|
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
|
|
|