD------------GILEDYCSGQFFIK---------------------KIGVEGVEILKRARNNDKDAINIYKQ 213
Cdd:cd24063  159 GHL-VVDtesglkcgcggyGHWEAFASGRGIPRfarewaegfssrtslklrnpgGEGITAKEVFSAARKGDPLALKIIEK 237
                        250       260
                 ....*....|....*....|
gi 489106560 214 FGKHLGVAIKSIMYTLDPEV 233
Cdd:cd24063  238 LARYNGRGIANVINAYDPEL 257
ASKHA_NBD_ROK_BsGLK-like cd24062
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ...
13-284 9.38e-21

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: 90.04  E-value: 9.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  13 VGVDIGGTKVNAGRVCGENLLDSYLSkIPPDAEHNAQSVIDVVINTIAKVFT------SEVEGIGVGISSVADREKGIVY 86
Cdd:cd24062    3 VGIDVGGTTIKMAFLTQEGEIVQKWE-IPTNKLEGGENIITDIAESIQQLLEelgyskEDLIGIGVGVPGPVDVETGTVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  87 DVQNIkSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEF 166
Cdd:cd24062   82 VAVNL-GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 167 GMLPYLD-----------GILEDYCSGQfFIKKIGVEGVE---------------------ILKRARNNDKDAINIYKQF 214
Cdd:cd24062  161 GHITVNPeggapcncgktGCLETVASAT-GIVRIAREELEegkgssalrilalggeltakdVFEAAKAGDELALAVVDTV 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 215 GKHLGVAIKSIMYTLDPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKIKIEWSETEGDFQVFSAA 284
Cdd:cd24062  240 ARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAA 309
ASKHA_NBD_ROK_TtHK-like cd24065
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ...
11-233 3.23e-19

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: 85.46  E-value: 3.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  11 TVVGVDIGGTKVNAGRVCGENLLDSYLSKIPpdaehnaQSVIDVVINTIAKVFTS------EVEGIGVGISSVADREKGI 84
Cdd:cd24065    1 STIGLDLGGTKIAAGVVDGGRILSRLVVPTP-------REGGEAVLDALARAVEAlqaeapGVEAVGLGVPGPLDFRRGR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  85 VYDVQNIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAG 164
Cdd:cd24065   74 VRFAPNIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 165 EFG---MLPY-------LDGILEDYCSGQF------FIKKIGVEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSIMYT 228
Cdd:cd24065  154 EIGhttVLPGgpmcgcgLVGCLEALASGRAlardasFAYGRPMSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKA 233

                 ....*
gi 489106560 229 LDPEV 233
Cdd:cd24065  234 LDPEV 238
ASKHA_ATPase_ROK_YphH-like cd24072
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ...
12-288 4.39e-18

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: 82.46  E-value: 4.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRV--CGENLLD-SYLSKIPPDAEHNAQSVIDVVINTIAKVfTSEVEGIGVGISSVADREKGIVydv 88
Cdd:cd24072    3 VLGIVVSPNSLRAQVGnaCGELLGEfEYRVITLETPEALIDEIIDCIDRLLKLW-KDRVKGIALAIQGLVDSHKGVS--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  89 qnIKS----WQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAG 164
Cdd:cd24072   79 --LWSpgapWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 165 EFG-MLPYLDGI---------LEDYCS--------GQFF-----IKKIGVEGVEILKRA-RNNDKDAINIYKQFGKHLGV 220
Cdd:cd24072  157 EIGhTKVNPDGArcdcgrrgcLETVASnsalkrnaRVTLklgpvSADPEKLTMEQLIEAlEEGEPIATQIFDRAANAIGR 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489106560 221 AIKSIMYTLDPEVIIIAWSIISAREFFEKAMWDEIKTFAFTQSAKKI-KIEWSETEGDFQVFsAAAVYL 288
Cdd:cd24072  237 SLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAIAENPFSQHATQIgFGQLSTEQGCAQQA-LGLVYL 304
ASKHA_ATPase_ROK_SaXylR-like cd24077
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ...
42-233 1.26e-17

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: 81.05  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  42 PDAEHNAQSVIDVVINTIaKVFTSEVE-------GIGVGIssvadreKGIVYDvQNIK-----SWQDIHLKEILEAEFKV 109
Cdd:cd24077   31 KLLDISFENILEILKSII-QELISQAPktpyglvGIGIGI-------HGIVDE-NEIIftpyyDLEDIDLKEKLEEKFNV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 110 PVFIDNDANCFAIGQRLYgkGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFG-MLPYLDGI---------LEDY 179
Cdd:cd24077  102 PVYLENEANLSALAERTF--SEDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEIGhMIIVPNGKpcpcgnkgcLEQY 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489106560 180 CSG----QFFIKKIGVEGV--EILKRARN-NDKDAINIYKQFGKHLGVAIKSIMYTLDPEV 233
Cdd:cd24077  180 ASEkallKELSEKKGLETLtfDDLIQLYNeGDPEALELIDQFIKYLAIGINNIINTFNPEI 240
ASKHA_NBD_ROK_AlsK cd24070
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ...
10-233 1.01e-16

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: 78.36  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  10 RTVVGVDIGGTKVNAGRVC-GENLLDSYlsKIPPDAEHNAQSVIDVVINTIAKV---FTSEVEGIGVGISSVADREKGIV 85
Cdd:cd24070    1 KYVLGIDIGGTNIRIGLVDeDGKLLDFE--KVPSKDLLRAGDPVEVLADLIREYieeAGLKPAAIVIGVPGTVDKDRRTV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  86 YDVQNIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYE------------NFVGItigtgigggiinKG 153
Cdd:cd24070   79 ISTPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGvvlgfyigtgigNAILI------------NG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 154 SLLKDSNCGAGEFGMLPYLD----------GILEDYCSG--------QFFIKkigVEGVEILKRArnNDKDAIniyKQFG 215
Cdd:cd24070  147 KPLRGKNGVAGELGHIPVYGngkpcgcgntGCLETYASGraleeiaeEHYPD---TPILDIFVDH--GDEPEL---DEFV 218
                        250
                 ....*....|....*...
gi 489106560 216 KHLGVAIKSIMYTLDPEV 233
Cdd:cd24070  219 EDLALAIATEINILDPDA 236
ASKHA_NBD_ROK_GNE cd24060
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ...
15-232 1.27e-15

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: 75.53  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  15 VDIGGTKVNAGRVC--GEnLLDSYLSKIPPDAEHNAQSVIDVVINTIAKVFTSEVEGIGVGISS---VADREKGIVYDVQ 89
Cdd:cd24060    5 VDLGGTNLRVAIVSmkGE-IVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTggrVNPREGIVLHSTK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  90 NIKSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFGML 169
Cdd:cd24060   84 LIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELGHI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 170 PY-LD---------GILEDYCSG---QFFIKKIG------VEGVEI-----------LKRARNNDKDAINIYKQFGKHLG 219
Cdd:cd24060  164 VVsLDgpdcmcgshGCVEAYASGmalQREAKKLHdedlllVEGMSVtndeevtakhlIQAAKLGNAKAQKILRTAGTALG 243
                        250
                 ....*....|...
gi 489106560 220 VAIKSIMYTLDPE 232
Cdd:cd24060  244 LGIVNILHTLNPS 256
ASKHA_NBD_ROK_NAGK cd24057
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
14-233 6.36e-15

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: 73.42  E-value: 6.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  14 GVDIGGTKVNAGRVcGENLLDSYLSKIPPDAeHNAQSVIDVVINTIAKVF--TSEVEGIGVGISSVADREKGIVYdVQNI 91
Cdd:cd24057    4 GFDIGGTKIEFAVF-DEALQLVWTKRVPTPT-DDYAAFLAAIAELVAEADarFGVKGPVGIGIPGVIDPEDGTLI-TANI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  92 KSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYEN-------------FVGItigtgigggiinkGSLLKD 158
Cdd:cd24057   81 PAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSvfglilgtgvgggLVVN-------------GRLVGG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 159 SNCGAGEFGMLPY-------------------LDGILEDYCSGQFF------IKKIGVEGVEILKRARNNDKDAINIYKQ 213
Cdd:cd24057  148 RSGIAGEWGHGPLpadalllgydlpvlrcgcgQTGCLETYLSGRGLerlyahLYGEELDAPEIIAAWAAGDPQAVAHVDR 227
                        250       260
                 ....*....|....*....|
gi 489106560 214 FGKHLGVAIKSIMYTLDPEV 233
Cdd:cd24057  228 WLDLLAGCLANILTALDPDV 247
PRK09698 PRK09698
D-allose kinase; Provisional
12-233 5.81e-10

D-allose kinase; Provisional


Pssm-ID: 182034 [Multi-domain]  Cd Length: 302  Bit Score: 58.84  E-value: 5.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVnagRVCgenLLDSYL----SKIPPDAEHNAQSV----IDVVINTIAKvFTSEVEGIGVGISSVADREKG 83
Cdd:PRK09698   6 VLGIDMGGTHI---RFC---LVDAEGeilhCEKKRTAEVIAPDLvsglGEMIDEYLRR-FNARCHGIVMGFPALVSKDRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  84 IVYDVQNIKSW-QDIH-LKEILEAEFKVPVFIDNDANCfaigQRLYgKGKQYE----NFVGITIGTGIGGGIINKGSLLK 157
Cdd:PRK09698  79 TVISTPNLPLTaLDLYdLADKLENTLNCPVFFSRDVNL----QLLW-DVKENNltqqLVLGAYLGTGMGFAVWMNGAPWT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 158 DSNCGAGEFGMLPYLD----------GILEDYCSGqFFIKKI--------GVEgvEILKRARNNDkdainIYKQFGKHLG 219
Cdd:PRK09698 154 GAHGVAGELGHIPLGDmtqhcgcgnpGCLETNCSG-MALRRWyeqqprdyPLS--DLFVHAGDHP-----FIQSLLENLA 225
                        250
                 ....*....|....
gi 489106560 220 VAIKSIMYTLDPEV 233
Cdd:PRK09698 226 RAIATSINLFDPDA 239
ASKHA_NBD_ROK_EcNanK-like cd24069
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ...
15-221 1.26e-08

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: 54.98  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  15 VDIGGTKVNAGRVCGENLLDSylSKIPPDAEHNAQSVIDVVINTIAKvFTSEVEGIGVGISSVADreKGIVYDV--QNIK 92
Cdd:cd24069    3 IDIGGTKIAAALIGNGQIIDR--RQIPTPRSGTPEALADALASLLAD-YQGQFDRVAVASTGIIR--DGVLTALnpKNLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  93 SWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFG-MLPY 171
Cdd:cd24069   78 GLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGhTLAD 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489106560 172 LDGI---------LEDYCSGqffiKKIGVEGVEILKRArnndKDAINIYKQFGKHLGVA 221
Cdd:cd24069  158 PPGPvcgcgrrgcVEAIASG----TAIAAAASEILGEP----VDAKDVFERARSGDEEA 208
ASKHA_NBD_ROK_EcFRK-like cd24066
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ...
13-233 3.46e-08

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: 53.75  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  13 VGVDIGGTKV------NAGRVCgenlldsYLSKIPPDAEhNAQSVIDVVINTIAKV--FTSEVEGIGVGISSVADREKGI 84
Cdd:cd24066    2 IGIDLGGTKIegialdRAGREL-------LRRRVPTPRG-DYEATLDAIADLVEEAeeELGAPATVGIGTPGSISPRTGL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  85 VydvQNIKS-WQDIH-LKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCG 162
Cdd:cd24066   74 V---KNANStWLNGKpLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 163 AGEFG--MLPYLD--------------GILEDYCSGQFF----IKKIG--VEGVEILKRARNNDKDAINIYKQFGKHLGV 220
Cdd:cd24066  151 AGEWGhnPLPWPDedelpgppcycgkrGCVETFLSGPALerdyARLTGktLSAEEIVALARAGDAAAVATLDRFLDRLGR 230
                        250
                 ....*....|...
gi 489106560 221 AIKSIMYTLDPEV 233
Cdd:cd24066  231 ALANVINILDPDV 243
PRK13310 PRK13310
N-acetyl-D-glucosamine kinase; Provisional
14-233 4.89e-08

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 183967 [Multi-domain]  Cd Length: 303  Bit Score: 53.07  E-value: 4.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  14 GVDIGGTKVNAGrVCGENLLDSYLSKIPPDAEhNAQSVIDVVINTIAKVFTS-EVEG-IGVGISSVADREKGIVYDVqNI 91
Cdd:PRK13310   4 GFDIGGTKIELG-VFNEKLELQWEERVPTPRD-SYDAFLDAVCELVAEADQRfGCKGsVGIGIPGMPETEDGTLYAA-NV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  92 KSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFG--ML 169
Cdd:PRK13310  81 PAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGhmRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 170 PY--LD----------------GILEDYCSGQFF------IKKIGVEGVEILKRARNNDKDAINIYKQFGKHLGVAIKSI 225
Cdd:PRK13310 161 PVdaLTllgwdaplrrcgcgqkGCIENYLSGRGFewlyqhYYGEPLQAPEIIALYYQGDEQAVAHVERYLDLLAICLGNI 240

                 ....*...
gi 489106560 226 MYTLDPEV 233
Cdd:PRK13310 241 LTIVDPHL 248
ASKHA_NBD_ROK_PPGK cd24058
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ...
12-137 2.43e-07

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: 50.65  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  12 VVGVDIGGTKVNAGRV---CGENLLDSYLSKIPPDAEHNAqsVIDVvINTIAKVFtsEVEG-IGVGISSVADRekGIVYD 87
Cdd:cd24058    1 ILGIDIGGSGIKGAIVdtdTGELLSERIRIPTPQPATPEA--VADV-VAELVAHF--PWFGpVGVGFPGVVRR--GVVRT 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489106560  88 VQNI-KSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFV 137
Cdd:cd24058   74 AANLdKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVV 124
PRK13311 PRK13311
N-acetyl-D-glucosamine kinase; Provisional
14-167 2.07e-06

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 106271 [Multi-domain]  Cd Length: 256  Bit Score: 48.10  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  14 GVDIGGTKVNAGrVCGENLLDSYLSKIPPDAEHNAQsVIDVV--INTIAKVFTSEVEGIGVGISSVADREKGIVYdVQNI 91
Cdd:PRK13311   4 GFDMGGTKIELG-VFDENLQRIWHKRVPTPREDYPQ-LLQILrdLTEEADTYCGVQGSVGIGIPGLPNADDGTVF-TANV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489106560  92 KSWQDIHLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFG 167
Cdd:PRK13311  81 PSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFG 156
ASKHA_ATPase_ROK_Mlc cd24074
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ...
77-233 2.15e-06

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: 48.46  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  77 VADREKGIVYDVQ--NIKSWQdihLKEILEAEFKVPVFIDNDANCFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGS 154
Cdd:cd24074   73 IIDPESGIVHRLPfyDIKNLP---LGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQ 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 155 LLKDSNCGAGEFGMLPYLDGILEDYCSGQFFIKKIgVEGVEILKRARN------------------------NDKD--AI 208
Cdd:cd24074  150 LLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETV-ASIPAILEQANQlleqspdsmlhgqpisieslcqaaLAGDplAQ 228
                        170       180
                 ....*....|....*....|....*
gi 489106560 209 NIYKQFGKHLGVAIKSIMYTLDPEV 233
Cdd:cd24074  229 DIIIQVGRHLGRILAILVNLFNPEK 253
ASKHA_ATPase_ROK_NagC cd24075
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ...
45-232 6.30e-06

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: 46.98  E-value: 6.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  45 EHNAQSVIDVVINTIAKVFTS------EVEGIGVGISSVADREKGIVYDVQNIkSWQDIHLKEILEAEFKVPVFIDNDAN 118
Cdd:cd24075   34 ALNQEALLSQLIEEIAQFLKShrrktqRLIAISITLPGLINPKTGVVHYMPHI-QVKSWPIVEELEQRFNVPCFIGNDIR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560 119 CFAIGQRLYGKGKQYENFVGITIGTGIGGGIINKGSLLKDSNCGAGEFG---MLPYLD-------GILEDYCSGQFFIKK 188
Cdd:cd24075  113 SLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEIGhiqIEPLGErchcgnfGCLETVASNAAIEQR 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489106560 189 ------------IGVEGV---EILKRARNNDKDAINIYKQFGKHLGVAIKSIMYTLDPE 232
Cdd:cd24075  193 vkkllkqgyasqLTLQDCtikDICQAALNGDQLAQDVIKRAGRYLGKVIAILINLLNPQ 251
PRK09557 PRK09557
fructokinase; Reviewed
13-132 2.31e-04

fructokinase; Reviewed


Pssm-ID: 236565 [Multi-domain]  Cd Length: 301  Bit Score: 41.93  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106560  13 VGVDIGGTKVNAgrVCGENLLDSYLSKIPPDAEHNAQSVIDVVINTI--AKVFTSEVEGIGVGISSVADREKGIVydvQN 90
Cdd:PRK09557   3 IGIDLGGTKIEV--IALDDAGEELFRKRLPTPRDDYQQTIEAIATLVdmAEQATGQRGTVGVGIPGSISPYTGLV---KN 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489106560  91 IKS-W-----QDIHLKEILEAEFKVPvfidNDANCFAIGQRLYG--KGKQ 132
Cdd:PRK09557  78 ANStWlngqpLDKDLSARLNREVRLA----NDANCLAVSEAVDGaaAGKQ 123
 
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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