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Conserved domains on  [gi|446588783|ref|WP_000666129|]
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MULTISPECIES: ROK family protein [Bacillus]

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 1.30e-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: 331.83  E-value: 1.30e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEHTISGIGISTAGIVDVNRGVVTGGADH 83
Cdd:cd24068    2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGISSAGQVDPKTGEVIYATDN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  84 IPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNML 163
Cdd:cd24068   82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 164 IEG----------KTFEEVASISGLIHLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPET 233
Cdd:cd24068  162 VDPggrpcccggkGCLEQYASGTALVRRVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446588783 234 IIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAIYH 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 1.30e-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: 331.83  E-value: 1.30e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEHTISGIGISTAGIVDVNRGVVTGGADH 83
Cdd:cd24068    2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGISSAGQVDPKTGEVIYATDN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  84 IPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNML 163
Cdd:cd24068   82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 164 IEG----------KTFEEVASISGLIHLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPET 233
Cdd:cd24068  162 VDPggrpcccggkGCLEQYASGTALVRRVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446588783 234 IIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAIYH 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 7.03e-98

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: 289.87  E-value: 7.03e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   1 MKEYIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLI-----LLSKKLMSEHTISGIGISTAGIVDVNRG 75
Cdd:COG1940    4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAelieeLLAEAGISRGRILGIGIGVPGPVDPETG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  76 VVTGgADHIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYS 155
Cdd:COG1940   84 VVLN-APNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 156 AGEWGNMLIE--------GKT--FEEVASISGLIHLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:COG1940  163 AGEIGHMPVDpdgplcgcGNRgcLETYASGPALLRRARELGGAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANL 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446588783 226 AYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAIYHFLH 289
Cdd:COG1940  243 INLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALALE 306
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
5-283 3.27e-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: 159.81  E-value: 3.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783    5 IAFDIGGTQIKYGIVSETGIVL--KHKTVPTEIHlggEQIIQKLILLSKKLMSEHT--ISGIGISTAGIVDVNRGVVTGG 80
Cdd:pfam00480   1 IGIDIGGTKIAAALFDEEGEILarERVPTPTTTT---EETLVDAIAFFVDSAQRKFgeLIAVGIGSPGLISPKYGYITNT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   81 ADhiPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWG 160
Cdd:pfam00480  78 PN--IGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  161 NMLIEGKTF----------EEVASISGlihLVRNYKGKG-NWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIF 229
Cdd:pfam00480 156 HIQLDPNGPkcgcgnhgclETIASGRA---LEKRYQQKGeDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLF 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446588783  230 NPETIIIGGGITDRGnQFLKEVKEEVGRYLNKEI-YSDCEIELAQNGNRAGMIGA 283
Cdd:pfam00480 233 DPQAIVLGGGVSNAD-GLLEAIRSLVKKYLNGYLpVPPVIIVAASLGDNAGALGA 286
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
5-283 3.34e-47

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: 160.45  E-value: 3.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783    5 IAFDIGGTQIKYGIVSETGIVL-KHK----TVPTEIHLGGEQIIQKLILLSKKlmSEHTISGIGISTAGIVDVNRGVVTG 79
Cdd:TIGR00744   1 IGVDIGGTTIKLGVVDEEGNILsKWKvptdTTPETIVDAIASAVDSFIQHIAK--VGHEIVAIGIGAPGPVNRQRGTVYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   80 GADhiPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEW 159
Cdd:TIGR00744  79 AVN--LDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  160 GNMLIE---------GKT--FEEVASISGLIHLVRNYKGK-------------GNWNGKTIFELYDKGDREVTQAVEVFF 215
Cdd:TIGR00744 157 GHIRMVpdgrllcncGKQgcIETYASATGLVRYAKRANAKperaevllalgdgDGISAKHVFVAARQGDPVAVDSYREVA 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446588783  216 KHLAIGISNLAYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGA 283
Cdd:TIGR00744 237 RWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGA 304
PRK13310 PRK13310
N-acetyl-D-glucosamine kinase; Provisional
4-288 9.34e-25

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 183967 [Multi-domain]  Cd Length: 303  Bit Score: 100.83  E-value: 9.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEiHLGGEQIIQKLILLSKKLMSEHTISG-IGISTAGIVDVNRGVVTggAD 82
Cdd:PRK13310   2 YYGFDIGGTKIELGVFNEKLELQWEERVPTP-RDSYDAFLDAVCELVAEADQRFGCKGsVGIGIPGMPETEDGTLY--AA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  83 HIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNM 162
Cdd:PRK13310  79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 163 -------LIEGKTF-------------EEVASISGLIHLVRNYKGKgNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGI 222
Cdd:PRK13310 159 rlpvdalTLLGWDAplrrcgcgqkgciENYLSGRGFEWLYQHYYGE-PLQAPEIIALYYQGDEQAVAHVERYLDLLAICL 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588783 223 SNLAYIFNPETIIIGGGITDrgnqfLKEVKEEVGRYLNKEIYSDCE---IELAQNGNRAGMIGAIYHFL 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 1.30e-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: 331.83  E-value: 1.30e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEHTISGIGISTAGIVDVNRGVVTGGADH 83
Cdd:cd24068    2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGISSAGQVDPKTGEVIYATDN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  84 IPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNML 163
Cdd:cd24068   82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 164 IEG----------KTFEEVASISGLIHLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPET 233
Cdd:cd24068  162 VDPggrpcccggkGCLEQYASGTALVRRVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446588783 234 IIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAIYH 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 7.03e-98

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: 289.87  E-value: 7.03e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   1 MKEYIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLI-----LLSKKLMSEHTISGIGISTAGIVDVNRG 75
Cdd:COG1940    4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAelieeLLAEAGISRGRILGIGIGVPGPVDPETG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  76 VVTGgADHIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYS 155
Cdd:COG1940   84 VVLN-APNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 156 AGEWGNMLIE--------GKT--FEEVASISGLIHLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:COG1940  163 AGEIGHMPVDpdgplcgcGNRgcLETYASGPALLRRARELGGAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANL 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446588783 226 AYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAIYHFLH 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 9.16e-74

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: 226.19  E-value: 9.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEH----TISGIGISTAGIVDVNRGVVTGg 80
Cdd:cd23763    1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAgvreRILGIGIGVPGPVDPETGIVLF- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  81 ADHIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWG 160
Cdd:cd23763   80 APNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 161 NMLIegktFEEVAsisglihlvrnykgkgnwngktifelydkgdrevtqavevffKHLAIGISNLAYIFNPETIIIGGGI 240
Cdd:cd23763  160 HITV----LEEAA------------------------------------------RYLGIGLANLINLLNPELIVLGGGV 193
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 446588783 241 TDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAIY 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 1.22e-69

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: 217.05  E-value: 1.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTeIHLGGEQIIQKLILLSKKLMSEhtISGIGISTAGIVDVNRGVVTGGAdH 83
Cdd:cd24152    2 YLVFDIGGTFIKYALVDENGNIIKKGKIPT-PKDSLEEFLDYIKKIIKRYDEE--IDGIAISAPGVIDPETGIIYGGG-A 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  84 IPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNML 163
Cdd:cd24152   78 LPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 164 I-----EGKTFEEVASISGLIHLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPETIIIGG 238
Cdd:cd24152  158 TddddkDLLFFSGLASMFGLVKRYNKAKGLEPLDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIYNIQYILDPEVIVIGG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446588783 239 GITDRgNQFLKEVKEEVGRYLNKEIYSD--CEIELAQNGNRAGMIGAIYH 286
Cdd:cd24152  238 GISEQ-PLFIEDLKKEVNEILANRPGSIpkPEIKACKFGNDANLLGALYN 286
ASKHA_ATPase_ROK_BsXylR-like cd24076
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ...
5-284 1.84e-58

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: 188.93  E-value: 1.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKL-----MSEHTISGIGISTAGIVDVNRGVVTg 79
Cdd:cd24076    4 IGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREAlaaapDSPLGILGIGVGVPGLVDSEDGVVL- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  80 gadHIP--GYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAG 157
Cdd:cd24076   83 ---LAPnlGWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 158 EWGNMLIE--------GKT--FEEVASISGLIHLVRNyKGKGNWNGKT--IFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:cd24076  160 EIGHMTVDpdgppcscGNRgcWETYASERALLRAAGR-LGAGGEPLSLaeLVEAARAGDPAALAALEEVGEYLGIGLANL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446588783 226 AYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAI 284
Cdd:cd24076  239 VNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAA 297
ASKHA_NBD_ROK_BsGLK-like cd24062
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ...
4-286 9.04e-58

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: 187.50  E-value: 9.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETG-IVLKHKtVPTEIHLGGEQIIQKLI-----LLSKKLMSEHTISGIGISTAGIVDVNRGVV 77
Cdd:cd24062    2 IVGIDVGGTTIKMAFLTQEGeIVQKWE-IPTNKLEGGENIITDIAesiqqLLEELGYSKEDLIGIGVGVPGPVDVETGTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  78 TGGADHipGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAG 157
Cdd:cd24062   81 EVAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 158 EWGNMLIE---------GKT--FEEVASISGLI-------------HLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEV 213
Cdd:cd24062  159 EIGHITVNpeggapcncGKTgcLETVASATGIVriareeleegkgsSALRILALGGELTAKDVFEAAKAGDELALAVVDT 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588783 214 FFKHLAIGISNLAYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAIYH 286
Cdd:cd24062  239 VARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAAWL 311
ASKHA_NBD_ROK_SgGLK-like cd24061
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ...
5-283 5.75e-56

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: 182.94  E-value: 5.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSETGIVLKHKTVPTEIhlGGEQIIQKLILLSKKLMSEHTISGIGISTAGIVDVNRGVVTGgADHI 84
Cdd:cd24061    2 IGVDIGGTKIAAGVVDEEGEILATERVPTPP--TADGIVDAIVEAVEELREGHDVSAVGVAAAGFVDADRATVLF-APNI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  85 PgYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNMLI 164
Cdd:cd24061   79 A-WRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 165 E--------GKT--FEEVASISGLIH---------------LVRNYKGKGNwNGKTIFELYDKGDREVTQAVEVFFKHLA 219
Cdd:cd24061  158 VpdgllcgcGSRgcWEQYASGRALVRyakeaanatpegaavLLADGSVDGI-TGKHISEAARAGDPVALDALRELARWLG 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446588783 220 IGISNLAYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYL-NKEIYSDCEIELAQNGNRAGMIGA 283
Cdd:cd24061  237 AGLASLAALLDPELFVIGGGVSDAGDLLLDPIREAFERWLpGRGWRPIPRLRTAQLGNDAGLIGA 301
ASKHA_NBD_ROK_TmGLK-like cd24064
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ...
5-283 4.53e-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: 4.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEHTISGIGISTAGIVDVNRGVVTGGADhI 84
Cdd:cd24064    2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRIAETVNELIEEMELLGIGIGSPGSIDRENGIVRFSPN-F 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  85 PGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNMLI 164
Cdd:cd24064   81 PDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 165 EGK----------TFEEVASISGLIHLVRNYKGK---------GNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNL 225
Cdd:cd24064  161 EPNgpicgcgnrgCVEAFASATAIIRYARESRKRypdslagesEKINAKHVFDAARKNDPLATMVFRRVVDALAIAIGGF 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446588783 226 AYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGA 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 2.86e-47

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: 160.06  E-value: 2.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEHT----ISGIGISTAGIVDVNRGVVTG 79
Cdd:cd24059    3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRLLEKENikskILGIGIGAPGPLDVEKGIILN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  80 gADHIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEW 159
Cdd:cd24059   83 -PPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 160 GNMLIE--GK--------TFEEVASISGLIHLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIF 229
Cdd:cd24059  162 GHTSIDinGPrcscgnrgCLELYASIPAIEKKARSALGSGRSFQLDIVEALQKGDPIADEVIEEAAKYLGIGLVNLINLL 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446588783 230 NPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAI 284
Cdd:cd24059  242 NPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAA 296
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
5-283 3.27e-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: 159.81  E-value: 3.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783    5 IAFDIGGTQIKYGIVSETGIVL--KHKTVPTEIHlggEQIIQKLILLSKKLMSEHT--ISGIGISTAGIVDVNRGVVTGG 80
Cdd:pfam00480   1 IGIDIGGTKIAAALFDEEGEILarERVPTPTTTT---EETLVDAIAFFVDSAQRKFgeLIAVGIGSPGLISPKYGYITNT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   81 ADhiPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWG 160
Cdd:pfam00480  78 PN--IGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  161 NMLIEGKTF----------EEVASISGlihLVRNYKGKG-NWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIF 229
Cdd:pfam00480 156 HIQLDPNGPkcgcgnhgclETIASGRA---LEKRYQQKGeDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLF 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446588783  230 NPETIIIGGGITDRGnQFLKEVKEEVGRYLNKEI-YSDCEIELAQNGNRAGMIGA 283
Cdd:pfam00480 233 DPQAIVLGGGVSNAD-GLLEAIRSLVKKYLNGYLpVPPVIIVAASLGDNAGALGA 286
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
5-283 3.34e-47

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: 160.45  E-value: 3.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783    5 IAFDIGGTQIKYGIVSETGIVL-KHK----TVPTEIHLGGEQIIQKLILLSKKlmSEHTISGIGISTAGIVDVNRGVVTG 79
Cdd:TIGR00744   1 IGVDIGGTTIKLGVVDEEGNILsKWKvptdTTPETIVDAIASAVDSFIQHIAK--VGHEIVAIGIGAPGPVNRQRGTVYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   80 GADhiPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEW 159
Cdd:TIGR00744  79 AVN--LDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  160 GNMLIE---------GKT--FEEVASISGLIHLVRNYKGK-------------GNWNGKTIFELYDKGDREVTQAVEVFF 215
Cdd:TIGR00744 157 GHIRMVpdgrllcncGKQgcIETYASATGLVRYAKRANAKperaevllalgdgDGISAKHVFVAARQGDPVAVDSYREVA 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446588783  216 KHLAIGISNLAYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGA 283
Cdd:TIGR00744 237 RWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGA 304
ASKHA_ATPase_ROK_Lmo0178-like cd24071
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ...
1-290 1.07e-43

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: 151.28  E-value: 1.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   1 MKEYIAFDIggTQIKYGIVSETGIVLKHKTVPTEIhlgGEQIIQKLILLSKKLMSEHTISGIGISTAGIVDVNRGVVTGG 80
Cdd:cd24071    9 EEGYLVLAL--TDLKGKILEKTRIPFDHETDPEKV---IELIAENIKKLIKNKHVEKKLLGIGIAVSGLVDSKKGIVIRS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  81 AdhIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWG 160
Cdd:cd24071   84 T--ILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 161 NMLI--EGK--------TFEEVASISGLIHLVRNYKGKGN---------WNGKTIFELYDKGDREVTQAVEVFFKHLAIG 221
Cdd:cd24071  162 HMTIqpDGRkcycgqkgCLEAYASFEALVNEIKELTESYPlsllkeledFEIEKVREAAEEGDSVATELFKKAGEYLGIG 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588783 222 ISNLAYIFNPETIIIGGGITDRGNQFLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGAIYHFLHH 290
Cdd:cd24071  242 IKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALLVIDH 310
ASKHA_NBD_ROK_TtHK-like cd24065
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ...
5-283 1.32e-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: 145.16  E-value: 1.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSEtGIVLKHKTVPTEIHlGGEQIIQKLILLSKKLMSEH-TISGIGISTAGIVDVNRGVVTGgADH 83
Cdd:cd24065    3 IGLDLGGTKIAAGVVDG-GRILSRLVVPTPRE-GGEAVLDALARAVEALQAEApGVEAVGLGVPGPLDFRRGRVRF-APN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  84 IPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNML 163
Cdd:cd24065   80 IPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 164 I-----------EGkTFEEVASISGLIHLVRNYKGKGNWNgKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPE 232
Cdd:cd24065  160 VlpggpmcgcglVG-CLEALASGRALARDASFAYGRPMST-AELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALDPE 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446588783 233 TIIIGGGITDRGNQFLKEVKEEVGRYLnkEIYSDCEIELAQNGNRAGMIGA 283
Cdd:cd24065  238 VFVLGGGVAQVGDYYLLPVQEAARRYT--EGWHAPPLRLAHLGTDAGVIGA 286
ASKHA_NBD_ROK_ApGLK-like cd24063
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ...
3-283 1.17e-39

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: 140.55  E-value: 1.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   3 EYIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEHT---ISGIGISTAGIVDVNRGVVTG 79
Cdd:cd24063    1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIETLLSKAGkdsIEGIGVSSAGPLDLRKGTIVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  80 gADHIPGYStIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEW 159
Cdd:cd24063   81 -SPNIKGKE-IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 160 GNMLIE--------------------GKTFEEVAS------ISGLIHLVRNYKGKGNwNGKTIFELYDKGDREVTQAVEV 213
Cdd:cd24063  159 GHLVVDtesglkcgcggyghweafasGRGIPRFARewaegfSSRTSLKLRNPGGEGI-TAKEVFSAARKGDPLALKIIEK 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 214 FFKHLAIGISNLAYIFNPETIIIGGGITDRGNQFLKEVKEEVGRylNKEIYSDCEIELAQNGNRAGMIGA 283
Cdd:cd24063  238 LARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEK--NPAISKGPEIVLSELGDDVGLIGA 305
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
25-283 1.68e-39

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: 139.99  E-value: 1.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  25 VLKHKTVPTEIHlGGEQIIQKLILLSKKLMSEHT-----ISGIGISTAGIVDVNRGVVTggADHIPGYSTIPIINRLQEV 99
Cdd:cd24073   24 VLASHTLPLDSG-DPEAVAEAIAEAVAELLAQAGlspdrLLGIGVGLPGLVDAETGICR--WSPLLGWRDVPLAELLEER 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 100 LKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNMLIE--------GKT--F 169
Cdd:cd24073  101 LGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGHTTVDpdgppcrcGKRgcL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 170 EEVASISGLIHLVRNYKGKGnwNGKTIFELYD---KGDREVTQAVEVFFKHLAIGISNLAYIFNPETIIIGGGITDRGNQ 246
Cdd:cd24073  181 EAYASDPAILRQAREAGLRG--EPLTIEDLLAaarAGDPAARAILRRAGRALGLALANLVNLLDPELIIISGEGVRAGDL 258
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446588783 247 FLKEVKEEVGRYLNKEIYSDCEIELAQNGNRAGMIGA 283
Cdd:cd24073  259 LFEPMREALRAHVFPGLASDLELVIHPWGDEAWARGA 295
ASKHA_ATPase_ROK_SaXylR-like cd24077
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ...
4-288 1.78e-39

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: 139.60  E-value: 1.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTeIHLGGEQIIQKLILLSKKLMSE-----HTISGIGISTAGIVDVNRGVVT 78
Cdd:cd24077    3 SIGIDLGYNYISLMLTYLDGEIISSKQIKL-LDISFENILEILKSIIQELISQapktpYGLVGIGIGIHGIVDENEIIFT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  79 ggadhiPGYST--IPIINRLQEVLKVPVSIENDVNCAALGEKwnGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSA 156
Cdd:cd24077   82 ------PYYDLedIDLKEKLEEKFNVPVYLENEANLSALAER--TFSEDYDNLISISIHSGIGAGIIINNQLYRGYNGFA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 157 GEWGNMLIE--GKT--------FEEVASISGLIHLVRNYKGKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLA 226
Cdd:cd24077  154 GEIGHMIIVpnGKPcpcgnkgcLEQYASEKALLKELSEKKGLETLTFDDLIQLYNEGDPEALELIDQFIKYLAIGINNII 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446588783 227 YIFNPETIIIGGGITDRGNQFLKEVKEevgrYLNKEIYSDCEIELAQNGNRAGMIGA----IYHFL 288
Cdd:cd24077  234 NTFNPEIIIINSSLINEIPELLEKIKE----QLSSSFNKYVEILISTLGKNATLLGGaavaIKNFL 295
ASKHA_NBD_ROK_NAGK cd24057
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
4-283 1.17e-36

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: 132.36  E-value: 1.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGE--QIIQKLILLSKKLMSEHTisGIGISTAGIVDVNRGVVTggA 81
Cdd:cd24057    2 YYGFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAAflAAIAELVAEADARFGVKG--PVGIGIPGVIDPEDGTLI--T 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  82 DHIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGN 161
Cdd:cd24057   78 ANIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 162 M------LIEGKTF-------------EEVASISGLIHLVRNYKGKGNwNGKTIFELYDKGDREVTQAVEVFFKHLAIGI 222
Cdd:cd24057  158 GplpadaLLLGYDLpvlrcgcgqtgclETYLSGRGLERLYAHLYGEEL-DAPEIIAAWAAGDPQAVAHVDRWLDLLAGCL 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446588783 223 SNLAYIFNPETIIIGGGITDrgnqfLKEVKEEVGRYLNKEIYS--DC-EIELAQNGNRAGMIGA 283
Cdd:cd24057  237 ANILTALDPDVVVLGGGLSN-----FPALIAELPAALPAHLLSgaRTpRIVPARHGDAGGVRGA 295
ASKHA_NBD_ROK_AlsK cd24070
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ...
4-287 1.82e-36

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: 131.52  E-value: 1.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEH--TISGIGISTAGIVDVNRGVVTGgA 81
Cdd:cd24070    3 VLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGDPVEVLADLIREYIEEAglKPAAIVIGVPGTVDKDRRTVIS-T 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  82 DHIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGN 161
Cdd:cd24070   82 PNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 162 MLIEGKT----------FEEVASISGLIHLVRNYKGKGNwngkTIFELYDKGDREVtqaVEVFFKHLAIGISNLAYIFNP 231
Cdd:cd24070  162 IPVYGNGkpcgcgntgcLETYASGRALEEIAEEHYPDTP----ILDIFVDHGDEPE---LDEFVEDLALAIATEINILDP 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446588783 232 ETIIIGGGITDRgNQFLKEV-KEEVGRYLNK-EIYSDCEIELAQNGNRAGMIGAIYHF 287
Cdd:cd24070  235 DAVILGGGVIDM-KGFPRETlEEYIRKHLRKpYPADNLKIIYAELGPEAGVIGAAIYA 291
ASKHA_NBD_ROK_GNE cd24060
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ...
5-251 2.34e-36

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: 131.77  E-value: 2.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSETGIVLKHKTVPTEihLGGEQIIQKLILLSKKLMSEHT-----ISGIGISTAGIVDVNRGVVTG 79
Cdd:cd24060    3 LAVDLGGTNLRVAIVSMKGEIVKKYTQPNP--KTYEERIDLILQMCVEAASEAVklncrILGVGISTGGRVNPREGIVLH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  80 GADHIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEW 159
Cdd:cd24060   81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 160 GN---------------------------------------MLIEGKTFEEVASISGlIHLVRNYKgKGNWNGKTIFely 200
Cdd:cd24060  161 GHivvsldgpdcmcgshgcveayasgmalqreakklhdedlLLVEGMSVTNDEEVTA-KHLIQAAK-LGNAKAQKIL--- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446588783 201 dkgdREVTQAvevffkhLAIGISNLAYIFNPETIIIGGGITDRGNQFLKEV 251
Cdd:cd24060  236 ----RTAGTA-------LGLGIVNILHTLNPSLVILSGVLASHYENIVKDV 275
ASKHA_ATPase_ROK_YphH-like cd24072
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ...
26-288 4.85e-35

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: 128.30  E-value: 4.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  26 LKHKTVPTEIHLGGEQ-IIQKLI--LLSKKLMSEHTISGIGISTAGIVDVNRGVVTggadHIPGYS--TIPIINRLQEVL 100
Cdd:cd24072   24 LLGEFEYRVITLETPEaLIDEIIdcIDRLLKLWKDRVKGIALAIQGLVDSHKGVSL----WSPGAPwrNIEIKYLLEERY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 101 KVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNMLIE--------GKT--FE 170
Cdd:cd24072  100 GIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGHTKVNpdgarcdcGRRgcLE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 171 EVASISGLIH----LVRNYKGKGNWNGKTIFELYDK---GDREVTQAVEVFFKHLAIGISNLAYIFNPETIIIGGGITDR 243
Cdd:cd24072  180 TVASNSALKRnarvTLKLGPVSADPEKLTMEQLIEAleeGEPIATQIFDRAANAIGRSLANILNLLNPEQVLLYGRGCRA 259
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446588783 244 GNQFLKEVKEEVGRYLNKEIYSDC-EIELAQNGNRAG-MIGAIYHFL 288
Cdd:cd24072  260 GDLLLPAIRRAIAENPFSQHATQIgFGQLSTEQGCAQqALGLVYLYI 306
ASKHA_NBD_ROK_BsFRK-like cd24067
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ...
4-285 2.83e-29

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: 112.64  E-value: 2.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIhlgGEQIIQKLILLSKKLmsEHTISGIGISTAGIVDVNRGVVTGGAdh 83
Cdd:cd24067    1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPTTT---PEETLQAVIDFFREQ--EEPIDAIGIASFGPIDLNPTSPTYGY-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  84 I-----PGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSagE 158
Cdd:cd24067   74 ItttpkPGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLHP--E 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 159 WGNMLIE---------------GKTFEEVAS---ISGlihlvrnykgkgnWNGKTIFELYDkgDREVTqavEVFFKHLAI 220
Cdd:cd24067  152 MGHIRVPrhpdddgfpgvcpfhGDCLEGLASgpaIAA-------------RWGIPAEELPD--DHPAW---DLEAYYLAQ 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446588783 221 GISNLAYIFNPETIIIGGGITDRgNQFLKEVKEEVGRYLN-----KEIYSDCE--IELAQNGNRAGMIGAIY 285
Cdd:cd24067  214 ACANLTLTLSPERIVLGGGVMQR-PGLFPRIREKFRKLLNgylevPRLLPDIDeyIVPPALGNDAGILGALA 284
ASKHA_NBD_ROK_EcFRK-like cd24066
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ...
5-283 4.97e-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: 109.22  E-value: 4.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSETGIVLKHKTVPTEiHLGGEQIIQKLILLSKKLMSE-HTISGIGISTAGIVDVNRGVVTGGAdh 83
Cdd:cd24066    2 IGIDLGGTKIEGIALDRAGRELLRRRVPTP-RGDYEATLDAIADLVEEAEEElGAPATVGIGTPGSISPRTGLVKNAN-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  84 ipgySTI----PIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEW 159
Cdd:cd24066   79 ----STWlngkPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEW 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 160 GNMLIEGKTFEEVAS--------------ISGlIHLVRNYKGKGN--WNGKTIFELYDKGDREVTQAVEVFFKHLAIGIS 223
Cdd:cd24066  155 GHNPLPWPDEDELPGppcycgkrgcvetfLSG-PALERDYARLTGktLSAEEIVALARAGDAAAVATLDRFLDRLGRALA 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588783 224 NLAYIFNPETIIIGGGITDrgnqfLKEVKEEVGRYLNKEIYSD-CEIELAQN--GNRAGMIGA 283
Cdd:cd24066  234 NVINILDPDVIVLGGGLSN-----IDELYTEGPAALARYVFSDeVETPIVKNkhGDSSGVRGA 291
ASKHA_NBD_ROK_EcNanK-like cd24069
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ...
5-286 2.73e-26

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: 104.29  E-value: 2.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVsETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMSEHTIsgIGISTAGIVDvNRGVVTGGADHI 84
Cdd:cd24069    1 LAIDIGGTKIAAALI-GNGQIIDRRQIPTPRSGTPEALADALASLLADYQGQFDR--VAVASTGIIR-DGVLTALNPKNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  85 PGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNMLI 164
Cdd:cd24069   77 GGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 165 EGK----------TFEEVASISGLIHLVRNYKGKGNwNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYIFNPETI 234
Cdd:cd24069  157 DPPgpvcgcgrrgCVEAIASGTAIAAAASEILGEPV-DAKDVFERARSGDEEAARLIDRAARALADLIADLKATLDLDCV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446588783 235 IIGGGITDrgnqfLKEVKEEVGRYLNKE--IYSdCEIELAQNGNRAGMIGAIYH 286
Cdd:cd24069  236 VIGGSVGL-----AEGFLERVEQYLADEpaIFR-VSLEPARLGQDAGLLGAALL 283
PRK13310 PRK13310
N-acetyl-D-glucosamine kinase; Provisional
4-288 9.34e-25

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 183967 [Multi-domain]  Cd Length: 303  Bit Score: 100.83  E-value: 9.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEiHLGGEQIIQKLILLSKKLMSEHTISG-IGISTAGIVDVNRGVVTggAD 82
Cdd:PRK13310   2 YYGFDIGGTKIELGVFNEKLELQWEERVPTP-RDSYDAFLDAVCELVAEADQRFGCKGsVGIGIPGMPETEDGTLY--AA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  83 HIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGNM 162
Cdd:PRK13310  79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 163 -------LIEGKTF-------------EEVASISGLIHLVRNYKGKgNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGI 222
Cdd:PRK13310 159 rlpvdalTLLGWDAplrrcgcgqkgciENYLSGRGFEWLYQHYYGE-PLQAPEIIALYYQGDEQAVAHVERYLDLLAICL 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588783 223 SNLAYIFNPETIIIGGGITDrgnqfLKEVKEEVGRYLNKEIYSDCE---IELAQNGNRAGMIGAIYHFL 288
Cdd:PRK13310 238 GNILTIVDPHLVVLGGGLSN-----FDAIYEQLPKRLPRHLLPVARvprIEKARHGDAGGVRGAAFLHL 301
ASKHA_ATPase_ROK_NagC cd24075
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ...
5-241 3.56e-23

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: 96.67  E-value: 3.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSETGIVLKHKTVPTEiHLGGEQIIQKLILLSKKLMSEHT-----ISGIGISTAGIVDVNRGVVTg 79
Cdd:cd24075    4 LAVRLGRHDLTLGLYDLSGELLAEHTVPLT-ALNQEALLSQLIEEIAQFLKSHRrktqrLIAISITLPGLINPKTGVVH- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  80 gadHIPGYS--TIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAG 157
Cdd:cd24075   82 ---YMPHIQvkSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 158 EWGNMLIE--GK--------TFEEVASISGLIHLVRNYKGKG--------NWNGKTIFELYDKGDREVTQAVEVFFKHLA 219
Cdd:cd24075  159 EIGHIQIEplGErchcgnfgCLETVASNAAIEQRVKKLLKQGyasqltlqDCTIKDICQAALNGDQLAQDVIKRAGRYLG 238
                        250       260
                 ....*....|....*....|..
gi 446588783 220 IGISNLAYIFNPETIIIGGGIT 241
Cdd:cd24075  239 KVIAILINLLNPQKIIIAGEIT 260
PRK09698 PRK09698
D-allose kinase; Provisional
1-285 3.13e-21

D-allose kinase; Provisional


Pssm-ID: 182034 [Multi-domain]  Cd Length: 302  Bit Score: 91.20  E-value: 3.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   1 MKEYIA-FDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGeQIIQKLILLSKKLMSEH--TISGIGISTAGIVDVNRGVV 77
Cdd:PRK09698   2 QKNVVLgIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAP-DLVSGLGEMIDEYLRRFnaRCHGIVMGFPALVSKDRRTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  78 TGgADHIPGYST--IPIINRLQEVLKVPVSIENDVNCAALgekWNGIGREKENFIMLT--LGTGIGGAIFIDRELYRGHS 153
Cdd:PRK09698  81 IS-TPNLPLTALdlYDLADKLENTLNCPVFFSRDVNLQLL---WDVKENNLTQQLVLGayLGTGMGFAVWMNGAPWTGAH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 154 YSAGE-----WGNMLIE---GKTFEEVASISGLiHLVRNYKGkgNWNGKTIFELYDKGDREvtQAVEVFFKHLAIGISNL 225
Cdd:PRK09698 157 GVAGElghipLGDMTQHcgcGNPGCLETNCSGM-ALRRWYEQ--QPRDYPLSDLFVHAGDH--PFIQSLLENLARAIATS 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446588783 226 AYIFNPETIIIGGGITDRgNQFLKE-VKEEVGRYLNKEI-YSDCEIELAQNGNRAGMIGAIY 285
Cdd:PRK09698 232 INLFDPDAIILGGGVMDM-PAFPREtLIAMIQKYLRKPLpYEVVRFIYASSSDFNGAQGAAI 292
ASKHA_NBD_ROK_PPGK cd24058
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ...
6-284 4.46e-20

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: 86.85  E-value: 4.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   6 AFDIGGTQIKYGIVSETGIVLKHK--TVPTEIHLGGEQIIQKLILLSKKLmSEHTISGIGIStaGIVdvNRGVVTGGADH 83
Cdd:cd24058    3 GIDIGGSGIKGAIVDTDTGELLSEriRIPTPQPATPEAVADVVAELVAHF-PWFGPVGVGFP--GVV--RRGVVRTAANL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  84 IPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENF-IMLTLGTGIGGAIFIDrelyrGHSYSAGEWGNM 162
Cdd:cd24058   78 DKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVvLVLTLGTGIGSALFVD-----GHLVPNTELGHL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 163 LIEGKTFEEVASISglihlVRNYKGKGN--WNgktifelydkgdrevtqavevffKHLAIGISNLAYIFNPETIIIGGGI 240
Cdd:cd24058  153 EIRGKDAEERASLG-----VRAREDLGWkrWA-----------------------KRVNKYLQYLERLFNPDLFIIGGGN 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 446588783 241 TDRGNQFLKEVKEEvgrylnkeiysdCEIELAQNGNRAGMIGAI 284
Cdd:cd24058  205 SKKADKFLPLLDVK------------TPVVPAVLRNDAGIVGAA 236
PRK13311 PRK13311
N-acetyl-D-glucosamine kinase; Provisional
4-225 5.08e-17

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 106271 [Multi-domain]  Cd Length: 256  Bit Score: 78.53  E-value: 5.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHlGGEQIIQKLILLSKKLMSEHTISG-IGISTAGIVDVNRGVVTGGad 82
Cdd:PRK13311   2 YYGFDMGGTKIELGVFDENLQRIWHKRVPTPRE-DYPQLLQILRDLTEEADTYCGVQGsVGIGIPGLPNADDGTVFTA-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  83 HIPGYSTIPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGN- 161
Cdd:PRK13311  79 NVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHf 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 162 ------MLIEGKTFEEVASISGLIHLVRNY-KGKG-NW----------NGKTIFELYDKGDREVTQAVEVFFKHLAIGIS 223
Cdd:PRK13311 159 rlpvdaLDILGADIPRVPCGCGHRGCIENYiSGRGfEWmyshfyqhtlPATDIIAHYAAGEPKAVAHVERFMDVLAVCLG 238

                 ..
gi 446588783 224 NL 225
Cdd:PRK13311 239 NL 240
PRK05082 PRK05082
N-acetylmannosamine kinase; Provisional
6-283 6.55e-17

N-acetylmannosamine kinase; Provisional


Pssm-ID: 235338 [Multi-domain]  Cd Length: 291  Bit Score: 78.80  E-value: 6.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   6 AFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGEQIIQKLILLSKKLMseHTISGIGISTAGIvdVNRGVVT------- 78
Cdd:PRK05082   5 AIDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQ--AQADRVAVASTGI--INDGILTalnphnl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  79 GGADHIPGYSTIPIINRLqevlkvPVSIENDVNCAALGEkWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGE 158
Cdd:PRK05082  81 GGLLHFPLVQTLEQLTDL------PTIALNDAQAAAWAE-YQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGH 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 159 WGNMLIE--------GKT--FEEVASISGLIHLVRNYkgKGNWNGKTIFELYDKGDREVTQAVEVFFKHLAIGISNLAYI 228
Cdd:PRK05082 154 IGHTLADphgpvcgcGRRgcVEAIASGRAIAAAAQGW--LAGCDAKTIFERAGQGDEQAQALINRSAQAIARLIADLKAT 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446588783 229 FNPETIIIGGGItdrG--NQFLKEVKEevgrYLNK--EIYSdCEIELAQNGNRAGMIGA 283
Cdd:PRK05082 232 LDCQCVVLGGSV---GlaEGYLELVQA----YLAQepAIYH-VPLLAAHYRHDAGLLGA 282
PRK09557 PRK09557
fructokinase; Reviewed
5-283 5.61e-15

fructokinase; Reviewed


Pssm-ID: 236565 [Multi-domain]  Cd Length: 301  Bit Score: 73.52  E-value: 5.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   5 IAFDIGGTQIKYGIVSETGIVLKHKTVPT--EIHLGGEQIIQKLILLSKKLMSEHTISGIGIStaGIVDVNRGVV-TGGA 81
Cdd:PRK09557   3 IGIDLGGTKIEVIALDDAGEELFRKRLPTprDDYQQTIEAIATLVDMAEQATGQRGTVGVGIP--GSISPYTGLVkNANS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  82 DHIPGYstiPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIGGAIFIDRELYRGHSYSAGEWGN 161
Cdd:PRK09557  81 TWLNGQ---PLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWGH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 162 MLIEGKTFEEVAS-----------------ISGlIHLVRNYKGKGN--WNGKTIFELYDKGDREVTQAVEVFFKHLAIGI 222
Cdd:PRK09557 158 NPLPWMDEDELRYrnevpcycgkqgcietfISG-TGFATDYRRLSGkaLKGSEIIRLVEEGDPVAELAFRRYEDRLAKSL 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446588783 223 SNLAYIFNPETIIIGGGITDrgnqfLKEVKEEVGRYLNKEIYS-DCEIELAQN--GNRAGMIGA 283
Cdd:PRK09557 237 AHVINILDPDVIVLGGGMSN-----VDRLYPTLPALLKQYVFGgECETPVRKAlhGDSSGVRGA 295
ASKHA_NBD_GLK cd24008
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ...
4-286 1.08e-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: 73.03  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   4 YIAFDIGGTQIKYGIVSET---GIVLKHKTVPTEIHLGGEQIIQKLIllskKLMSEHTISGIGISTAGIVDVNRGVVTGG 80
Cdd:cd24008    1 ILVGDIGGTNARLALADAGdgsGDLLFVRKYPSADFASLEDALAAFL----AELGAPRPKAACIAVAGPVDGGRVRLTNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  81 ADHIPGystipiiNRLQEVLKV-PVSIENDVNCAALG---------EKWNGIGREKENFIMLTL--GTGIGGAIFIDREL 148
Cdd:cd24008   77 DWSIDA-------AELRKALGIgRVRLLNDFEAAAYGlpalgpedlLVLYGGGGPLPGGPRAVLgpGTGLGVALLVPDGD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 149 YR--------GHSYSA--GEWGNMLIE--------GKTFEEVASISGLIHLVRNYKGKGNW-----NGKTIFELYDKGDR 205
Cdd:cd24008  150 GGyvvlpsegGHADFApvTEEEAELLEflrkrfgrSVSYEDVLSGPGLENIYEFLAKLDGAeppdlTAEEIAEAALAGDP 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 206 EVTQAVEVFFKHLAIGISNLAYIFNP-ETIIIGGGITDRgNQFLKEVKEEVGRYLNKEIYS----DCEIELAQNGNrAGM 280
Cdd:cd24008  230 LAREALDLFARILGRFAGNLALSFLAtGGVYLAGGIAPK-NLDLLDSSAFREAFLDKGRMSdlleDIPVYLVTNED-LGL 307

                 ....*.
gi 446588783 281 IGAIYH 286
Cdd:cd24008  308 LGAAAY 313
ASKHA_ATPase_ROK_Mlc cd24074
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ...
62-247 1.78e-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: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  62 IGISTAGIVDVNRGVVTggadHIPGYST--IPIINRLQEVLKVPVSIENDVNCAALGEKWNGIGREKENFIMLTLGTGIG 139
Cdd:cd24074   66 IAITLPGIIDPESGIVH----RLPFYDIknLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 140 GAIFIDRELYRGHSYSAGEWGNMLIEGK----------TFEEVASISGLIHLVRNYKGKG-----NWNGKTIFELYDKGD 204
Cdd:cd24074  142 AGVITDGQLLHAGSSRLGELGHTQIDPYgkrcycgnhgCLETVASIPAILEQANQLLEQSpdsmlHGQPISIESLCQAAL 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446588783 205 REVTQAVEV---FFKHLAIGISNLAYIFNPETIIIGGGITDRGNQF 247
Cdd:cd24074  222 AGDPLAQDIiiqVGRHLGRILAILVNLFNPEKILIGSPLNNAAEIL 267
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
4-68 7.83e-06

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: 46.18  E-value: 7.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446588783    4 YIAFDIGGTQIKYGIVSETGIVLKHKTVPTEIHLGGE--------QIIQKLILLSKKLMSEHTIS-----GIGISTAG 68
Cdd:pfam00370   2 YLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPgwaeqdpdEIWQAVAQCIAKTLSQLGISlkqikGIGISNQG 79
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
2-283 5.26e-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: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783   2 KEYIAFDIGGTQIKYGIVSETG-----IVLKHKTVPTEIHLGG-----EQIIQKLillsKKLMSEHTIS---GIGIS--- 65
Cdd:cd24000   43 GEFLAIDLGGTNLRVALVSLDGkgievTISKKYEIPDEIKTASaeeffDFIADCI----AEFLKENGLKkplPLGFTfsf 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783  66 TAGIVDVNRGVVTGGADhipGYSTIPIINR-----LQEVLK------VPVSIENDVNCAALGEKWngigREKENFIMLTL 134
Cdd:cd24000  119 PLEQTSLNDGKLLSWTK---GFKIPGVEGKdvgelLNDALKkrglpvKVVAVLNDTVATLLAGAY----KDPDCRIGLIL 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 135 GTGIGGAIFIdrELYRGHSYSAG-----EWGN----MLIEGKTFEEVASISGLihlvrnykgkgnwNGKTIFE------- 198
Cdd:cd24000  192 GTGTNAAYLE--PTSNILLGDGGmiintEWGNfgknSLPRTEYDREVDKASEN-------------PGFQPLEkmvsgky 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588783 199 --------LYDKGDREVTQAVEVFFKH----LAIGISNLAYIFNPE-----TIIIGGGITDRGNQFLKEVKEEVGRYLNK 261
Cdd:cd24000  257 lgelvrliLKDLADEILRKICELVAERsarlAAAAIAALLRKTGDSpekkiTIAVDGSLFEKYPGYRERLEEYLKELLGR 336
                        330       340
                 ....*....|....*....|..
gi 446588783 262 EIysDCEIELAQNGnraGMIGA 283
Cdd:cd24000  337 GI--RIELVLVEDG---SLIGA 353
 
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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