|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
1-304 |
0e+00 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 600.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 1 MLYGLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIPGFVNQSTGIAEITNI 80
Cdd:PRK13310 1 MYYGFDIGGTKIELGVFNEKLELQWEERVPTPRDSYDAFLDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLYAANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQL 160
Cdd:PRK13310 81 PAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHMRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 161 NYHALKLLGWDnAPIYQCGCGNIACLDTYLSGRGFEMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGN 240
Cdd:PRK13310 161 PVDALTLLGWD-APLRRCGCGQKGCIENYLSGRGFEWLYQHYYGEPLQAPEIIALYYQGDEQAVAHVERYLDLLAICLGN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502357555 241 IITAFDPHLIVLGGGLSNFDYLYEALPKALPAHLMRTAKVPVIKKAKYGDSGGVRGAAALFLSR 304
Cdd:PRK13310 240 ILTIVDPHLVVLGGGLSNFDAIYEQLPKRLPRHLLPVARVPRIEKARHGDAGGVRGAAFLHLTD 303
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
1-300 |
3.38e-138 |
|
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: 392.37 E-value: 3.38e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 1 MLYGLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIPGFVNQSTGIAEITNI 80
Cdd:cd24057 1 MYYGFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAAFLAAIAELVAEADARFGVKGPVGIGIPGVIDPEDGTLITANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQL 160
Cdd:cd24057 81 PAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 161 NYHALkLLGWDnAPIYQCGCGNIACLDTYLSGRGFEMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGN 240
Cdd:cd24057 161 PADAL-LLGYD-LPVLRCGCGQTGCLETYLSGRGLERLYAHLYGEELDAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLAN 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 241 IITAFDPHLIVLGGGLSNFDYLYEALPKALPAHLMRTAKVPVIKKAKYGDSGGVRGAAAL 300
Cdd:cd24057 239 ILTALDPDVVVLGGGLSNFPALIAELPAALPAHLLSGARTPRIVPARHGDAGGVRGAAFL 298
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
3-302 |
3.87e-106 |
|
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: 310.81 E-value: 3.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 3 YGLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWL-NAIVNLVKKADEKFGCKGSVGLGIPGFVN-QSTGIAEITNI 80
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEETLvDAIAFFVDSAQRKFGELIAVGIGSPGLISpKYGYITNTPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVaDNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQL 160
Cdd:pfam00480 81 GW-DNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 161 NYHALKllgwdnapiyqCGCGNIACLDTYLSGRGFEMFYRDlKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGN 240
Cdd:pfam00480 160 DPNGPK-----------CGCGNHGCLETIASGRALEKRYQQ-KGEDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIAN 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502357555 241 IITAFDPHLIVLGGGLSNFDYLYEALPKALPAHLMRTAKVPV--IKKAKYGDSGGVRGAAALFL 302
Cdd:pfam00480 228 LINLFDPQAIVLGGGVSNADGLLEAIRSLVKKYLNGYLPVPPviIVAASLGDNAGALGAAALAK 291
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
4-300 |
1.20e-94 |
|
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: 281.79 E-value: 1.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIPGFVNQSTGIAEITNIRVA 83
Cdd:cd24066 3 GIDLGGTKIEGIALDRAGRELLRRRVPTPRGDYEATLDAIADLVEEAEEELGAPATVGIGTPGSISPRTGLVKNANSTWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 84 DNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHlqlnyH 163
Cdd:cd24066 83 NGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGH-----N 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 164 ALKLLGWDNAPIYQCGCGNIACLDTYLSGRGFEMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGNIIT 243
Cdd:cd24066 158 PLPWPDEDELPGPPCYCGKRGCVETFLSGPALERDYARLTGKTLSAEEIVALARAGDAAAVATLDRFLDRLGRALANVIN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 502357555 244 AFDPHLIVLGGGLSNFDYLYEALPKALPAHLM-RTAKVPVIkKAKYGDSGGVRGAAAL 300
Cdd:cd24066 238 ILDPDVIVLGGGLSNIDELYTEGPAALARYVFsDEVETPIV-KNKHGDSSGVRGAAWL 294
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
1-300 |
1.60e-86 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 261.11 E-value: 1.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 1 MLYGLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIPGFVNQSTGIAEITNI 80
Cdd:PRK09557 1 MRIGIDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTIEAIATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKNANS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQL 160
Cdd:PRK09557 81 TWLNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWGHNPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 161 NYHALKLLGWDNApiYQCGCGNIACLDTYLSGRGFEMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGN 240
Cdd:PRK09557 161 PWMDEDELRYRNE--VPCYCGKQGCIETFISGTGFATDYRRLSGKALKGSEIIRLVEEGDPVAELAFRRYEDRLAKSLAH 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502357555 241 IITAFDPHLIVLGGGLSNFDYLYEALPKALPAHLM-RTAKVPViKKAKYGDSGGVRGAAAL 300
Cdd:PRK09557 239 VINILDPDVIVLGGGMSNVDRLYPTLPALLKQYVFgGECETPV-RKALHGDSSGVRGAAWL 298
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-303 |
6.58e-86 |
|
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: 259.83 E-value: 6.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 1 MLYGLDIGGTKIELAVFNSQLEKQYSERVETPK-TSYEDWLNAIVNLVKKADEKFGCKGS----VGLGIPGFVNQSTGIA 75
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTPAgAGPEAVLEAIAELIEELLAEAGISRGrilgIGIGVPGPVDPETGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 76 EIT-NIRVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGE 154
Cdd:COG1940 86 LNApNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 155 LGHLQLNYHALkllgwdnapiyQCGCGNIACLDTYLSGRGFEMFYRDLKG-ESLSAKDIIQRFYAGDKSAVDFVGVFIEL 233
Cdd:COG1940 166 IGHMPVDPDGP-----------LCGCGNRGCLETYASGPALLRRARELGGaEKLTAEELFAAARAGDPLALEVLDEAARY 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502357555 234 AAISIGNIITAFDPHLIVLGGGLSN-FDYLYEALPKALPAHLMRTA-KVPVIKKAKYGDSGGVRGAAALFLS 303
Cdd:COG1940 235 LGIGLANLINLLDPEVIVLGGGVSAaGDLLLEPIREALAKYALPPArEDPRIVPASLGDDAGLLGAAALALE 306
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
1-243 |
6.20e-78 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 238.00 E-value: 6.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 1 MLYGLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIPGFVNQSTGIAEITNI 80
Cdd:PRK13311 1 MYYGFDMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGSVGIGIPGLPNADDGTVFTANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQL 160
Cdd:PRK13311 81 PSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 161 NYHALKLLGWDnAPIYQCGCGNIACLDTYLSGRGFEMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGN 240
Cdd:PRK13311 161 PVDALDILGAD-IPRVPCGCGHRGCIENYISGRGFEWMYSHFYQHTLPATDIIAHYAAGEPKAVAHVERFMDVLAVCLGN 239
|
...
gi 502357555 241 IIT 243
Cdd:PRK13311 240 LLT 242
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
4-300 |
7.31e-59 |
|
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: 190.08 E-value: 7.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSY-EDWLNAIVNLVKKADEKFGCKGsVGLGIPGFVNQSTGiaEIT---- 78
Cdd:cd24068 4 GIDIGGTKIKYGLVDADGEILEKDSVPTPASKGgDAILERLLEIIAELKEKYDIEG-IGISSAGQVDPKTG--EVIyatd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 79 NIRVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHL 158
Cdd:cd24068 81 NLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 159 QLNYHALkllgwdnapiyQCGCGNIACLDTYLSGRGFEMFYRDLKGES-LSAKDIIQRFYAGDKSAVDFVGVFIELAAIS 237
Cdd:cd24068 161 VVDPGGR-----------PCCCGGKGCLEQYASGTALVRRVAEALGEPgIDGREIFDLADAGDPLAKEVVEEFAEDLATG 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502357555 238 IGNIITAFDPHLIVLGGGLSN-----FDYLYEALPKALPAHLMRTAKvpvIKKAKYGDSGGVRGAAAL 300
Cdd:cd24068 230 LANLVHIFDPEVIVIGGGISAqgelfLEELREELRKLLMPPLLDATK---IEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
4-300 |
3.84e-48 |
|
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: 160.71 E-value: 3.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKT-SYEDWLNAIVNLVKKADEKFGCKG---SVGLGIPGFVNQSTGIAEI-T 78
Cdd:cd23763 2 GIDIGGTKIRAALVDLDGEILARERVPTPAEeGPEAVLDRIAELIEELLAEAGVRErilGIGIGVPGPVDPETGIVLFaP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 79 NIRVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHL 158
Cdd:cd23763 82 NLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGHI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 159 QLnyhalkllgWDNApiyqcgcgniacldtylsgrgfemfyrdlkGESLsakdiiqrfyagdksavdfvgvfielaAISI 238
Cdd:cd23763 162 TV---------LEEA------------------------------ARYL---------------------------GIGL 175
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502357555 239 GNIITAFDPHLIVLGGGLSN-FDYLYEALPKALPAHLMRTAKVPV-IKKAKYGDSGGVRGAAAL 300
Cdd:cd23763 176 ANLINLLNPELIVLGGGVAEaGDLLLEPIREAVRRRALPPLRRRVrIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
4-300 |
1.85e-46 |
|
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: 158.11 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFgcKGsVGLGIPGFVNQSTGIA-EITNIRV 82
Cdd:cd24152 4 VFDIGGTFIKYALVDENGNIIKKGKIPTPKDSLEEFLDYIKKIIKRYDEEI--DG-IAISAPGVIDPETGIIyGGGALPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 83 ADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQLNY 162
Cdd:cd24152 81 LKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYLLTDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 163 HALKLLGWDNapiyqcgcgniacldtYLSGRGFEMFYRDLKG-ESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGNI 241
Cdd:cd24152 161 DDKDLLFFSG----------------LASMFGLVKRYNKAKGlEPLDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIYNI 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502357555 242 ITAFDPHLIVLGGGLSNFDYLYEALPKALPAHLMRTAKV---PVIKKAKYGDSGGVRGAAAL 300
Cdd:cd24152 225 QYILDPEVIVIGGGISEQPLFIEDLKKEVNEILANRPGSipkPEIKACKFGNDANLLGALYN 286
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
4-301 |
6.14e-46 |
|
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: 156.94 E-value: 6.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVET-PKTSYEDWLNAIVNLVKKADEKFGCK-GSVGLGIPGFVN-QSTGIAEITNI 80
Cdd:cd24070 5 GIDIGGTNIRIGLVDEDGKLLDFEKVPSkDLLRAGDPVEVLADLIREYIEEAGLKpAAIVIGVPGTVDkDRRTVISTPNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLql 160
Cdd:cd24070 85 PGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHI-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 161 nyhalkllgwdnaPIY----QCGCGNIACLDTYLSGRGFEMFYRDLKGESlsakDIIQRF-YAGDKSAVDfvgVFIELAA 235
Cdd:cd24070 163 -------------PVYgngkPCGCGNTGCLETYASGRALEEIAEEHYPDT----PILDIFvDHGDEPELD---EFVEDLA 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502357555 236 ISIGNIITAFDPHLIVLGGGLSN-----FDYL----YEALPKALPAHLMRtakvpvIKKAKYGDSGGVRGAAALF 301
Cdd:cd24070 223 LAIATEINILDPDAVILGGGVIDmkgfpRETLeeyiRKHLRKPYPADNLK------IIYAELGPEAGVIGAAIYA 291
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
4-298 |
2.99e-45 |
|
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: 154.79 E-value: 2.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSErVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIPGFVNQSTGiaEIT---NI 80
Cdd:cd24065 4 GLDLGGTKIAAGVVDGGRILSRLV-VPTPREGGEAVLDALARAVEALQAEAPGVEAVGLGVPGPLDFRRG--RVRfapNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADNKPILRDLSALLEREVRAENDANCFALSE-----AWDAENAQYpsvlgLILGTGFGGGFVINGKIHSGQTGMAGEL 155
Cdd:cd24065 81 PGLTDFPIRRGLAERLGLPVVLENDANAAALAEhhygaARGTESSVY-----VTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 156 GHLQLNYHalkllgwdnAPIyqCGCGNIACLDTYLSGRGFEMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAA 235
Cdd:cd24065 156 GHTTVLPG---------GPM--CGCGLVGCLEALASGRALARDASFAYGRPMSTAELFELAQQGEPKALRIVEQAAAHLG 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502357555 236 ISIGNIITAFDPHLIVLGGGLS-NFDYLYEALPKALPAHLmRTAKVPVIKKAKYGDSGGVRGAA 298
Cdd:cd24065 225 IGLANLQKALDPEVFVLGGGVAqVGDYYLLPVQEAARRYT-EGWHAPPLRLAHLGTDAGVIGAA 287
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
4-300 |
2.36e-43 |
|
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: 150.52 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKT-SYEDWLNAIVNLVKKADEKFGCKGS----VGLGIPGFVNQSTGiaeit 78
Cdd:cd24062 4 GIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLeGGENIITDIAESIQQLLEELGYSKEdligIGVGVPGPVDVETG----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 79 NIRVADN-----KPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAG 153
Cdd:cd24062 79 TVEVAVNlgwknFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 154 ELGHLqlnyHALKLLGwdnapiYQCGCGNIACLDTYLSGRGF---------------EMFYRDlKGESLSAKDIIQRFYA 218
Cdd:cd24062 159 EIGHI----TVNPEGG------APCNCGKTGCLETVASATGIvriareeleegkgssALRILA-LGGELTAKDVFEAAKA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 219 GDKSAVDFVGVFIELAAISIGNIITAFDPHLIVLGGGLSNF-DYLYEALPKALPAH-LMRTAKVPVIKKAKYGDSGGVRG 296
Cdd:cd24062 228 GDELALAVVDTVARYLGLALANLANTLNPEKIVIGGGVSAAgEFLLSPVKEYFDRFtFPRVRQDTEIVLATLGNDAGVIG 307
|
....
gi 502357555 297 AAAL 300
Cdd:cd24062 308 AAWL 311
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
4-300 |
2.45e-42 |
|
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: 147.89 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSyEDWLNAIVNLVKKADEKFGCkGSVGLGIPGFVNQSTG-IAEITNIRV 82
Cdd:cd24061 3 GVDIGGTKIAAGVVDEEGEILATERVPTPPTA-DGIVDAIVEAVEELREGHDV-SAVGVAAAGFVDADRAtVLFAPNIAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 83 aDNKPILRDLSALLEREVRAENDANCFALSE-AWDAENAQYPSVLgLILGTGFGGGFVINGKIHSGQTGMAGELGHLQL- 160
Cdd:cd24061 81 -RNEPLKDLLEARIGLPVVIENDANAAAWAEyRFGAGRGTDDMVM-ITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRVv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 161 -NYHAlkllgwdnapiyqCGCGNIACLDTYLSGR---------------GFEMFYRDLKGESLSAKDIIQRFYAGDKSAV 224
Cdd:cd24061 159 pDGLL-------------CGCGSRGCWEQYASGRalvryakeaanatpeGAAVLLADGSVDGITGKHISEAARAGDPVAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 225 DFVGVFIELAAISIGNIITAFDPHLIVLGGGLSN-----FDYLYEALPKALPAHLMRTakVPVIKKAKYGDSGGVRGAAA 299
Cdd:cd24061 226 DALRELARWLGAGLASLAALLDPELFVIGGGVSDagdllLDPIREAFERWLPGRGWRP--IPRLRTAQLGNDAGLIGAAD 303
|
.
gi 502357555 300 L 300
Cdd:cd24061 304 L 304
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
4-304 |
1.18e-40 |
|
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: 143.47 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETP-KTSYEDWLNAIVNLVKKA-----DEKFGCKGsVGLGIPGFVNQSTGIaei 77
Cdd:cd24076 5 GVELGVDYITVVVTDLAGEVLWRREVPLPaSDDPDEVLAQLAALIREAlaaapDSPLGILG-IGVGVPGLVDSEDGV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 78 tnIRVAdnkPILR----DLSALLERE----VRAENDANCFALSEAW-----DAENAQYPSVlglilGTGFGGGFVINGKI 144
Cdd:cd24076 81 --VLLA---PNLGwrdvPLRDLLEEAlgvpVFVDNEANAAALAEKRfgagrGVSDLVYLSA-----GVGIGAGIILDGEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 145 HSGQTGMAGELGHLQLNYHALKllgwdnapiyqCGCGNIACLDTYLSGRGFEMFYRDL--KGESLSAKDIIQRFYAGDK- 221
Cdd:cd24076 151 YRGASGFAGEIGHMTVDPDGPP-----------CSCGNRGCWETYASERALLRAAGRLgaGGEPLSLAELVEAARAGDPa 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 222 --SAVDFVGVFIelaAISIGNIITAFDPHLIVLGGGLSNF-DYLYEALPKALPAHLMRTAKVPV-IKKAKYGDSGGVRGA 297
Cdd:cd24076 220 alAALEEVGEYL---GIGLANLVNTFNPELVVLGGALAPLgPWLLPPLRAEVARRALPAPARDVrIVVSRLGEDAAALGA 296
|
....*..
gi 502357555 298 AALFLSR 304
Cdd:cd24076 297 AALAIDH 303
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
4-300 |
2.17e-39 |
|
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: 140.42 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSyedwlNAIVNLVKKADEKFGCKGS--------VGLGIPGFVNQSTGIA 75
Cdd:TIGR00744 2 GVDIGGTTIKLGVVDEEGNILSKWKVPTDTTP-----ETIVDAIASAVDSFIQHIAkvgheivaIGIGAPGPVNRQRGTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 76 EITNIRVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGEL 155
Cdd:TIGR00744 77 YFAVNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 156 GHLQLnyhalkllgwDNAPIYQCGCGNIACLDTYLSGRGF--------------EMFYRDLKGESLSAKDIIQRFYAGDK 221
Cdd:TIGR00744 157 GHIRM----------VPDGRLLCNCGKQGCIETYASATGLvryakranakperaEVLLALGDGDGISAKHVFVAARQGDP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 222 SAVDFVGVFIELAAISIGNIITAFDPHLIVLGGGLSNF-DYLYEALPKALPAHLM-RTAKVPVIKKAKYGDSGGVRGAAA 299
Cdd:TIGR00744 227 VAVDSYREVARWAGAGLADLASLFNPSAIVLGGGLSDAgDLLLDPIRKSYKRWLFgGARQVADIIAAQLGNDAGLVGAAD 306
|
.
gi 502357555 300 L 300
Cdd:TIGR00744 307 L 307
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
2-300 |
1.05e-37 |
|
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: 135.70 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 2 LYGLDIGGTKIELAVFNSQ----LEKQYSERVETPKtsyEDWLNAIVNLVKKADEKFGCKGsVGLGIPGFVNQSTGIAEI 77
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENgdilKKKTIDTKVENGK---EDVINRIAETVNELIEEMELLG-IGIGSPGSIDRENGIVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 78 T-NIRVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELG 156
Cdd:cd24064 77 SpNFPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 157 HLQLNyhalkllgwDNAPiyQCGCGNIACLDTYLSGRGFEMFYRDLKG----------ESLSAKDIIQRFYAGDKSAVDF 226
Cdd:cd24064 157 HVIVE---------PNGP--ICGCGNRGCVEAFASATAIIRYARESRKrypdslagesEKINAKHVFDAARKNDPLATMV 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502357555 227 VGVFIELAAISIGNIITAFDPHLIVLGGGLSNF-DYLYEALPKALPAHLMRT-AKVPVIKKAKYGDSGGVRGAAAL 300
Cdd:cd24064 226 FRRVVDALAIAIGGFVHIFNPEIIIIGGGISRAgSFLLDPIREKTKKYVMLSfQDTYSIELSNLVEDAGILGAASI 301
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
4-300 |
4.38e-35 |
|
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: 129.00 E-value: 4.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWL-NAIVNLVKKADEKFGCKGSVGLGIP--GFVNQSTGIAEITNI 80
Cdd:cd24063 4 AVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVsEQVLGLIETLLSKAGKDSIEGIGVSsaGPLDLRKGTIVNSPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQL 160
Cdd:cd24063 84 IKGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHLVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 161 NYHALKllgwdnapiyQCGCGNIACLDTYLSGRGFEMFY---------------RDLKGESLSAKDIIQRFYAGDKSAVD 225
Cdd:cd24063 164 DTESGL----------KCGCGGYGHWEAFASGRGIPRFArewaegfssrtslklRNPGGEGITAKEVFSAARKGDPLALK 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502357555 226 FVGVFIELAAISIGNIITAFDPHLIVLGGGL-SNFDYLYEALPKALPAHLmRTAKVPVIKKAKYGDSGGVRGAAAL 300
Cdd:cd24063 234 IIEKLARYNGRGIANVINAYDPELIVIGGSVfNNNKDILDPLIEYLEKNP-AISKGPEIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
4-303 |
8.85e-34 |
|
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: 125.39 E-value: 8.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWL-----NAIVNLVKKADEKFGCKGsVGLGIPGFVNQSTG-IAEI 77
Cdd:cd24059 5 GVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVleklyELIDRLLEKENIKSKILG-IGIGAPGPLDVEKGiILNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 78 TNIRVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGH 157
Cdd:cd24059 84 PNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEIGH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 158 LQLNYhalkllgwdNAPiyQCGCGNIACLDTYLSGRGFEMFYRDLKGESLS-AKDIIQRFYAGDKSAVDFVGVFIELAAI 236
Cdd:cd24059 164 TSIDI---------NGP--RCSCGNRGCLELYASIPAIEKKARSALGSGRSfQLDIVEALQKGDPIADEVIEEAAKYLGI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502357555 237 SIGNIITAFDPHLIVLGGGLSNF-DYLYEALPKALPAHLMRTAKVPV-IKKAKYGDSGGVRGAAALFLS 303
Cdd:cd24059 233 GLVNLINLLNPEAIIIGGELIYLgERYLEPIEKEVNSRLFGRNAREVrILKSSLGEDAPLLGAAALVLN 301
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
4-304 |
2.13e-33 |
|
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: 124.20 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGS----VGLGIPGFVNQSTGIaeitn 79
Cdd:cd24073 5 GVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSPDrllgIGVGLPGLVDAETGI----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 80 IRVAdnkPIL--RD--LSALLER----EVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGM 151
Cdd:cd24073 80 CRWS---PLLgwRDvpLAELLEErlglPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 152 AGELGHLQLnyhalkllgWDNAPiyQCGCGNIACLDTYLSGRGF--EMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGV 229
Cdd:cd24073 157 AGEIGHTTV---------DPDGP--PCRCGKRGCLEAYASDPAIlrQAREAGLRGEPLTIEDLLAAARAGDPAARAILRR 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502357555 230 FIELAAISIGNIITAFDPHLIVLGG-GLSNFDYLYEALPKALPAHLMRTA--KVPVIKKAkYGDSGGVRGAAALFLSR 304
Cdd:cd24073 226 AGRALGLALANLVNLLDPELIIISGeGVRAGDLLFEPMREALRAHVFPGLasDLELVIHP-WGDEAWARGAAALALQE 302
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
4-304 |
4.48e-31 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 118.16 E-value: 4.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFG--CKGsVGLGIPGFV-NQSTGIAEITNI 80
Cdd:PRK09698 8 GIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVSGLGEMIDEYLRRFNarCHG-IVMGFPALVsKDRRTVISTPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RV--ADNKPILRDLSALLEREVRAENDANcFALSeaWDAE--NAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELG 156
Cdd:PRK09698 87 PLtaLDLYDLADKLENTLNCPVFFSRDVN-LQLL--WDVKenNLTQQLVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 157 HLqlnyhalkllgwdnaPIY----QCGCGNIACLDTYLSG----RGFEMFYRDLKGESLSAKdiiqrfyAGDKSAVDfvg 228
Cdd:PRK09698 164 HI---------------PLGdmtqHCGCGNPGCLETNCSGmalrRWYEQQPRDYPLSDLFVH-------AGDHPFIQ--- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502357555 229 VFIELAAISIGNIITAFDPHLIVLGGG-LSNFDYLYEALPKALPAHLMR--TAKVPVIKKAKYGDSGGVRGAAALFLSR 304
Cdd:PRK09698 219 SLLENLARAIATSINLFDPDAIILGGGvMDMPAFPRETLIAMIQKYLRKplPYEVVRFIYASSSDFNGAQGAAILAHQR 297
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
5-300 |
4.18e-30 |
|
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar proteins; N-acetylmannosamine kinase (NanK; EC 2.7.1.60), also called ManNAc kinase, or N-acetyl-D-mannosamine kinase, catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. It has also low level glucokinase activity in vitro. This subfamily also contains Brucella melitensis bifunctional enzyme NanE/NanK (EC 5.1.3.9/EC 2.7.1.60), which also converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466919 [Multi-domain] Cd Length: 283 Bit Score: 115.07 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 5 LDIGGTKIELA-VFNSQLEKqySERVETPKT-SYEDWLNAIVNLVKKADEKFGCkgsVGLGIPGFVNQSTGIA-EITNIR 81
Cdd:cd24069 3 IDIGGTKIAAAlIGNGQIID--RRQIPTPRSgTPEALADALASLLADYQGQFDR---VAVASTGIIRDGVLTAlNPKNLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 82 VADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQLN 161
Cdd:cd24069 78 GLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 162 YHALkllgwdnapiyQCGCGNIACLDTYLSGRGFEMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGNI 241
Cdd:cd24069 158 PPGP-----------VCGCGRRGCVEAIASGTAIAAAASEILGEPVDAKDVFERARSGDEEAARLIDRAARALADLIADL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502357555 242 ITAFDPHLIVLGGGLSNFDYLYEALPKALPA--HLMRtakvPVIKKAKYGDSGGVRGAAAL 300
Cdd:cd24069 227 KATLDLDCVVIGGSVGLAEGFLERVEQYLADepAIFR----VSLEPARLGQDAGLLGAALL 283
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
4-303 |
6.89e-29 |
|
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: 112.38 E-value: 6.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTS-YEDWLNAIVNLVKKADEKFGCKGS---VGLGIPGFVNQSTGIAEITN 79
Cdd:cd24071 5 GVKIEEGYLVLALTDLKGKILEKTRIPFDHETdPEKVIELIAENIKKLIKNKHVEKKllgIGIAVSGLVDSKKGIVIRST 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 80 IRVADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQ 159
Cdd:cd24071 85 ILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIGHMT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 160 LNYHAlkllgwdnapiYQCGCGNIACLDTYLSGRGFEMFYRDLK----------GESLSAKDIIQRFYAGDKSAVDFVGV 229
Cdd:cd24071 165 IQPDG-----------RKCYCGQKGCLEAYASFEALVNEIKELTesyplsllkeLEDFEIEKVREAAEEGDSVATELFKK 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502357555 230 FIELAAISIGNIITAFDPHLIVLGG-GLSNFDYLYEALPKALPAH-LMRTAKVPVIKKAKYGDSGGVRGAAALFLS 303
Cdd:cd24071 234 AGEYLGIGIKNLINIFNPEAIIIGGeGLEFKDYFLPKIIEIAKENfFGKAGRNVIILVDSLGEDAWVLGAALLVID 309
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
4-276 |
1.13e-28 |
|
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: 111.74 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEK--QYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIPGFVNQSTGIAEITNIR 81
Cdd:cd24072 5 GIVVSPNSLRAQVGNACGELlgEFEYRVITLETPEALIDEIIDCIDRLLKLWKDRVKGIALAIQGLVDSHKGVSLWSPGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 82 VADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQLN 161
Cdd:cd24072 85 PWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGHTKVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 162 YHALkllgwdnapiyQCGCGNIACLDTYLS--------GRGFEMFYRDLKGESLSAKDIIQRFYAGDKSAVDFVGVFIEL 233
Cdd:cd24072 165 PDGA-----------RCDCGRRGCLETVASnsalkrnaRVTLKLGPVSADPEKLTMEQLIEALEEGEPIATQIFDRAANA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 502357555 234 AAISIGNIITAFDPHLIVL-GGGLSNFDYLYEALPKALPAHLMR 276
Cdd:cd24072 234 IGRSLANILNLLNPEQVLLyGRGCRAGDLLLPAIRRAIAENPFS 277
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
4-304 |
2.85e-27 |
|
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: 107.63 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSERVETPKTSYEDWLNAIVNLVKKA-----DEKFGCKGsVGLGIPGFVNQSTGIaeIT 78
Cdd:cd24077 5 GIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENILEILKSIIQELisqapKTPYGLVG-IGIGIHGIVDENEII--FT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 79 NIRVADNKPILRDLSALLEREVRAENDANCFALseawdAENAQYPSVLGLI---LGTGFGGGFVINGKIHSGQTGMAGEL 155
Cdd:cd24077 82 PYYDLEDIDLKEKLEEKFNVPVYLENEANLSAL-----AERTFSEDYDNLIsisIHSGIGAGIIINNQLYRGYNGFAGEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 156 GHLQLNYHAlkllgwdnapiYQCGCGNIACLDTYLSGRGFEMFYRDLKG-ESLSAKDIIQRFYAGDKSAVDFVGVFIELA 234
Cdd:cd24077 157 GHMIIVPNG-----------KPCPCGNKGCLEQYASEKALLKELSEKKGlETLTFDDLIQLYNEGDPEALELIDQFIKYL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502357555 235 AISIGNIITAFDPHLIVLGGGLSNfdYLYEALPKaLPAHL-MRTAKVPVIKKAKYGDSGGVRGAAALFLSR 304
Cdd:cd24077 226 AIGINNIINTFNPEIIIINSSLIN--EIPELLEK-IKEQLsSSFNKYVEILISTLGKNATLLGGAAVAIKN 293
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
6-282 |
3.17e-27 |
|
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: 107.89 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 6 DIGGTKIELAVFNSQLEKQYSERVETPKTsYEDWLNAIVNLVKKA---DEKFGCK-GSVGLGIPGFVNQSTGIAEITNIR 81
Cdd:cd24060 6 DLGGTNLRVAIVSMKGEIVKKYTQPNPKT-YEERIDLILQMCVEAaseAVKLNCRiLGVGISTGGRVNPREGIVLHSTKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 82 VADNKPI-LRD-LSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQ 159
Cdd:cd24060 85 IQEWSSVdLRTpISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELGHIV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 160 LNYhalkllgwdNAPiyQCGCGNIACLDTYLSGRGFEMFYRDL--------------KGESLSAKDIIQRFYAGDKSAVD 225
Cdd:cd24060 165 VSL---------DGP--DCMCGSHGCVEAYASGMALQREAKKLhdedlllvegmsvtNDEEVTAKHLIQAAKLGNAKAQK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 226 FVGVFIELAAISIGNIITAFDPHLIVLGGGLSNF--DYLYEALP-KALPAhlMRTAKVPV 282
Cdd:cd24060 234 ILRTAGTALGLGIVNILHTLNPSLVILSGVLASHyeNIVKDVIAqRALPS--VQNVDVVV 291
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
7-254 |
1.00e-16 |
|
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: 78.95 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 7 IGGTKIELAVFN--SQL--EKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIPGFVNQSTGIAEITNIRV 82
Cdd:cd24075 8 LGRHDLTLGLYDlsGELlaEHTVPLTALNQEALLSQLIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVVHYMPHIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 83 ADNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGQTGMAGELGHLQLNY 162
Cdd:cd24075 88 VKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEIGHIQIEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 163 halklLGwdnapiYQCGCGNIACLDTYLSGRGFEMFYRDLK---------GESLSAKDIIQRFYAGDKSAVDfvgvFIEL 233
Cdd:cd24075 168 -----LG------ERCHCGNFGCLETVASNAAIEQRVKKLLkqgyasqltLQDCTIKDICQAALNGDQLAQD----VIKR 232
|
250 260
....*....|....*....|....*
gi 502357555 234 AAISIGNIITA----FDPHLIVLGG 254
Cdd:cd24075 233 AGRYLGKVIAIlinlLNPQKIIIAG 257
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
5-301 |
2.03e-16 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 77.65 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 5 LDIGGTKIELAVFNSqlEKQYSERVE--TPKTSYEDWLN-AIVNLVKKADEKFGckgSVGLGipgfvnqSTGIaeITN-I 80
Cdd:PRK05082 6 IDIGGTKIAAALVGE--DGQIRQRRQipTPASQTPEALRqALSALVSPLQAQAD---RVAVA-------STGI--INDgI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADNKPILRDLSAL-LEREVRAENDANCFALSEAWDAENAQY----PSVLGLI---LGTGFGGGFVINGKIHSGQTGMA 152
Cdd:PRK05082 72 LTALNPHNLGGLLHFpLVQTLEQLTDLPTIALNDAQAAAWAEYqalpDDIRNMVfitVSTGVGGGIVLNGKLLTGPGGLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 153 GELGHlqlnyhalkLLGWDNAPIyqCGCGNIACLDTYLSGRGFEMFYRDLKGEsLSAKDIIQRFYAGDKSAVDFVGVFIE 232
Cdd:PRK05082 152 GHIGH---------TLADPHGPV--CGCGRRGCVEAIASGRAIAAAAQGWLAG-CDAKTIFERAGQGDEQAQALINRSAQ 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502357555 233 LAAISIGNIITAFDPHLIVLGG--GLSNfDYLyEALPKALpAHLMRTAKVPVIkKAKYGDSGGVRGAAALF 301
Cdd:PRK05082 220 AIARLIADLKATLDCQCVVLGGsvGLAE-GYL-ELVQAYL-AQEPAIYHVPLL-AAHYRHDAGLLGAALWA 286
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
4-300 |
2.39e-12 |
|
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: 66.03 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQysERVETPKTSYEDWLNAIVNLVKKADEKFgckgsVGLGIPGF----VN-QSTGIAEIT 78
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNII--ERTEFPTTTPEETLQAVIDFFREQEEPI-----DAIGIASFgpidLNpTSPTYGYIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 79 NIRVA--DNKPILRDLSALLEREVRAENDANCFALSEAWDAENAQYPSVLGLILGTGFGGGFVINGKIHSGqTGMAgELG 156
Cdd:cd24067 76 TTPKPgwRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHG-LLHP-EMG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 157 HLQLNYHAlkllgWDNAPIYQCGCGNiACLDTYLSGRGFEMFYrDLKGESLSAkdiiqrfyagDKSAVDFVGVFIELAAI 236
Cdd:cd24067 154 HIRVPRHP-----DDDGFPGVCPFHG-DCLEGLASGPAIAARW-GIPAEELPD----------DHPAWDLEAYYLAQACA 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502357555 237 sigNIITAFDPHLIVLGGGLSN----FDYLYEALPKAL---PAHLMRTAKVP-VIKKAKYGDSGGVRGAAAL 300
Cdd:cd24067 217 ---NLTLTLSPERIVLGGGVMQrpglFPRIREKFRKLLngyLEVPRLLPDIDeYIVPPALGNDAGILGALAL 285
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
4-160 |
2.05e-10 |
|
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: 59.89 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNSQLEKQYSER--VETPKTSYEDwlnAIVNLVKKADEKFGCKGSVGLGIPGFVNQstGIAeITNIR 81
Cdd:cd24058 3 GIDIGGSGIKGAIVDTDTGELLSERirIPTPQPATPE---AVADVVAELVAHFPWFGPVGVGFPGVVRR--GVV-RTAAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 82 VAD---NKPILRDLSALLEREVRAENDANCFALSEA-WDAENAQYPSVLGLILGTGFGGGFVINGKI--HSgqtgmagEL 155
Cdd:cd24058 77 LDKswiGFDAAKLLSKRLGRPVRVLNDADAAGLAEMkGGAGKGEKGVVLVLTLGTGIGSALFVDGHLvpNT-------EL 149
|
....*
gi 502357555 156 GHLQL 160
Cdd:cd24058 150 GHLEI 154
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
104-298 |
2.11e-10 |
|
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: 60.40 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 104 NDANCFALSE-----AWDAENAQYpsvlgLILGTGFGGGFVINGKIHSGQTGMAGELGHLQLNYHALKllgwdnapiyqC 178
Cdd:cd24074 110 HDISAWTLAErffgaAKGAKNIIQ-----IVIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKR-----------C 173
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 179 GCGNIACLDTYLSGRGFEMFYRD---------LKGESLSAKDIIQRFYAGDKSAVDFVGVFIELAAISIGNIITAFDPHL 249
Cdd:cd24074 174 YCGNHGCLETVASIPAILEQANQlleqspdsmLHGQPISIESLCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEK 253
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502357555 250 IVLGGGLSNF-DYLYEAL-----PKALPAHLMRTAkvpvIKKAKYGDSGGVRGAA 298
Cdd:cd24074 254 ILIGSPLNNAaEILFPALsqsirQQSLPAYSQHLQ----IESTKFYNDGTMPGAA 304
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| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
6-262 |
1.32e-09 |
|
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: 58.00 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 6 DIGGTKIELAVFN-SQLEKQYSERVETPKTSYEDwLNAIVNLVKKADEKFGCKGSVgLGIPGFVNQstGIAEITN----I 80
Cdd:cd24008 5 DIGGTNARLALADaGDGSGDLLFVRKYPSADFAS-LEDALAAFLAELGAPRPKAAC-IAVAGPVDG--GRVRLTNldwsI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 81 RVADnkpiLRdlSALLEREVRAEND--ANCFALSEAWDAE----------NAQYPSVLgLILGTGFGGGFVINGKIHSGQ 148
Cdd:cd24008 81 DAAE----LR--KALGIGRVRLLNDfeAAAYGLPALGPEDllvlyggggpLPGGPRAV-LGPGTGLGVALLVPDGDGGYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 149 TgMAGELGHLQ-----------LNYHALKLlgwdnapiyqcgcGNIACLDTYLSGRGFEMFYR------DLKGESLSAKD 211
Cdd:cd24008 154 V-LPSEGGHADfapvteeeaelLEFLRKRF-------------GRSVSYEDVLSGPGLENIYEflakldGAEPPDLTAEE 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502357555 212 IIQRFYAGDKSAVDFVGVFIELAAISIGNIITAFDPHL-IVLGGGL--SNFDYL 262
Cdd:cd24008 220 IAEAALAGDPLAREALDLFARILGRFAGNLALSFLATGgVYLAGGIapKNLDLL 273
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| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
3-157 |
8.89e-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: 37.25 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 3 YGLDIGGTKIELAVFN-------SQLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKGSVGLGIP-GFVNQSTGI 74
Cdd:cd24000 46 LAIDLGGTNLRVALVSldgkgieVTISKKYEIPDEIKTASAEEFFDFIADCIAEFLKENGLKKPLPLGFTfSFPLEQTSL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 75 --AEIT------NIRVADNKPILRDL-SALLEREVRAE-----NDANCFALSEAWdaenAQYPSVLGLILGTGFGGGFVI 140
Cdd:cd24000 126 ndGKLLswtkgfKIPGVEGKDVGELLnDALKKRGLPVKvvavlNDTVATLLAGAY----KDPDCRIGLILGTGTNAAYLE 201
|
170 180
....*....|....*....|
gi 502357555 141 -NGKIHSGQTGMA--GELGH 157
Cdd:cd24000 202 pTSNILLGDGGMIinTEWGN 221
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| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
4-158 |
9.38e-03 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466857 [Multi-domain] Cd Length: 295 Bit Score: 37.28 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 4 GLDIGGTKIELAVFNS---QLEKQYSERVETPKTSYEDWLNAIVNLVKKADEKFGCKG---SVGLGIPGFVNQstgiAEI 77
Cdd:cd24007 3 GVDGGGTKTRAVLADEdgkILGRGKGGPSNPASVGIEEAKENLKEAVREALSQAGSLGeidAICLGLAGIDSE----EDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502357555 78 TNIRvadnkPILRDLsaLLEREVRAENDANCfALSEAWDAEnaqyPSVLgLILGTGfGGGFVINGKihsGQTGMAGELGH 157
Cdd:cd24007 79 ERLR-----SALKEL--FLSGRIIIVNDAEI-ALAAALGGG----PGIV-VIAGTG-SVAYGRNGD---GEEARVGGWGH 141
|
.
gi 502357555 158 L 158
Cdd:cd24007 142 L 142
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