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Conserved domains on  [gi|2136272599|gb|UEP94294|]
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ROK family protein [Bacillus pacificus]

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
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
 4-286 8.34e-114

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: 329.90  E-value: 8.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLMGKHTISGIGISTAGIVDVNKGIVTGGVDH 83
Cdd:cd24068     2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGISSAGQVDPKTGEVIYATDN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 IPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNML 163
Cdd:cd24068    82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 164 VEG----------KPFEEIASISGLIRLVRKYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPEV 233
Cdd:cd24068   162 VDPggrpcccggkGCLEQYASGTALVRRVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2136272599 234 IVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAIYH 286
Cdd:cd24068   242 IVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAYL 294
 
Name Accession Description Interval E-value
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
 4-286 8.34e-114

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: 329.90  E-value: 8.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLMGKHTISGIGISTAGIVDVNKGIVTGGVDH 83
Cdd:cd24068     2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGISSAGQVDPKTGEVIYATDN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 IPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNML 163
Cdd:cd24068    82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 164 VEG----------KPFEEIASISGLIRLVRKYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPEV 233
Cdd:cd24068   162 VDPggrpcccggkGCLEQYASGTALVRRVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2136272599 234 IVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAIYH 286
Cdd:cd24068   242 IVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAYL 294
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
 1-289 1.19e-97

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: 289.49  E-value: 1.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   1 MKEYIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLI-----LLSKNLMGKHTISGIGISTAGIVDVNKG 75
Cdd:COG1940     4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAelieeLLAEAGISRGRILGIGIGVPGPVDPETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  76 IVTGGVdHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFS 155
Cdd:COG1940    84 VVLNAP-NLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 156 AGEWGNMLVE--------GKP--FEEIASISGLIRLVRKYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:COG1940   163 AGEIGHMPVDpdgplcgcGNRgcLETYASGPALLRRARELGGAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANL 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2136272599 226 AYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAIYHFLH 289
Cdd:COG1940   243 INLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALALE 306
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
 5-283 1.07e-48

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: 164.30  E-value: 1.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVL-KHK----TVPTEIHLGGEQIIQ-KLILLSKNlmgKHTISGIGISTAGIVDVNKGIVT 78
Cdd:TIGR00744   1 IGVDIGGTTIKLGVVDEEGNILsKWKvptdTTPETIVDAIASAVDsFIQHIAKV---GHEIVAIGIGAPGPVNRQRGTVY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  79 GGVDhiPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGE 158
Cdd:TIGR00744  78 FAVN--LDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 159 WGNMLVE---------GKP--FEEIASISGLIRLVRKY-------------KDESDWNGKKIFELYDKGDREVTQAVEVF 214
Cdd:TIGR00744 156 IGHIRMVpdgrllcncGKQgcIETYASATGLVRYAKRAnakperaevllalGDGDGISAKHVFVAARQGDPVAVDSYREV 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136272599 215 FKHLAIGISNLAYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGA 283
Cdd:TIGR00744 236 ARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGA 304
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
 5-283 1.42e-47

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: 160.58  E-value: 1.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVL--KHKTVPTEIHlggEQIIQKLILLSKNLMGKHT--ISGIGISTAGIVDVNKGIVTGg 80
Cdd:pfam00480   1 IGIDIGGTKIAAALFDEEGEILarERVPTPTTTT---EETLVDAIAFFVDSAQRKFgeLIAVGIGSPGLISPKYGYITN- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  81 vDHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWG 160
Cdd:pfam00480  77 -TPNIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 161 NMLVE--------GKP--FEEIASISGLIRLVRKYKDESDwnGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFN 230
Cdd:pfam00480 156 HIQLDpngpkcgcGNHgcLETIASGRALEKRYQQKGEDLE--GKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFD 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2136272599 231 PEVIVIGGGITDRGnEFLKEVKEEVSKYLNKEIYSN-CEIELAQNGNCAGMVGA 283
Cdd:pfam00480 234 PQAIVLGGGVSNAD-GLLEAIRSLVKKYLNGYLPVPpVIIVAASLGDNAGALGA 286
PRK13310 PRK13310
N-acetyl-D-glucosamine kinase; Provisional
 4-288 1.25e-28

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 183967 [Multi-domain]  Cd Length: 303  Bit Score: 111.23  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEiHLGGEQIIQKLILLSKNLMGKHTISG-IGISTAGIVDVNKGIVTggVD 82
Cdd:PRK13310    2 YYGFDIGGTKIELGVFNEKLELQWEERVPTP-RDSYDAFLDAVCELVAEADQRFGCKGsVGIGIPGMPETEDGTLY--AA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  83 HIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNM 162
Cdd:PRK13310   79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 163 ---------LVEGKP-----------FEEIASISGLIRLVRKYKDESdWNGKKIFELYDKGDREVTQAVEVFFKHLAIGI 222
Cdd:PRK13310  159 rlpvdaltlLGWDAPlrrcgcgqkgcIENYLSGRGFEWLYQHYYGEP-LQAPEIIALYYQGDEQAVAHVERYLDLLAICL 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136272599 223 SNLAYIFNPEVIVIGGGITDrgnefLKEVKEEVSKYLNKEIYSNCE---IELAQNGNCAGMVGAIYHFL 288
Cdd:PRK13310  238 GNILTIVDPHLVVLGGGLSN-----FDAIYEQLPKRLPRHLLPVARvprIEKARHGDAGGVRGAAFLHL 301
 
Name Accession Description Interval E-value
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
 4-286 8.34e-114

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: 329.90  E-value: 8.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLMGKHTISGIGISTAGIVDVNKGIVTGGVDH 83
Cdd:cd24068     2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGISSAGQVDPKTGEVIYATDN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 IPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNML 163
Cdd:cd24068    82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 164 VEG----------KPFEEIASISGLIRLVRKYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPEV 233
Cdd:cd24068   162 VDPggrpcccggkGCLEQYASGTALVRRVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2136272599 234 IVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAIYH 286
Cdd:cd24068   242 IVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAYL 294
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
 1-289 1.19e-97

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: 289.49  E-value: 1.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   1 MKEYIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLI-----LLSKNLMGKHTISGIGISTAGIVDVNKG 75
Cdd:COG1940     4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAelieeLLAEAGISRGRILGIGIGVPGPVDPETG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  76 IVTGGVdHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFS 155
Cdd:COG1940    84 VVLNAP-NLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 156 AGEWGNMLVE--------GKP--FEEIASISGLIRLVRKYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:COG1940   163 AGEIGHMPVDpdgplcgcGNRgcLETYASGPALLRRARELGGAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANL 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2136272599 226 AYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAIYHFLH 289
Cdd:COG1940   243 INLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALALE 306
ASKHA_ATPase_ROK cd23763
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ...
 5-285 1.46e-73

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: 225.42  E-value: 1.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLMGKH----TISGIGISTAGIVDVNKGIVTGG 80
Cdd:cd23763     1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAgvreRILGIGIGVPGPVDPETGIVLFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  81 VdHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWG 160
Cdd:cd23763    81 P-NLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 161 NMLVegkpFEEIAsisglirlvrkykdesdwngkkifelydkgdrevtqavevffKHLAIGISNLAYIFNPEVIVIGGGI 240
Cdd:cd23763   160 HITV----LEEAA------------------------------------------RYLGIGLANLINLLNPELIVLGGGV 193

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2136272599 241 TDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAIY 285
Cdd:cd23763   194 AEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLLGAAA 238
ASKHA_NBD_ROK-like cd24152
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ...
 4-286 8.29e-71

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: 220.13  E-value: 8.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTeIHLGGEQIIQKLILLSKNLMGKhtISGIGISTAGIVDVNKGIVTGGvDH 83
Cdd:cd24152     2 YLVFDIGGTFIKYALVDENGNIIKKGKIPT-PKDSLEEFLDYIKKIIKRYDEE--IDGIAISAPGVIDPETGIIYGG-GA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 IPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNML 163
Cdd:cd24152    78 LPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 164 VEGKP-----FEEIASISGLIRLVRKYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPEVIVIGG 238
Cdd:cd24152   158 TDDDDkdllfFSGLASMFGLVKRYNKAKGLEPLDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIYNIQYILDPEVIVIGG 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2136272599 239 GITDRgNEFLKEVKEEVSKYLnKEIYSN---CEIELAQNGNCAGMVGAIYH 286
Cdd:cd24152   238 GISEQ-PLFIEDLKKEVNEIL-ANRPGSipkPEIKACKFGNDANLLGALYN 286
ASKHA_NBD_ROK_BsGLK-like cd24062
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ...
 4-286 3.69e-60

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: 193.66  E-value: 3.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLI-----LLSKNLMGKHTISGIGISTAGIVDVNKGIVT 78
Cdd:cd24062     2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIITDIAesiqqLLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  79 GGVDHipGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGE 158
Cdd:cd24062    82 VAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 159 WGNMLV---EGKP--------FEEIASISGLIRLVRK-------------YKDESDWNGKKIFELYDKGDREVTQAVEVF 214
Cdd:cd24062   160 IGHITVnpeGGAPcncgktgcLETVASATGIVRIAREeleegkgssalriLALGGELTAKDVFEAAKAGDELALAVVDTV 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2136272599 215 FKHLAIGISNLAYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAIYH 286
Cdd:cd24062   240 ARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAAWL 311
ASKHA_NBD_ROK_SgGLK-like cd24061
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ...
 5-283 5.15e-59

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: 190.64  E-value: 5.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLKHKTVPTEIhlGGEQIIQKLILLSKNLMGKHTISGIGISTAGIVDVNKGIVTGGvDHI 84
Cdd:cd24061     2 IGVDIGGTKIAAGVVDEEGEILATERVPTPP--TADGIVDAIVEAVEELREGHDVSAVGVAAAGFVDADRATVLFA-PNI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  85 PgYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNMLV 164
Cdd:cd24061    79 A-WRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 165 E--GKP--------FEEIASISGLIRLVRK------------YKDESDW--NGKKIFELYDKGDREVTQAVEVFFKHLAI 220
Cdd:cd24061   158 VpdGLLcgcgsrgcWEQYASGRALVRYAKEaanatpegaavlLADGSVDgiTGKHISEAARAGDPVALDALRELARWLGA 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2136272599 221 GISNLAYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYL-NKEIYSNCEIELAQNGNCAGMVGA 283
Cdd:cd24061   238 GLASLAALLDPELFVIGGGVSDAGDLLLDPIREAFERWLpGRGWRPIPRLRTAQLGNDAGLIGA 301
ASKHA_ATPase_ROK_BsXylR-like cd24076
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ...
 5-284 4.66e-57

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: 185.46  E-value: 4.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLI-----LLSKNLMGKHTISGIGISTAGIVDVNKGIVTg 79
Cdd:cd24076     4 IGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAalireALAAAPDSPLGILGIGVGVPGLVDSEDGVVL- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  80 gvdHIP--GYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAG 157
Cdd:cd24076    83 ---LAPnlGWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 158 EWGNMLVE--GKP--------FEEIASISGLIRLV-RKYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLA 226
Cdd:cd24076   160 EIGHMTVDpdGPPcscgnrgcWETYASERALLRAAgRLGAGGEPLSLAELVEAARAGDPAALAALEEVGEYLGIGLANLV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2136272599 227 YIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAI 284
Cdd:cd24076   240 NTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAA 297
ASKHA_NBD_ROK_TmGLK-like cd24064
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ...
 5-283 4.48e-51

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: 169.98  E-value: 4.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLMGKHTISGIGISTAGIVDVNKGIVTGGvDHI 84
Cdd:cd24064     2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRIAETVNELIEEMELLGIGIGSPGSIDRENGIVRFS-PNF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  85 PGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNMLV 164
Cdd:cd24064    81 PDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVIV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 165 EGKP----------FEEIASISGLIRLVRKYKDE---------SDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:cd24064   161 EPNGpicgcgnrgcVEAFASATAIIRYARESRKRypdslagesEKINAKHVFDAARKNDPLATMVFRRVVDALAIAIGGF 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2136272599 226 AYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGA 283
Cdd:cd24064   241 VHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVEDAGILGA 298
ASKHA_NBD_ROK_TM1224-like cd24059
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ...
 4-284 5.60e-49

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: 164.68  E-value: 5.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLMGKHT----ISGIGISTAGIVDVNKGIVTG 79
Cdd:cd24059     3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRLLEKENikskILGIGIGAPGPLDVEKGIILN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  80 gVDHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEW 159
Cdd:cd24059    83 -PPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 160 GNMLVE--GKP--------FEEIASISGLIRLVRK--YKDESDWNGkkIFELYDKGDREVTQAVEVFFKHLAIGISNLAY 227
Cdd:cd24059   162 GHTSIDinGPRcscgnrgcLELYASIPAIEKKARSalGSGRSFQLD--IVEALQKGDPIADEVIEEAAKYLGIGLVNLIN 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2136272599 228 IFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAI 284
Cdd:cd24059   240 LLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAA 296
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
 5-283 1.07e-48

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: 164.30  E-value: 1.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVL-KHK----TVPTEIHLGGEQIIQ-KLILLSKNlmgKHTISGIGISTAGIVDVNKGIVT 78
Cdd:TIGR00744   1 IGVDIGGTTIKLGVVDEEGNILsKWKvptdTTPETIVDAIASAVDsFIQHIAKV---GHEIVAIGIGAPGPVNRQRGTVY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  79 GGVDhiPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGE 158
Cdd:TIGR00744  78 FAVN--LDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 159 WGNMLVE---------GKP--FEEIASISGLIRLVRKY-------------KDESDWNGKKIFELYDKGDREVTQAVEVF 214
Cdd:TIGR00744 156 IGHIRMVpdgrllcncGKQgcIETYASATGLVRYAKRAnakperaevllalGDGDGISAKHVFVAARQGDPVAVDSYREV 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136272599 215 FKHLAIGISNLAYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGA 283
Cdd:TIGR00744 236 ARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGA 304
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
 5-283 1.42e-47

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: 160.58  E-value: 1.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVL--KHKTVPTEIHlggEQIIQKLILLSKNLMGKHT--ISGIGISTAGIVDVNKGIVTGg 80
Cdd:pfam00480   1 IGIDIGGTKIAAALFDEEGEILarERVPTPTTTT---EETLVDAIAFFVDSAQRKFgeLIAVGIGSPGLISPKYGYITN- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  81 vDHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWG 160
Cdd:pfam00480  77 -TPNIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 161 NMLVE--------GKP--FEEIASISGLIRLVRKYKDESDwnGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFN 230
Cdd:pfam00480 156 HIQLDpngpkcgcGNHgcLETIASGRALEKRYQQKGEDLE--GKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFD 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2136272599 231 PEVIVIGGGITDRGnEFLKEVKEEVSKYLNKEIYSN-CEIELAQNGNCAGMVGA 283
Cdd:pfam00480 234 PQAIVLGGGVSNAD-GLLEAIRSLVKKYLNGYLPVPpVIIVAASLGDNAGALGA 286
ASKHA_ATPase_ROK_Lmo0178-like cd24071
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ...
 9-290 2.00e-45

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: 155.52  E-value: 2.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   9 IGGTQIKYGIVSETGTVLKHKTVP----TEIHLGGEQIIQKLILLSKNLMGKHTISGIGISTAGIVDVNKGIVTGGVdhI 84
Cdd:cd24071     8 IEEGYLVLALTDLKGKILEKTRIPfdheTDPEKVIELIAENIKKLIKNKHVEKKLLGIGIAVSGLVDSKKGIVIRST--I 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  85 PGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNMLV 164
Cdd:cd24071    86 LGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIGHMTI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 165 --EGKP--------FEEIASISGLIRLVRKYKDES---------DWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:cd24071   166 qpDGRKcycgqkgcLEAYASFEALVNEIKELTESYplsllkeleDFEIEKVREAAEEGDSVATELFKKAGEYLGIGIKNL 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136272599 226 AYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGAIYHFLHH 290
Cdd:cd24071   246 INIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALLVIDH 310
ASKHA_NBD_ROK_ApGLK-like cd24063
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ...
 3-283 2.34e-41

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: 144.79  E-value: 2.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   3 EYIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLM---GKHTISGIGISTAGIVDVNKGIVTG 79
Cdd:cd24063     1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIETLLskaGKDSIEGIGVSSAGPLDLRKGTIVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  80 GvDHIPGYSmIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEW 159
Cdd:cd24063    81 S-PNIKGKE-IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 160 GNMLVEGKP-----------FEEIASISGLIRLVR-----------KYKDESDWNG---KKIFELYDKGDREVTQAVEVF 214
Cdd:cd24063   159 GHLVVDTESglkcgcggyghWEAFASGRGIPRFARewaegfssrtsLKLRNPGGEGitaKEVFSAARKGDPLALKIIEKL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136272599 215 FKHLAIGISNLAYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKylNKEIYSNCEIELAQNGNCAGMVGA 283
Cdd:cd24063   239 ARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEK--NPAISKGPEIVLSELGDDVGLIGA 305
ASKHA_NBD_ROK_TtHK-like cd24065
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ...
 5-283 2.75e-41

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: 144.39  E-value: 2.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSEtGTVLKHKTVPTEIHlGGEQIIQKLILLSKNLMGKH-TISGIGISTAGIVDVNKGIVTGGvDH 83
Cdd:cd24065     3 IGLDLGGTKIAAGVVDG-GRILSRLVVPTPRE-GGEAVLDALARAVEALQAEApGVEAVGLGVPGPLDFRRGRVRFA-PN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 IPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNML 163
Cdd:cd24065    80 IPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 164 V-EGKP---------FEEIASISGLIRLVRkYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPEV 233
Cdd:cd24065   160 VlPGGPmcgcglvgcLEALASGRALARDAS-FAYGRPMSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALDPEV 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2136272599 234 IVIGGGITDRGNEFLKEVKEEVSKYLnkEIYSNCEIELAQNGNCAGMVGA 283
Cdd:cd24065   239 FVLGGGVAQVGDYYLLPVQEAARRYT--EGWHAPPLRLAHLGTDAGVIGA 286
ASKHA_ATPase_ROK_SaXylR-like cd24077
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ...
 4-288 4.69e-41

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: 143.84  E-value: 4.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTeIHLGGEQIIQKLILLSKNLMG-----KHTISGIGISTAGIVDVNKGIVT 78
Cdd:cd24077     3 SIGIDLGYNYISLMLTYLDGEIISSKQIKL-LDISFENILEILKSIIQELISqapktPYGLVGIGIGIHGIVDENEIIFT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  79 ggvdhiPGYSM--IPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREkgNFIMLTLGTGIGGAIFIDGELYRGHLFSA 156
Cdd:cd24077    82 ------PYYDLedIDLKEKLEEKFNVPVYLENEANLSALAERTFSEDYD--NLISISIHSGIGAGIIINNQLYRGYNGFA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 157 GEWGNMLVE--GKP--------FEEIASISGLIRLVRKYKDESDWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLA 226
Cdd:cd24077   154 GEIGHMIIVpnGKPcpcgnkgcLEQYASEKALLKELSEKKGLETLTFDDLIQLYNEGDPEALELIDQFIKYLAIGINNII 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2136272599 227 YIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEiysnCEIELAQNGNCAGMVGA----IYHFL 288
Cdd:cd24077   234 NTFNPEIIIINSSLINEIPELLEKIKEQLSSSFNKY----VEILISTLGKNATLLGGaavaIKNFL 295
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
 23-283 6.34e-40

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: 141.15  E-value: 6.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  23 GTVLKHKTVPTEIHlGGEQIIQKLILLSKNLMGKHT-----ISGIGISTAGIVDVNKGIVTggVDHIPGYSMIPIMNKLQ 97
Cdd:cd24073    22 GNVLASHTLPLDSG-DPEAVAEAIAEAVAELLAQAGlspdrLLGIGVGLPGLVDAETGICR--WSPLLGWRDVPLAELLE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  98 EVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNMLVE--GKP------- 168
Cdd:cd24073    99 ERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGHTTVDpdGPPcrcgkrg 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 169 -FEEIASISGLIRLVRKY---KDESDWNgkKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPEVIVIGGGITDRG 244
Cdd:cd24073   179 cLEAYASDPAILRQAREAglrGEPLTIE--DLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPELIIISGEGVRAG 256

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2136272599 245 NEFLKEVKEEVSKYLNKEIYSNCEIELAQNGNCAGMVGA 283
Cdd:cd24073   257 DLLFEPMREALRAHVFPGLASDLELVIHPWGDEAWARGA 295
ASKHA_NBD_ROK_NAGK cd24057
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
 4-283 2.32e-39

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: 139.29  E-value: 2.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGE--QIIQKLILLSKNLMGKHTisGIGISTAGIVDVNKGIVTggV 81
Cdd:cd24057     2 YYGFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAAflAAIAELVAEADARFGVKG--PVGIGIPGVIDPEDGTLI--T 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  82 DHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGN 161
Cdd:cd24057    78 ANIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 162 M-----LVEGKP--------------FEEIASISGLIRLVRKYKDEsdwnGKKIFEL---YDKGDREVTQAVEVFFKHLA 219
Cdd:cd24057   158 GplpadALLLGYdlpvlrcgcgqtgcLETYLSGRGLERLYAHLYGE----ELDAPEIiaaWAAGDPQAVAHVDRWLDLLA 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136272599 220 IGISNLAYIFNPEVIVIGGGITDrgnefLKEVKEEVSKYLNKEIYSNC---EIELAQNGNCAGMVGA 283
Cdd:cd24057   234 GCLANILTALDPDVVVLGGGLSN-----FPALIAELPAALPAHLLSGArtpRIVPARHGDAGGVRGA 295
ASKHA_NBD_ROK_GNE cd24060
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ...
 5-256 4.82e-37

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: 133.70  E-value: 4.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQ--IIQKLILLSK---NLMGKhtISGIGISTAGIVDVNKGIVTG 79
Cdd:cd24060     3 LAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIdlILQMCVEAASeavKLNCR--ILGVGISTGGRVNPREGIVLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  80 GVDHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEW 159
Cdd:cd24060    81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 160 GNMLV--EGKP--------FEEIASISGLIRLVRKYKDESD--WNGKKIfelydKGDREVT-----QA-----------V 211
Cdd:cd24060   161 GHIVVslDGPDcmcgshgcVEAYASGMALQREAKKLHDEDLllVEGMSV-----TNDEEVTakhliQAaklgnakaqkiL 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2136272599 212 EVFFKHLAIGISNLAYIFNPEVIVIGGGITDRGNEFLKEVKEEVS 256
Cdd:cd24060   236 RTAGTALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRA 280
ASKHA_ATPase_ROK_YphH-like cd24072
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ...
 5-288 1.82e-34

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: 126.76  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLkHKTVPTEIHLGGEQ-IIQKLI--LLSKNLMGKHTISGIGISTAGIVDVNKGIVTggv 81
Cdd:cd24072     4 LGIVVSPNSLRAQVGNACGELL-GEFEYRVITLETPEaLIDEIIdcIDRLLKLWKDRVKGIALAIQGLVDSHKGVSL--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  82 dHIPGYSM--IPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEW 159
Cdd:cd24072    80 -WSPGAPWrnIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 160 GNMLVE--------GKP--FEEIASISGLIR----LVRKYKDESDWNGKKIFELYDK---GDREVTQAVEVFFKHLAIGI 222
Cdd:cd24072   159 GHTKVNpdgarcdcGRRgcLETVASNSALKRnarvTLKLGPVSADPEKLTMEQLIEAleeGEPIATQIFDRAANAIGRSL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2136272599 223 SNLAYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEIYSNC-EIELAQNGNCAG-MVGAIYHFL 288
Cdd:cd24072   239 ANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAIAENPFSQHATQIgFGQLSTEQGCAQqALGLVYLYI 306
ASKHA_NBD_ROK_AlsK cd24070
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ...
 4-287 6.66e-34

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: 124.97  E-value: 6.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLMGKH--TISGIGISTAGIVDVNKGIVTGgV 81
Cdd:cd24070     3 VLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGDPVEVLADLIREYIEEAglKPAAIVIGVPGTVDKDRRTVIS-T 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  82 DHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGN 161
Cdd:cd24070    82 PNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 162 MLV--EGKP--------FEEIASISGLIRLVRKYKdeSDWNGKKIFElyDKGDREVtqaVEVFFKHLAIGISNLAYIFNP 231
Cdd:cd24070   162 IPVygNGKPcgcgntgcLETYASGRALEEIAEEHY--PDTPILDIFV--DHGDEPE---LDEFVEDLALAIATEINILDP 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2136272599 232 EVIVIGGGITDRGNEFLKEVKEEVSKYLNK-EIYSNCEIELAQNGNCAGMVGAIYHF 287
Cdd:cd24070   235 DAVILGGGVIDMKGFPRETLEEYIRKHLRKpYPADNLKIIYAELGPEAGVIGAAIYA 291
ASKHA_NBD_ROK_BsFRK-like cd24067
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ...
 4-285 1.01e-31

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: 118.80  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIhlgGEQIIQKLILLSKNLmgKHTISGIGISTAGIVDVNKGIVTGGvdH 83
Cdd:cd24067     1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPTTT---PEETLQAVIDFFREQ--EEPIDAIGIASFGPIDLNPTSPTYG--Y 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 I-----PGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSagE 158
Cdd:cd24067    74 ItttpkPGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLHP--E 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 159 WGNMLV---------EGKPF------EEIASiSGLIRlvrkykdesDWNGKKIFELYDkgDREVTqavEVFFKHLAIGIS 223
Cdd:cd24067   152 MGHIRVprhpdddgfPGVCPfhgdclEGLAS-GPAIA---------ARWGIPAEELPD--DHPAW---DLEAYYLAQACA 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136272599 224 NLAYIFNPEVIVIGGGITDRgNEFLKEVKEEVSKYLN-----KEIYSNCE--IELAQNGNCAGMVGAIY 285
Cdd:cd24067   217 NLTLTLSPERIVLGGGVMQR-PGLFPRIREKFRKLLNgylevPRLLPDIDeyIVPPALGNDAGILGALA 284
ASKHA_NBD_ROK_EcNanK-like cd24069
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ...
 5-286 3.42e-31

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: 117.38  E-value: 3.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVsETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLMGKHTIsgIGISTAGIVDvnKGIVTGGVDH- 83
Cdd:cd24069     1 LAIDIGGTKIAAALI-GNGQIIDRRQIPTPRSGTPEALADALASLLADYQGQFDR--VAVASTGIIR--DGVLTALNPKn 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 IPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNML 163
Cdd:cd24069    76 LGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 164 VEGKP----------FEEIASISGLIRLVrkykdeSDWNG-----KKIFELYDKGDREVTQAVEVFFKHLAIGISNLAYI 228
Cdd:cd24069   156 ADPPGpvcgcgrrgcVEAIASGTAIAAAA------SEILGepvdaKDVFERARSGDEEAARLIDRAARALADLIADLKAT 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 229 FNPEVIVIGGGITDrgnefLKEVKEEVSKYLNKE--IYsNCEIELAQNGNCAGMVGAIYH 286
Cdd:cd24069   230 LDLDCVVIGGSVGL-----AEGFLERVEQYLADEpaIF-RVSLEPARLGQDAGLLGAALL 283
PRK13310 PRK13310
N-acetyl-D-glucosamine kinase; Provisional
 4-288 1.25e-28

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 183967 [Multi-domain]  Cd Length: 303  Bit Score: 111.23  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEiHLGGEQIIQKLILLSKNLMGKHTISG-IGISTAGIVDVNKGIVTggVD 82
Cdd:PRK13310    2 YYGFDIGGTKIELGVFNEKLELQWEERVPTP-RDSYDAFLDAVCELVAEADQRFGCKGsVGIGIPGMPETEDGTLY--AA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  83 HIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGNM 162
Cdd:PRK13310   79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 163 ---------LVEGKP-----------FEEIASISGLIRLVRKYKDESdWNGKKIFELYDKGDREVTQAVEVFFKHLAIGI 222
Cdd:PRK13310  159 rlpvdaltlLGWDAPlrrcgcgqkgcIENYLSGRGFEWLYQHYYGEP-LQAPEIIALYYQGDEQAVAHVERYLDLLAICL 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136272599 223 SNLAYIFNPEVIVIGGGITDrgnefLKEVKEEVSKYLNKEIYSNCE---IELAQNGNCAGMVGAIYHFL 288
Cdd:PRK13310  238 GNILTIVDPHLVVLGGGLSN-----FDAIYEQLPKRLPRHLLPVARvprIEKARHGDAGGVRGAAFLHL 301
ASKHA_NBD_ROK_EcFRK-like cd24066
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ...
 5-283 2.34e-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: 110.37  E-value: 2.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLKHKTVPTEiHLGGEQIIQKLILLSKNLMGK-HTISGIGISTAGIVDVNkgivTGGVDH 83
Cdd:cd24066     2 IGIDLGGTKIEGIALDRAGRELLRRRVPTP-RGDYEATLDAIADLVEEAEEElGAPATVGIGTPGSISPR----TGLVKN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 IPGYSMI--PIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGN 161
Cdd:cd24066    77 ANSTWLNgkPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGH 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 162 MLVEGKPFEEIAS--------------ISGlIRLVRKYKDES--DWNGKKIFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:cd24066   157 NPLPWPDEDELPGppcycgkrgcvetfLSG-PALERDYARLTgkTLSAEEIVALARAGDAAAVATLDRFLDRLGRALANV 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2136272599 226 AYIFNPEVIVIGGGITDrgnefLKEVKEEVSKYLNKEIYSN-CEIELAQN--GNCAGMVGA 283
Cdd:cd24066   236 INILDPDVIVLGGGLSN-----IDELYTEGPAALARYVFSDeVETPIVKNkhGDSSGVRGA 291
ASKHA_ATPase_ROK_NagC cd24075
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ...
 5-241 8.74e-25

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: 100.90  E-value: 8.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLKHKTVPTEiHLGGEQIIQKLILLSKNLMGKHT-----ISGIGISTAGIVDVNKGIVTg 79
Cdd:cd24075     4 LAVRLGRHDLTLGLYDLSGELLAEHTVPLT-ALNQEALLSQLIEEIAQFLKSHRrktqrLIAISITLPGLINPKTGVVH- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  80 gvdHIPGYSM--IPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAG 157
Cdd:cd24075    82 ---YMPHIQVksWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 158 EWGNMLVE--GKP--------FEEIASISGLIRLVRKYKDE--------SDWNGKKIFELYDKGDREVTQAVEVFFKHLA 219
Cdd:cd24075   159 EIGHIQIEplGERchcgnfgcLETVASNAAIEQRVKKLLKQgyasqltlQDCTIKDICQAALNGDQLAQDVIKRAGRYLG 238

                         250       260
                  ....*....|....*....|..
gi 2136272599 220 IGISNLAYIFNPEVIVIGGGIT 241
Cdd:cd24075   239 KVIAILINLLNPQKIIIAGEIT 260
PRK09698 PRK09698
D-allose kinase; Provisional
 1-285 2.27e-22

D-allose kinase; Provisional


Pssm-ID: 182034 [Multi-domain]  Cd Length: 302  Bit Score: 94.28  E-value: 2.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   1 MKEYIA-FDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGeQIIQKLILLSKNLMGKH--TISGIGISTAGIVDVNKGIV 77
Cdd:PRK09698    2 QKNVVLgIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAP-DLVSGLGEMIDEYLRRFnaRCHGIVMGFPALVSKDRRTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  78 TGgVDHIP--GYSMIPIMNKLQEVLKVPVSIDNDVNCAAFgekWNGS--GREKGNFIMLTLGTGIGGAIFIDGELYRGHL 153
Cdd:PRK09698   81 IS-TPNLPltALDLYDLADKLENTLNCPVFFSRDVNLQLL---WDVKenNLTQQLVLGAYLGTGMGFAVWMNGAPWTGAH 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 154 FSAGE-----WGNMLVE---GKP--FEEIAsiSGLiRLVRKYkdESDWNGKKIFELYDKGDREvtQAVEVFFKHLAIGIS 223
Cdd:PRK09698  157 GVAGElghipLGDMTQHcgcGNPgcLETNC--SGM-ALRRWY--EQQPRDYPLSDLFVHAGDH--PFIQSLLENLARAIA 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136272599 224 NLAYIFNPEVIVIGGGITDRGNEFLKEVKEEVSKYLNKEI-YSNCEIELAQNGNCAGMVGAIY 285
Cdd:PRK09698  230 TSINLFDPDAIILGGGVMDMPAFPRETLIAMIQKYLRKPLpYEVVRFIYASSSDFNGAQGAAI 292
ASKHA_NBD_ROK_PPGK cd24058
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ...
 6-284 3.27e-21

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: 89.94  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   6 AFDIGGTQIKYGIV-SETGTVLKHK-TVPTEIHLGGEQIIQKLILLSKNLMGKHTIsGIGIStagivdvnkGIVTGGVDH 83
Cdd:cd24058     3 GIDIGGSGIKGAIVdTDTGELLSERiRIPTPQPATPEAVADVVAELVAHFPWFGPV-GVGFP---------GVVRRGVVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  84 I-----PGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGR-EKGNFIMLTLGTGIGGAIFIDGELYRgHLfsag 157
Cdd:cd24058    73 TaanldKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKgEKGVVLVLTLGTGIGSALFVDGHLVP-NT---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 158 EWGNMLVEGKPFEEIASISglirlVRKYKDESD--WNgkkifelydkgdrevtqavevffKHLAIGISNLAYIFNPEVIV 235
Cdd:cd24058   148 ELGHLEIRGKDAEERASLG-----VRAREDLGWkrWA-----------------------KRVNKYLQYLERLFNPDLFI 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2136272599 236 IGGGITDRGNEFLKEVKeevskylnkeiySNCEIELAQNGNCAGMVGAI 284
Cdd:cd24058   200 IGGGNSKKADKFLPLLD------------VKTPVVPAVLRNDAGIVGAA 236
PRK05082 PRK05082
N-acetylmannosamine kinase; Provisional
 6-283 4.40e-20

N-acetylmannosamine kinase; Provisional


Pssm-ID: 235338 [Multi-domain]  Cd Length: 291  Bit Score: 87.66  E-value: 4.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   6 AFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGEQIIQKLILLSKNLmgKHTISGIGISTAGIvdVNKGIVT------- 78
Cdd:PRK05082    5 AIDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPL--QAQADRVAVASTGI--INDGILTalnphnl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  79 GGVDHipgysmIPIMNKLQEVLKVPVSIDNDVNCAAFGEkWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGE 158
Cdd:PRK05082   81 GGLLH------FPLVQTLEQLTDLPTIALNDAQAAAWAE-YQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 159 WGNMLVEgkP------------FEEIASISGLIRLVRKYKDESDwnGKKIFELYDKGDREVTQAVEVFFKHLAIGISNLA 226
Cdd:PRK05082  154 IGHTLAD--PhgpvcgcgrrgcVEAIASGRAIAAAAQGWLAGCD--AKTIFERAGQGDEQAQALINRSAQAIARLIADLK 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2136272599 227 YIFNPEVIVIGGGItdrG--NEFLkevkEEVSKYLNK--EIYsNCEIELAQNGNCAGMVGA 283
Cdd:PRK05082  230 ATLDCQCVVLGGSV---GlaEGYL----ELVQAYLAQepAIY-HVPLLAAHYRHDAGLLGA 282
PRK09557 PRK09557
fructokinase; Reviewed
 5-283 9.59e-18

fructokinase; Reviewed


Pssm-ID: 236565 [Multi-domain]  Cd Length: 301  Bit Score: 81.23  E-value: 9.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   5 IAFDIGGTQIKYGIVSETGTVLKHKTVPT--EIHLGGEQIIQKLILLSKNLMGKHTISGIGIStaGIVDVNKGIV-TGGV 81
Cdd:PRK09557    3 IGIDLGGTKIEVIALDDAGEELFRKRLPTprDDYQQTIEAIATLVDMAEQATGQRGTVGVGIP--GSISPYTGLVkNANS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  82 DHIPGYsmiPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGN 161
Cdd:PRK09557   81 TWLNGQ---PLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWGH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 162 -----MLVE------------GKP--FEEIASISGLIRLVRKYKDESDwNGKKIFELYDKGDREVTQAVEVFFKHLAIGI 222
Cdd:PRK09557  158 nplpwMDEDelryrnevpcycGKQgcIETFISGTGFATDYRRLSGKAL-KGSEIIRLVEEGDPVAELAFRRYEDRLAKSL 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2136272599 223 SNLAYIFNPEVIVIGGGITDrgnefLKEVKEEVSKYLNKEIYSN-CEIELAQN--GNCAGMVGA 283
Cdd:PRK09557  237 AHVINILDPDVIVLGGGMSN-----VDRLYPTLPALLKQYVFGGeCETPVRKAlhGDSSGVRGA 295
PRK13311 PRK13311
N-acetyl-D-glucosamine kinase; Provisional
 4-161 2.53e-17

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 106271 [Multi-domain]  Cd Length: 256  Bit Score: 79.69  E-value: 2.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPT--EIHLGGEQIIQKLILLSKNLMGKHTISGIGIStaGIVDVNKGIVTGGv 81
Cdd:PRK13311    2 YYGFDMGGTKIELGVFDENLQRIWHKRVPTprEDYPQLLQILRDLTEEADTYCGVQGSVGIGIP--GLPNADDGTVFTA- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  82 dHIPGYSMIPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIGGAIFIDGELYRGHLFSAGEWGN 161
Cdd:PRK13311   79 -NVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGH 157
ASKHA_NBD_GLK cd24008
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ...
 4-286 5.82e-14

nucleotide-binding domain (NBD) of 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. Glucokinases are mainly found in invertebrates and microorganisms and highly specific for glucose. Glucokinases belong 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: 466858 [Multi-domain]  Cd Length: 313  Bit Score: 70.72  E-value: 5.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSET---GTVLKHKTVPTEIHLGGEQIIQKLIllskNLMGKHTISGIGISTAGIVDVNKGIVTGG 80
Cdd:cd24008     1 ILVGDIGGTNARLALADAGdgsGDLLFVRKYPSADFASLEDALAAFL----AELGAPRPKAACIAVAGPVDGGRVRLTNL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  81 VDHIPGysmipimNKLQEVLKV-PVSIDNDVNCAAFG---------EKWNGSGR--EKGNFIMLTLGTGIGGAIFIDGEL 148
Cdd:cd24008    77 DWSIDA-------AELRKALGIgRVRLLNDFEAAAYGlpalgpedlLVLYGGGGplPGGPRAVLGPGTGLGVALLVPDGD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 149 YR--------GHL-FSA-GEWGNMLVE------GKP--FEEIASISGLIR----LVRKYKDE-SDWNGKKIFELYDKGDR 205
Cdd:cd24008   150 GGyvvlpsegGHAdFAPvTEEEAELLEflrkrfGRSvsYEDVLSGPGLENiyefLAKLDGAEpPDLTAEEIAEAALAGDP 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 206 EVTQAVEVFFKHLAIGISNLAYIFNP-EVIVIGGGITDRGNEFLKE---VKEEVSKYLNKEIYSNCEIELAQNGNcAGMV 281
Cdd:cd24008   230 LAREALDLFARILGRFAGNLALSFLAtGGVYLAGGIAPKNLDLLDSsafREAFLDKGRMSDLLEDIPVYLVTNED-LGLL 308


                  ....*
gi 2136272599 282 GAIYH 286
Cdd:cd24008   309 GAAAY 313
ASKHA_ATPase_ROK_Mlc cd24074
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ...
 62-241 1.92e-12

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: 66.57  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  62 IGISTAGIVDVNKGIVtggvDHIPGYSM--IPIMNKLQEVLKVPVSIDNDVNCAAFGEKWNGSGREKGNFIMLTLGTGIG 139
Cdd:cd24074    66 IAITLPGIIDPESGIV----HRLPFYDIknLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIG 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 140 GAIFIDGELYRGHLFSAGEWGNMLVE--GKP--------FEEIASISGLIRLVR---KYKDESDWNGKKIF-----ELYD 201
Cdd:cd24074   142 AGVITDGQLLHAGSSRLGELGHTQIDpyGKRcycgnhgcLETVASIPAILEQANqllEQSPDSMLHGQPISieslcQAAL 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2136272599 202 KGDREVTQAVEVFFKHLAIGISNLAYIFNPEVIVIGGGIT 241
Cdd:cd24074   222 AGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLN 261
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
 4-68 3.61e-05

FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.


Pssm-ID: 395295 [Multi-domain]  Cd Length: 245  Bit Score: 44.25  E-value: 3.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVLKHKTVPTEIHLGGE--------QIIQKLILLSKNLMGKHTIS-----GIGISTAG 68
Cdd:pfam00370   2 YLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPgwaeqdpdEIWQAVAQCIAKTLSQLGISlkqikGIGISNQG 79
ASKHA_NBD_eukNAGK-like cd24007
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ...
 4-279 1.19e-04

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: 42.68  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   4 YIAFDIGGTQIKYGIVSETGTVL-KHKTVPTEIHLGG----EQIIQKLI-LLSKNLMGKHTISGIGISTAGIVDVN-KGI 76
Cdd:cd24007     1 VLGVDGGGTKTRAVLADEDGKILgRGKGGPSNPASVGieeaKENLKEAVrEALSQAGSLGEIDAICLGLAGIDSEEdRER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  77 VTggvdhipgysmipimNKLQEVLKV-PVSIDNDVNCAAFGekwnGSGREKGnfIMLTLGTG-IGGAIFIDGELYR---- 150
Cdd:cd24007    81 LR---------------SALKELFLSgRIIIVNDAEIALAA----ALGGGPG--IVVIAGTGsVAYGRNGDGEEARvggw 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 151 GHLF----SAGEWGNMLVEG--KPFEEIASISGLIRLVRKYKDESDWNG-------------------KKIFELYDKGDR 205
Cdd:cd24007   140 GHLLgdegSGYWIGRRALRAalRALDGRGPKTPLLDAILKFLGLDSIEElitaiyrssdrkkeiaslaPLVFEAAEEGDP 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136272599 206 EVTQAVEVFFKHLA---IGISNLAYIFNPEVIVIGGGITdRGNEFLKEVKEEvskyLNKEIYSNCEIELAQNGNCAG 279
Cdd:cd24007   220 VAQAILKEAAEELAklvVALAKLLLLGEKLPLALSGGVF-KNNYYLAEFLEE----LLKKKKPNAKVVEPKGSPVVG 291
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 2-279 5.31e-03

nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (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). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases 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: 466850 [Multi-domain]  Cd Length: 357  Bit Score: 38.03  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599   2 KEYIAFDIGGTQIKYGIVSETG-----TVLKHKTVPTEIHLGG-----EQIIQKLI-LLSKNLMGKHTISGI-------- 62
Cdd:cd24000    43 GEFLAIDLGGTNLRVALVSLDGkgievTISKKYEIPDEIKTASaeeffDFIADCIAeFLKENGLKKPLPLGFtfsfpleq 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599  63 -GISTAGIVDVNKGIVT-GGVDHIPGYSMIPIMNKLQEVLKVpVSIDNDVNCAAFGEKWngsgREKGNFIMLTLGTGIGG 140
Cdd:cd24000   123 tSLNDGKLLSWTKGFKIpGVEGKDVGELLNDALKKRGLPVKV-VAVLNDTVATLLAGAY----KDPDCRIGLILGTGTNA 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 141 AIFIdgELYRGHLFSAG-----EWGNMLVEGKPFEEIAsisglirlvRKYKDESDWNGKKIFE---------------LY 200
Cdd:cd24000   198 AYLE--PTSNILLGDGGmiintEWGNFGKNSLPRTEYD---------REVDKASENPGFQPLEkmvsgkylgelvrliLK 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136272599 201 DKGDREVTQAVEVFFKH----LAIGISNLAYIFNPE-----VIVIGGGITDRGNEFLKEVKEEVSKYLNKEIysNCEIEL 271
Cdd:cd24000   267 DLADEILRKICELVAERsarlAAAAIAALLRKTGDSpekkiTIAVDGSLFEKYPGYRERLEEYLKELLGRGI--RIELVL 344


                  ....*...
gi 2136272599 272 AQNGNCAG 279
Cdd:cd24000   345 VEDGSLIG 352
 
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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