|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
1-300 |
0e+00 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 610.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 1 MRIGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGSVGVGIPGTLSPFTGKVKNANS 80
Cdd:PRK09557 1 MRIGIDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTIEAIATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKNANS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 81 VWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNPL 160
Cdd:PRK09557 81 TWLNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWGHNPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 161 PWQNEEERQYQQEVACYCGKKGCIETFVSGTGFATDYFRMSGKQLKGHEIIALVAQGDAIAEQAMSHYEQRFAKSLAHVI 240
Cdd:PRK09557 161 PWMDEDELRYRNEVPCYCGKQGCIETFISGTGFATDYRRLSGKALKGSEIIRLVEEGDPVAELAFRRYEDRLAKSLAHVI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 241 NLFDPDVVVLGGGMSNVDRLYTTLPALISPWVFGGECQTPVRKALHGDSSGVRGAAWLWP 300
Cdd:PRK09557 241 NILDPDVIVLGGGMSNVDRLYPTLPALLKQYVFGGECETPVRKALHGDSSGVRGAAWLWP 300
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
2-298 |
2.24e-175 |
|
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: 486.33 E-value: 2.24e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 2 RIGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGSVGVGIPGTLSPFTGKVKNANSV 81
Cdd:cd24066 1 RIGIDLGGTKIEGIALDRAGRELLRRRVPTPRGDYEATLDAIADLVEEAEEELGAPATVGIGTPGSISPRTGLVKNANST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 82 WLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNPLP 161
Cdd:cd24066 81 WLNGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGHNPLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 162 WQNEEERqyqQEVACYCGKKGCIETFVSGTGFATDYFRMSGKQLKGHEIIALVAQGDAIAEQAMSHYEQRFAKSLAHVIN 241
Cdd:cd24066 161 WPDEDEL---PGPPCYCGKRGCVETFLSGPALERDYARLTGKTLSAEEIVALARAGDAAAVATLDRFLDRLGRALANVIN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 491331318 242 LFDPDVVVLGGGMSNVDRLYTTLPALISPWVFGGECQTPVRKALHGDSSGVRGAAWL 298
Cdd:cd24066 238 ILDPDVIVLGGGLSNIDELYTEGPAALARYVFSDEVETPIVKNKHGDSSGVRGAAWL 294
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
1-298 |
1.02e-104 |
|
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: 307.62 E-value: 1.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 1 MRIGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGSVGVGIPGTLSPFTGKVKNANS 80
Cdd:cd24057 1 MYYGFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAAFLAAIAELVAEADARFGVKGPVGIGIPGVIDPEDGTLITANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 81 VWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNPL 160
Cdd:cd24057 81 PAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 161 PWQNEEERQYQQEVACYCGKKGCIETFVSGTGFATDYFRMSGKQLKGHEIIALVAQGDAIAEQAMSHYEQRFAKSLAHVI 240
Cdd:cd24057 161 PADALLLGYDLPVLRCGCGQTGCLETYLSGRGLERLYAHLYGEELDAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLANIL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 491331318 241 NLFDPDVVVLGGGMSNVDRLYTTLPALISPWVFGGeCQTP-VRKALHGDSSGVRGAAWL 298
Cdd:cd24057 241 TALDPDVVVLGGGLSNFPALIAELPAALPAHLLSG-ARTPrIVPARHGDAGGVRGAAFL 298
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
3-301 |
1.65e-94 |
|
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: 281.15 E-value: 1.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTL-QAIATLVADAEQATGQQGSVGVGIPGTLSPFTGKV-KNANS 80
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEETLvDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYItNTPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 81 VWLNgQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNPL 160
Cdd:pfam00480 81 GWDN-FDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 161 PwqneeerqyQQEVACYCGKKGCIETFVSGTGFATDYfRMSGKQLKGHEIIALVAQGDAIAEQAMSHYEQRFAKSLAHVI 240
Cdd:pfam00480 160 D---------PNGPKCGCGNHGCLETIASGRALEKRY-QQKGEDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLI 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491331318 241 NLFDPDVVVLGGGMSNVDRLYTTLPALISPWVFGGECQTPVR--KALHGDSSGVRGAAWLWPT 301
Cdd:pfam00480 230 NLFDPQAIVLGGGVSNADGLLEAIRSLVKKYLNGYLPVPPVIivAASLGDNAGALGAAALAKQ 292
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-299 |
1.27e-90 |
|
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: 271.77 E-value: 1.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 1 MRIGIDLGGTKIEVIALANDGQELFRKRVDTP-RHDYQNTLQAIATLVADAEQATGQQGS----VGVGIPGTLSPFTGKV 75
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTPaGAGPEAVLEAIAELIEELLAEAGISRGrilgIGIGVPGPVDPETGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 76 KNANSV-WLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGE 154
Cdd:COG1940 86 LNAPNLpGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 155 WGHNPLPWQNEEerqyqqevaCYCGKKGCIETFVSGTGFATDYFRMSG-KQLKGHEIIALVAQGDAIAEQAMSHYEQRFA 233
Cdd:COG1940 166 IGHMPVDPDGPL---------CGCGNRGCLETYASGPALLRRARELGGaEKLTAEELFAAARAGDPLALEVLDEAARYLG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491331318 234 KSLAHVINLFDPDVVVLGGGMSNV-DRLYTTLPALISPWVFGGEC-QTPVRKALHGDSSGVRGAAWLW 299
Cdd:COG1940 237 IGLANLINLLDPEVIVLGGGVSAAgDLLLEPIREALAKYALPPAReDPRIVPASLGDDAGLLGAAALA 304
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
1-298 |
1.25e-87 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 264.16 E-value: 1.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 1 MRIGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGSVGVGIPGTLSPFTGKVKNANS 80
Cdd:PRK13310 1 MYYGFDIGGTKIELGVFNEKLELQWEERVPTPRDSYDAFLDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLYAANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 81 VWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNPL 160
Cdd:PRK13310 81 PAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHMRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 161 PWQ-----NEEERQYQqevaCYCGKKGCIETFVSGTGFATDYFRMSGKQLKGHEIIALVAQGDaiaEQAMSHYEqRF--- 232
Cdd:PRK13310 161 PVDaltllGWDAPLRR----CGCGQKGCIENYLSGRGFEWLYQHYYGEPLQAPEIIALYYQGD---EQAVAHVE-RYldl 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491331318 233 -AKSLAHVINLFDPDVVVLGGGMSNVDRLYTTLPALISPWVFGGECQTPVRKALHGDSSGVRGAAWL 298
Cdd:PRK13310 233 lAICLGNILTIVDPHLVVLGGGLSNFDAIYEQLPKRLPRHLLPVARVPRIEKARHGDAGGVRGAAFL 299
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
3-298 |
1.26e-53 |
|
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: 176.59 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNT-LQAIATLVADAEQATGQQGsVGVGIPGTLSPFTGKVK--NAN 79
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAiLERLLEIIAELKEKYDIEG-IGISSAGQVDPKTGEVIyaTDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 80 SVWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNP 159
Cdd:cd24068 82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 160 LPWQNEEerqyqqevaCYCGKKGCIETFVSGTGFATDYFRMSGK-QLKGHEIIALVAQGDAIAEQAMSHYEQRFAKSLAH 238
Cdd:cd24068 162 VDPGGRP---------CCCGGKGCLEQYASGTALVRRVAEALGEpGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLAN 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491331318 239 VINLFDPDVVVLGGGMSN-----VDRLYTTLPALISPWVFGGecqTPVRKALHGDSSGVRGAAWL 298
Cdd:cd24068 233 LVHIFDPEVIVIGGGISAqgelfLEELREELRKLLMPPLLDA---TKIEPAKLGNDAGLLGAAYL 294
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
1-237 |
1.04e-47 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 160.19 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 1 MRIGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGSVGVGIPGTLSPFTGKVKNANS 80
Cdd:PRK13311 1 MYYGFDMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGSVGIGIPGLPNADDGTVFTANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 81 VWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNPL 160
Cdd:PRK13311 81 PSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491331318 161 PWQNEEERQYQ-QEVACYCGKKGCIETFVSGTGFATDYFRMSGKQLKGHEIIALVAQGDAiaeQAMSHYEqRFAKSLA 237
Cdd:PRK13311 161 PVDALDILGADiPRVPCGCGHRGCIENYISGRGFEWMYSHFYQHTLPATDIIAHYAAGEP---KAVAHVE-RFMDVLA 234
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
3-296 |
1.66e-46 |
|
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: 158.26 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEViALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGSVGVGIPGTLSPFTGKVKNA-NSV 81
Cdd:cd24065 3 IGLDLGGTKIAA-GVVDGGRILSRLVVPTPREGGEAVLDALARAVEALQAEAPGVEAVGLGVPGPLDFRRGRVRFApNIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 82 WLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGH---- 157
Cdd:cd24065 82 GLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHttvl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 158 --NPLpwqneeerqyqqevaCYCGKKGCIETFVSGTGFATDYFRMSGKQLKGHEIIALVAQGDAIA----EQAMSHyeqr 231
Cdd:cd24065 162 pgGPM---------------CGCGLVGCLEALASGRALARDASFAYGRPMSTAELFELAQQGEPKAlrivEQAAAH---- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491331318 232 FAKSLAHVINLFDPDVVVLGGGMSNVDRLYTTLPALISPWVFGGECQTPVRKALHGDSSGVRGAA 296
Cdd:cd24065 223 LGIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARRYTEGWHAPPLRLAHLGTDAGVIGAA 287
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
3-298 |
2.58e-45 |
|
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: 153.39 E-value: 2.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRH-DYQNTLQAIATLVADAEQATGQQG---SVGVGIPGTLSPFTGKVKNA 78
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEeGPEAVLDRIAELIEELLAEAGVRErilGIGIGVPGPVDPETGIVLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 79 -NSVWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGH 157
Cdd:cd23763 81 pNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 158 NPLpwqneeerqyqqevacycgkkgcietfvsgtgfatdyFRMSGKQLkgheiialvaqgdAIAeqamshyeqrfaksLA 237
Cdd:cd23763 161 ITV-------------------------------------LEEAARYL-------------GIG--------------LA 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491331318 238 HVINLFDPDVVVLGGGMSNV-DRLYTTLPALISPWVF-GGECQTPVRKALHGDSSGVRGAAWL 298
Cdd:cd23763 177 NLINLLNPELIVLGGGVAEAgDLLLEPIREAVRRRALpPLRRRVRIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
3-296 |
6.79e-41 |
|
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: 143.86 E-value: 6.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTP-RHDYQNTLQAIATLVADAEQATGQQGS----VGVGIPGTLSPFTGKVKN 77
Cdd:cd24076 4 IGVELGVDYITVVVTDLAGEVLWRREVPLPaSDDPDEVLAQLAALIREALAAAPDSPLgilgIGVGVPGLVDSEDGVVLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 78 A-NSVWLN---GQMLdkdlSELLSRPVRLANDANCLAVSEATDGAGAGK-HLVFAAIiGTGCGSGIAIDGRVHAGGNGIA 152
Cdd:cd24076 84 ApNLGWRDvplRDLL----EEALGVPVFVDNEANAAALAEKRFGAGRGVsDLVYLSA-GVGIGAGIILDGELYRGASGFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 153 GEWGHNPLpwqNEEERQyqqevaCYCGKKGCIETFVSGTGFATDYFRMSGKQLKG--HEIIALVAQGDAIA----EQAMS 226
Cdd:cd24076 159 GEIGHMTV---DPDGPP------CSCGNRGCWETYASERALLRAAGRLGAGGEPLslAELVEAARAGDPAAlaalEEVGE 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491331318 227 HyeqrFAKSLAHVINLFDPDVVVLGGGMSNV-----DRLYTTLPALISPWVFGgecQTPVRKALHGDSSGVRGAA 296
Cdd:cd24076 230 Y----LGIGLANLVNTFNPELVVLGGALAPLgpwllPPLRAEVARRALPAPAR---DVRIVVSRLGEDAAALGAA 297
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
3-260 |
1.17e-40 |
|
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: 143.26 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPrHDYQNTLQAIATLVADAeQATGQQGSVGVGIPGTLSPFTGKVKNANSVW 82
Cdd:cd24061 2 IGVDIGGTKIAAGVVDEEGEILATERVPTP-PTADGIVDAIVEAVEEL-REGHDVSAVGVAAAGFVDADRATVLFAPNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 83 LNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHnplpw 162
Cdd:cd24061 80 WRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGH----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 163 qneeERQYQQEVACYCGKKGCIETFVSGT---------------GFATDYFRMSGKQLKGHEIIALVAQGDAIAEQAMSH 227
Cdd:cd24061 155 ----IRVVPDGLLCGCGSRGCWEQYASGRalvryakeaanatpeGAAVLLADGSVDGITGKHISEAARAGDPVALDALRE 230
|
250 260 270
....*....|....*....|....*....|...
gi 491331318 228 YEQRFAKSLAHVINLFDPDVVVLGGGMSNVDRL 260
Cdd:cd24061 231 LARWLGAGLASLAALLDPELFVIGGGVSDAGDL 263
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
3-298 |
5.38e-40 |
|
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: 141.66 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHD-YQNTLQAIA-----TLVADAEQATGQQGsVGVGIPGTLSPFTGKVK 76
Cdd:cd24062 3 VGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEgGENIITDIAesiqqLLEELGYSKEDLIG-IGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 77 NANSVWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAG-KHLVFAAiIGTGCGSGIAIDGRVHAGGNGIAGEW 155
Cdd:cd24062 82 VAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGaKDLVFIT-LGTGVGGGVIANGKIVHGANGAAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 156 GHNPLpwqNEEErqyqqEVACYCGKKGCIETFVSGTGF--------------ATDYFRMSGKQLKGHEIIALVAQGDAIA 221
Cdd:cd24062 161 GHITV---NPEG-----GAPCNCGKTGCLETVASATGIvriareeleegkgsSALRILALGGELTAKDVFEAAKAGDELA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 222 EQAMSHYEQRFAKSLAHVINLFDPDVVVLGGGMSN-----VDRLYTTLPALISPWVFGGecqTPVRKALHGDSSGVRGAA 296
Cdd:cd24062 233 LAVVDTVARYLGLALANLANTLNPEKIVIGGGVSAageflLSPVKEYFDRFTFPRVRQD---TEIVLATLGNDAGVIGAA 309
|
..
gi 491331318 297 WL 298
Cdd:cd24062 310 WL 311
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
1-264 |
4.37e-37 |
|
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: 133.46 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 1 MRIGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADA-EQATGqqgsVGVGIPGTLSPFTGKVKNAN 79
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPTPKDSLEEFLDYIKKIIKRYdEEIDG----IAISAPGVIDPETGIIYGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 80 S-VWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHn 158
Cdd:cd24152 77 AlPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSY- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 159 pLPWQNEEERQYQQEVACycgkkgcietfvSGTGFATDYFRMSGKQ-LKGHEIIALVAQGDAIAEQAMSHYEQRFAKSLA 237
Cdd:cd24152 156 -LLTDDDDKDLLFFSGLA------------SMFGLVKRYNKAKGLEpLDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIY 222
|
250 260
....*....|....*....|....*..
gi 491331318 238 HVINLFDPDVVVLGGGMSNVDRLYTTL 264
Cdd:cd24152 223 NIQYILDPEVIVIGGGISEQPLFIEDL 249
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
3-298 |
2.23e-35 |
|
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: 130.02 E-value: 2.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLqAIATLVADAEQATGQQG----SVGVGIPGTLSPFTGKVKNA 78
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVD-AIASAVDSFIQHIAKVGheivAIGIGAPGPVNRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 79 NSVWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHN 158
Cdd:TIGR00744 80 VNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 159 PLpwqneeerQYQQEVACYCGKKGCIETFVSGTG-------------FATDYFRM-SGKQLKGHEIIALVAQGDAIAEQA 224
Cdd:TIGR00744 160 RM--------VPDGRLLCNCGKQGCIETYASATGlvryakranakpeRAEVLLALgDGDGISAKHVFVAARQGDPVAVDS 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491331318 225 MSHYEQRFAKSLAHVINLFDPDVVVLGGGMSNV-DRLYTTLPALISPWVFGGECQ-TPVRKALHGDSSGVRGAAWL 298
Cdd:TIGR00744 232 YREVARWAGAGLADLASLFNPSAIVLGGGLSDAgDLLLDPIRKSYKRWLFGGARQvADIIAAQLGNDAGLVGAADL 307
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
3-296 |
3.99e-35 |
|
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: 128.44 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEvIALANDGQEL--FRKRVDTPRHDYQNTLQAIATLVADA-EQATGQQGSVGVGIPGTLSPFTGKVKNAN 79
Cdd:cd24070 4 LGIDIGGTNIR-IGLVDEDGKLldFEKVPSKDLLRAGDPVEVLADLIREYiEEAGLKPAAIVIGVPGTVDKDRRTVISTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 80 SV-WLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHN 158
Cdd:cd24070 83 NIpGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 159 PLPwqNEEERqyqqevaCYCGKKGCIETFVSG---TGFATDYFrmsgkqlKGHEIIALVAqgDAIAEQAMSHYEQRFAKS 235
Cdd:cd24070 163 PVY--GNGKP-------CGCGNTGCLETYASGralEEIAEEHY-------PDTPILDIFV--DHGDEPELDEFVEDLALA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491331318 236 LAHVINLFDPDVVVLGGGMSNV-----DRL------YTTLPALISPWVFggecqtpvRKALHGDSSGVRGAA 296
Cdd:cd24070 225 IATEINILDPDAVILGGGVIDMkgfprETLeeyirkHLRKPYPADNLKI--------IYAELGPEAGVIGAA 288
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
3-296 |
3.64e-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: 123.43 E-value: 3.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEViALAN-DGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGS----VGVGIPGTLSPFTGKVKN 77
Cdd:cd24073 4 VGVKLTEDRITA-VLTDlRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSPDrllgIGVGLPGLVDAETGICRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 78 A-NSVWLN---GQMLdkdlSELLSRPVRLANDANCLAVSEATDGAGAGkHLVFAAI-IGTGCGSGIAIDGRVHAGGNGIA 152
Cdd:cd24073 83 SpLLGWRDvplAELL----EERLGLPVYVENDVNALALAEHWFGAGRG-LDNFAVVtIGRGIGCGLVVDGRLYRGAHGGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 153 GEWGHNPL----PwqneeerqyqqevACYCGKKGCIETFVSGTGFATDYFRMSGKQLKG--HEIIALVAQGDAIAEQAMS 226
Cdd:cd24073 158 GEIGHTTVdpdgP-------------PCRCGKRGCLEAYASDPAILRQAREAGLRGEPLtiEDLLAAARAGDPAARAILR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491331318 227 HYEQRFAKSLAHVINLFDPDVVVLGG-GMSNVDRLYTTLPALISPWVFGGEcQTPVRKALH--GDSSGVRGAA 296
Cdd:cd24073 225 RAGRALGLALANLVNLLDPELIIISGeGVRAGDLLFEPMREALRAHVFPGL-ASDLELVIHpwGDEAWARGAA 296
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
3-296 |
2.38e-31 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 118.93 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQ-GSVGVGIPGTLS---PFTGKVKNA 78
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVSGLGEMIDEYLRRFNARcHGIVMGFPALVSkdrRTVISTPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 79 NSVWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKhLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHn 158
Cdd:PRK09698 87 PLTALDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKENNLTQQ-LVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELGH- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 159 pLPWQNEEERqyqqevaCYCGKKGCIETFVSGTGFATDYfrmsGKQLKGHEIIALVAqgDAIAEQAMSHYEQRFAKSLAH 238
Cdd:PRK09698 165 -IPLGDMTQH-------CGCGNPGCLETNCSGMALRRWY----EQQPRDYPLSDLFV--HAGDHPFIQSLLENLARAIAT 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491331318 239 VINLFDPDVVVLGGG-MSNVDRLYTTLPALISPWVFGGECQTPVR--KALHGDSSGVRGAA 296
Cdd:PRK09698 231 SINLFDPDAIILGGGvMDMPAFPRETLIAMIQKYLRKPLPYEVVRfiYASSSDFNGAQGAA 291
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
3-256 |
2.52e-30 |
|
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: 116.28 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTL-QAIATLVADAEQATGQQGSVGVGIpGTLSPF---TGKVKNA 78
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVsEQVLGLIETLLSKAGKDSIEGIGV-SSAGPLdlrKGTIVNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 79 NSVWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGK-HLVFAAIiGTGCGSGIAIDGRVHAGGNGIAGEWGH 157
Cdd:cd24063 82 PNIKGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTsNLVYITI-STGIGGGVIVDGRLLLGKNGNAAEVGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 158 npLPWQNEEERQyqqevaCYCGKKGCIETFVSGTGFA---------TDYFRMSGKQLKG------HEIIALVAQGDAIAE 222
Cdd:cd24063 161 --LVVDTESGLK------CGCGGYGHWEAFASGRGIPrfarewaegFSSRTSLKLRNPGgegitaKEVFSAARKGDPLAL 232
|
250 260 270
....*....|....*....|....*....|....
gi 491331318 223 QAMSHYEQRFAKSLAHVINLFDPDVVVLGGGMSN 256
Cdd:cd24063 233 KIIEKLARYNGRGIANVINAYDPELIVIGGSVFN 266
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
3-255 |
7.77e-28 |
|
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: 109.51 E-value: 7.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHD-YQNTLQAIATLVADAEQATGQQGsVGVGIPGTLSPFTGKVKNANSV 81
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENgKEDVINRIAETVNELIEEMELLG-IGIGSPGSIDRENGIVRFSPNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 82 --WLNGQMLDKdLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNP 159
Cdd:cd24064 81 pdWRNFPLVPL-IEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 160 LpwqneEERQYQqevaCYCGKKGCIETFVSGTGFAT----------DYFRMSGKQLKGHEIIALVAQGDAIAEQAMSHYE 229
Cdd:cd24064 160 V-----EPNGPI----CGCGNRGCVEAFASATAIIRyaresrkrypDSLAGESEKINAKHVFDAARKNDPLATMVFRRVV 230
|
250 260
....*....|....*....|....*.
gi 491331318 230 QRFAKSLAHVINLFDPDVVVLGGGMS 255
Cdd:cd24064 231 DALAIAIGGFVHIFNPEIIIIGGGIS 256
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
3-296 |
2.75e-26 |
|
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: 105.36 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEViALAN-DGQELFRKRVDTPRHD-YQNTLQAIATLVAD-AEQATGQQ--GSVGVGIPGTLSPFTGKVKN 77
Cdd:cd24059 4 IGVEIGRDLLSA-VLCDlSGNILAREKYPLDEKEnPEEVLEKLYELIDRlLEKENIKSkiLGIGIGAPGPLDVEKGIILN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 78 ANSVWLNGQM-LDKDLSELLSRPVRLANDANCLAVSEATDGAGAG-KHLVFAaIIGTGCGSGIAIDGRVHAGGNGIAGEW 155
Cdd:cd24059 83 PPNFPGWENIpLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNyDNFIYI-LADEGIGAGIIINGKLYRGVDGYAGEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 156 GHNPLPWQNEEerqyqqevaCYCGKKGCIETFVSGTGFaTDYFRMSGKQL--KGHEIIALVAQGDAIAEQAMSHYEQRFA 233
Cdd:cd24059 162 GHTSIDINGPR---------CSCGNRGCLELYASIPAI-EKKARSALGSGrsFQLDIVEALQKGDPIADEVIEEAAKYLG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491331318 234 KSLAHVINLFDPDVVVLGGGMSNV-DRLYTTLPALISPWVFG-GECQTPVRKALHGDSSGVRGAA 296
Cdd:cd24059 232 IGLVNLINLLNPEAIIIGGELIYLgERYLEPIEKEVNSRLFGrNAREVRILKSSLGEDAPLLGAA 296
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
5-298 |
5.08e-25 |
|
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: 101.21 E-value: 5.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 5 IDLGGTKIEViALANDGQELFRKRVDTPR-HDYQNTLQAIATLVADAEqatGQQGSVGVGIPGTLSPFTGKVKNANSVW- 82
Cdd:cd24069 3 IDIGGTKIAA-ALIGNGQIIDRRQIPTPRsGTPEALADALASLLADYQ---GQFDRVAVASTGIIRDGVLTALNPKNLGg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 83 LNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKH-LVFAAIiGTGCGSGIAIDGRVHAGGNGIAGEWGH---N 158
Cdd:cd24069 79 LSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGnLVFITV-STGVGGGLVLNGQLLTGPNGLAGHIGHtlaD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 159 PLPwqneeerqyqqeVACYCGKKGCIETFVSGTGFATDYFRMSGKQLKGHEIIALVAQGDAIAEQAMshyeQRFAKSLAH 238
Cdd:cd24069 158 PPG------------PVCGCGRRGCVEAIASGTAIAAAASEILGEPVDAKDVFERARSGDEEAARLI----DRAARALAD 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491331318 239 VIN----LFDPDVVVLGGGMSN----VDRLYTTLPALisPWVFggecQTPVRKALHGDSSGVRGAAWL 298
Cdd:cd24069 222 LIAdlkaTLDLDCVVIGGSVGLaegfLERVEQYLADE--PAIF----RVSLEPARLGQDAGLLGAALL 283
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
3-285 |
2.29e-24 |
|
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: 100.18 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQEL--FRKRVDTPRHDyQNTLQAIATLVADAEQATGQQ-GSVGVGIPGTLSPFTGKV-KNA 78
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLgeFEYRVITLETP-EALIDEIIDCIDRLLKLWKDRvKGIALAIQGLVDSHKGVSlWSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 79 NSVWLNGQMLDKdLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHn 158
Cdd:cd24072 83 GAPWRNIEIKYL-LEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGH- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 159 plpwqneeerqYQQE---VACYCGKKGCIETFVS--------GTGFATDYFRMSGKQLKGHEIIALVAQGDAIAEQAMSH 227
Cdd:cd24072 161 -----------TKVNpdgARCDCGRRGCLETVASnsalkrnaRVTLKLGPVSADPEKLTMEQLIEALEEGEPIATQIFDR 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 491331318 228 YEQRFAKSLAHVINLFDPDVVVL-GGGMSNVDRLYTTLPALISPWVFGGECQTPVRKAL 285
Cdd:cd24072 230 AANAIGRSLANILNLLNPEQVLLyGRGCRAGDLLLPAIRRAIAENPFSQHATQIGFGQL 288
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
3-269 |
4.17e-23 |
|
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: 96.46 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQ--GSVGVGIPgtlspFTGKVKNANS 80
Cdd:cd24077 4 IGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENILEILKSIIQELISQAPKTpyGLVGIGIG-----IHGIVDENEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 81 VW-----LNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAgKHLVfAAIIGTGCGSGIAIDGRVHAGGNGIAGEW 155
Cdd:cd24077 79 IFtpyydLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSEDY-DNLI-SISIHSGIGAGIIINNQLYRGYNGFAGEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 156 GHNPLpwqneeerqYQQEVACYCGKKGCIETFVSGTGFATDYfrmsgKQLKGHE------IIALVAQGDAIAEQAMSHYE 229
Cdd:cd24077 157 GHMII---------VPNGKPCPCGNKGCLEQYASEKALLKEL-----SEKKGLEtltfddLIQLYNEGDPEALELIDQFI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 491331318 230 QRFAKSLAHVINLFDPDVVVLGGgmsnvdRLYTTLPALIS 269
Cdd:cd24077 223 KYLAIGINNIINTFNPEIIIINS------SLINEIPELLE 256
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
60-298 |
3.46e-22 |
|
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: 94.27 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 60 VGVGIPGTLSPFTGKVKNANSV-WLNGQmLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGkHLVFAAI-IGTGCGSG 137
Cdd:cd24071 65 IGIAVSGLVDSKKGIVIRSTILgWENVE-LKKILKEKFKIPVFIDNDVNSFALAELWKGKGKG-YSNFICVtVGAGIGSS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 138 IAIDGRVHAGGNGIAGEWGHNPLpwqneeerqYQQEVACYCGKKGCIETFVSGTGFA-------TDYFRMSGKQLKGHEI 210
Cdd:cd24071 143 LVIDGKLYTGNFGGAGEIGHMTI---------QPDGRKCYCGQKGCLEAYASFEALVneikeltESYPLSLLKELEDFEI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 211 --IALVAQ-GDAIAEQAMSHYEQRFAKSLAHVINLFDPDVVVLGG-GMSNVDRLYTTLPALISPWVFG-GECQTPVRKAL 285
Cdd:cd24071 214 ekVREAAEeGDSVATELFKKAGEYLGIGIKNLINIFNPEAIIIGGeGLEFKDYFLPKIIEIAKENFFGkAGRNVIILVDS 293
|
250
....*....|...
gi 491331318 286 HGDSSGVRGAAWL 298
Cdd:cd24071 294 LGEDAWVLGAALL 306
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
5-298 |
7.49e-22 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 92.67 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 5 IDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTL-QAIATLVADAEqatGQQGSVGVGIPGTLSPftGKVKNANSVWL 83
Cdd:PRK05082 6 IDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALrQALSALVSPLQ---AQADRVAVASTGIIND--GILTALNPHNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 84 NGQM---LDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIiGTGCGSGIAIDGRVHAGGNGIAGEWGH--- 157
Cdd:PRK05082 81 GGLLhfpLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRNMVFITV-STGVGGGIVLNGKLLTGPGGLAGHIGHtla 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 158 NPlpwqneeerqyqQEVACYCGKKGCIETFVSGTGF---ATDYFrmsgKQLKGHEIIALVAQGDAIAEQAMshyeQRFAK 234
Cdd:PRK05082 160 DP------------HGPVCGCGRRGCVEAIASGRAIaaaAQGWL----AGCDAKTIFERAGQGDEQAQALI----NRSAQ 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491331318 235 SLAHVI-NL---FDPDVVVLGGG-------MSNVDRLYTTLPALispwvfggeCQTPVRKALHGDSSGVRGAAWL 298
Cdd:PRK05082 220 AIARLIaDLkatLDCQCVVLGGSvglaegyLELVQAYLAQEPAI---------YHVPLLAAHYRHDAGLLGAALW 285
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
5-257 |
3.96e-21 |
|
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: 91.32 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 5 IDLGGTKIEVIALANDGQELFRKRVDTPrHDYQNTLQAIATLV----ADAEQATGQQGSVGVGIPGTLSPFTGKVKNANS 80
Cdd:cd24060 5 VDLGGTNLRVAIVSMKGEIVKKYTQPNP-KTYEERIDLILQMCveaaSEAVKLNCRILGVGISTGGRVNPREGIVLHSTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 81 V---WlNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGH 157
Cdd:cd24060 84 LiqeW-SSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 158 NPLPWQNEEerqyqqevaCYCGKKGCIETFVSGTGFA--------TDYFRMSGKQLKGHEIIALV-----AQ-GDAIAEQ 223
Cdd:cd24060 163 IVVSLDGPD---------CMCGSHGCVEAYASGMALQreakklhdEDLLLVEGMSVTNDEEVTAKhliqaAKlGNAKAQK 233
|
250 260 270
....*....|....*....|....*....|....
gi 491331318 224 AMSHYEQRFAKSLAHVINLFDPDVVVLGGGMSNV 257
Cdd:cd24060 234 ILRTAGTALGLGIVNILHTLNPSLVILSGVLASH 267
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
3-252 |
1.63e-19 |
|
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: 86.65 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQA----IATLVADAEQATGQQGSVGVGIPGTLSPFTGKVKNA 78
Cdd:cd24075 4 LAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEALLSQlieeIAQFLKSHRRKTQRLIAISITLPGLINPKTGVVHYM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 79 NSVWLNGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGH- 157
Cdd:cd24075 84 PHIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEIGHi 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 158 --NPLPWQneeerqyqqevaCYCGKKGCIETFVSG------------TGFATdyfRMSGKQLKGHEIIALVAQGDAIAEQ 223
Cdd:cd24075 164 qiEPLGER------------CHCGNFGCLETVASNaaieqrvkkllkQGYAS---QLTLQDCTIKDICQAALNGDQLAQD 228
|
250 260
....*....|....*....|....*....
gi 491331318 224 AMSHYEQRFAKSLAHVINLFDPDVVVLGG 252
Cdd:cd24075 229 VIKRAGRYLGKVIAILINLLNPQKIIIAG 257
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
4-299 |
9.00e-19 |
|
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: 83.39 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 4 GIDLGGTKIEVIALANDGQELF--RKRVDTPRHdyqNTLQAIATLVADAEQATGQQGSVGVGIPGTLSpfTGKVKNANSV 81
Cdd:cd24058 3 GIDIGGSGIKGAIVDTDTGELLseRIRIPTPQP---ATPEAVADVVAELVAHFPWFGPVGVGFPGVVR--RGVVRTAANL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 82 ---WLnGQMLDKDLSELLSRPVRLANDANCLAVSEATDGAGAGKH-LVFAAIIGTGCGSGIAIDGRV--HAggngiagEW 155
Cdd:cd24058 78 dksWI-GFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKgVVLVLTLGTGIGSALFVDGHLvpNT-------EL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 156 GHNPLpwqneeerqyqqevacycgKKGCIETFVSgtgfatdyfrmsgkqlkgheiiALVAQGDAIAEQAmshYEQRFAKS 235
Cdd:cd24058 150 GHLEI-------------------RGKDAEERAS----------------------LGVRAREDLGWKR---WAKRVNKY 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491331318 236 LAHVINLFDPDVVVLGGGMSnvdrlyttlpALISPWVFGGECQTPVRKALHGDSSGVRGAAWLW 299
Cdd:cd24058 186 LQYLERLFNPDLFIIGGGNS----------KKADKFLPLLDVKTPVVPAVLRNDAGIVGAALLA 239
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
2-253 |
5.40e-15 |
|
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: 73.80 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 2 RIGIDLGGTKIEvIALAND----GQELFRKRVDTprHDYQNTLQAIATLVADAEQATGQQGSVGVgiPGTLSPftGKVKN 77
Cdd:cd24008 1 ILVGDIGGTNAR-LALADAgdgsGDLLFVRKYPS--ADFASLEDALAAFLAELGAPRPKAACIAV--AGPVDG--GRVRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 78 ANSVW-LNGQmldkDLSELLS-RPVRLAND--ANCLAVSEATD--------GAGAGKHLVFAAI-IGTGCGSGIAI---D 141
Cdd:cd24008 74 TNLDWsIDAA----ELRKALGiGRVRLLNDfeAAAYGLPALGPedllvlygGGGPLPGGPRAVLgPGTGLGVALLVpdgD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 142 GRVHAggngIAGEWGHNPLPWQNEEERQYQQEVACYCGKKGCIETFVSGTG------FATDYFRMSGKQLKGHEIIALVA 215
Cdd:cd24008 150 GGYVV----LPSEGGHADFAPVTEEEAELLEFLRKRFGRSVSYEDVLSGPGleniyeFLAKLDGAEPPDLTAEEIAEAAL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491331318 216 QGDAIAEQAMSHYEQ---RFAKSLAhvINLFDPDVVVLGGG 253
Cdd:cd24008 226 AGDPLAREALDLFARilgRFAGNLA--LSFLATGGVYLAGG 264
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
21-260 |
8.07e-15 |
|
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: 73.50 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 21 GQELFRKRVDTPRHDYQNTLQAIATLVAD--------AEQATgqqgSVGVGIPGTLSPFTGKVKNANSVWLNGQMLDKDL 92
Cdd:cd24074 23 GRLLAEERYPLPAKDNDPFLDRLLESISEffsrhqkkLERLT----AIAITLPGIIDPESGIVHRLPFYDIKNLPLGEAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 93 SELLSRPVRLANDANCLAVSEATDGAGAGKHLVFAAIIGTGCGSGIAIDGRVHAGGNGIAGEWGHNPLPWQNEEerqyqq 172
Cdd:cd24074 99 EQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKR------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 173 evaCYCGKKGCIETFVSgTGFATDYFRMSGKQLKG----HEII------ALVAQGDAIAEQAMSHYEQRFAKSLAHVINL 242
Cdd:cd24074 173 ---CYCGNHGCLETVAS-IPAILEQANQLLEQSPDsmlhGQPIsieslcQAALAGDPLAQDIIIQVGRHLGRILAILVNL 248
|
250
....*....|....*...
gi 491331318 243 FDPDVVVLGGGMSNVDRL 260
Cdd:cd24074 249 FNPEKILIGSPLNNAAEI 266
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
4-298 |
2.39e-11 |
|
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: 62.95 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 4 GIDLGGTKIeVIALAN-DGQELFRKRVDTprHDYQNTLQAIATLVADAEQATgqqgsVGVGI-------PGTLSPFTGKV 75
Cdd:cd24067 3 GIEAGGTKF-VCAVGTgDGNIIERTEFPT--TTPEETLQAVIDFFREQEEPI-----DAIGIasfgpidLNPTSPTYGYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 76 KNANSV-WLNGQMLDKdLSELLSRPVRLANDANCLAVSEATDGAGAGKHlVFAAI-IGTGCGSGIAIDGRVHAGgngiAG 153
Cdd:cd24067 75 TTTPKPgWRNFDILGA-LKRAFPVPVGFDTDVNAAALAEYRWGAAKGLD-SLAYItVGTGIGVGLVVNGKPVHG----LL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 154 --EWGHNPLPwQNEEERQYQqevacycGK----KGCIETFVSGTGFAtDYFRMSGKQLK-GHEIIALVAqgdaiaeqams 226
Cdd:cd24067 149 hpEMGHIRVP-RHPDDDGFP-------GVcpfhGDCLEGLASGPAIA-ARWGIPAEELPdDHPAWDLEA----------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 227 HYeqrFAKSLAHVINLFDPDVVVLGGGMSN----VDRLYTTLPALISPWVFGGECQTPVRK----ALHGDSSGVRGAAWL 298
Cdd:cd24067 209 YY---LAQACANLTLTLSPERIVLGGGVMQrpglFPRIREKFRKLLNGYLEVPRLLPDIDEyivpPALGNDAGILGALAL 285
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
3-156 |
4.93e-07 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 50.27 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGS------VGVGIPGTLSPftgkvk 76
Cdd:COG2971 4 LGVDGGGTKTRAVLVDADGEVLGRGRAGGANPQSVGLEEALASLREALEEALAAAGDpadieaVGFGLAGAGTP------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 77 nansvwLNGQMLDKDLSEL-LSRPVRLANDANCLAVSEATDGAGAgkhlvfAAIIGTG-CGSGIAIDGRVH-AGGNG-IA 152
Cdd:COG2971 78 ------EDAEALEAALRELfPFARVVVVNDALAALAGALGGEDGI------VVIAGTGsIAAGRDGDGRTArVGGWGyLL 145
|
....
gi 491331318 153 GEWG 156
Cdd:COG2971 146 GDEG 149
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
3-157 |
1.31e-06 |
|
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: 48.84 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDGQELFRKRVDTPRHDYQNTLQAIATLVADAEQATGQQGS------VGVGIPGTLSP-FTGKV 75
Cdd:cd24007 2 LGVDGGGTKTRAVLADEDGKILGRGKGGPSNPASVGIEEAKENLKEAVREALSQAGSlgeidaICLGLAGIDSEeDRERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 76 KNAnsvwlngqmldkdLSELL-SRPVRLANDANCLAVSEATDGAGAgkhlvfAAIIGTGCGS-GIAIDGRVH-AGGngia 152
Cdd:cd24007 82 RSA-------------LKELFlSGRIIIVNDAEIALAAALGGGPGI------VVIAGTGSVAyGRNGDGEEArVGG---- 138
|
....*
gi 491331318 153 geWGH 157
Cdd:cd24007 139 --WGH 141
|
|
| ASKHA_NBD_DdNAGK-like |
cd24081 |
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase ... |
3-156 |
2.07e-03 |
|
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; The family includes a group of uncharacterized proteins similar to Dictyostelium discoideum N-acetyl-D-glucosamine kinase (NAGK). NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, into GlcNAc 6-phosphate. It also has ManNAc kinase activity.
Pssm-ID: 466931 [Multi-domain] Cd Length: 311 Bit Score: 39.22 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 3 IGIDLGGTKIEVIALANDG---QELFRKRVDTPRHDY---------QNTLQAIATLVADAEQATGQQGSVGVGIPGTLSP 70
Cdd:cd24081 2 LGIDGGGTKTTCVAVDAATlgdNLLVLGRAVAGSSNYnsvgeeaarRAIEEAIAGALKQAGVPRSAVRAVCLGISGVDRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491331318 71 F-TGKVKNansvWLngqmldkdlSELL--SRPVRLANDAnCLAVSEATdgagAGKHLVFAAIIGTGCGS-GIAIDGR-VH 145
Cdd:cd24081 82 AdAERVRS----WL---------RELFpeNVKVFVFNDA-VAALASGT----AGKLHGCVLIAGTGTIAyGFNEDGKrAR 143
|
170
....*....|..
gi 491331318 146 AGGNG-IAGEWG 156
Cdd:cd24081 144 AGGWGpLLGDRG 155
|
|
| |
