|
Name |
Accession |
Description |
Interval |
E-value |
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
13-344 |
7.71e-148 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 420.59 E-value: 7.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 13 LVITNGMFIIDDIERSKYnIHYKNVPGGGGTFAILGACIISsGNVTSKGLKWIVDRGSDFPKEVIREIDSWGTDVRFRDD 92
Cdd:cd01943 1 DFTTLGMFIIDEIEYPDS-EPVTNVLGGAGTYAILGARLFL-PPPLSRSISWIVDKGSDFPKSVEDELESWGTGMVFRRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 93 FSRLTTKGLNYYEGsDDLRKFKFLTPKKQINVDDWISTFGQKIIDEMHAFHLLCS-GSRCLDIINDLLRVKSSKGTKPIV 171
Cdd:cd01943 79 PGRLTTRGLNIYDG-NDRRFFKYLTPKKRIDVSDDLNSTPLIRSSCIHLICSPERcASIVDDIINLFKLLKGNSPTRPKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 172 IWEPFPDLCDFDHQNDIKsvmQRNDVTVILSPNAEESSRLFGLSSKEPTSLEECLA---LAHRFDDFMDENNMCILRCGA 248
Cdd:cd01943 158 VWEPLPDSCDPENLEDLL---QALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEAvlqALLFSGILQDPGGGVVLRCGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 249 LGSISVSekfKNGRTYDHFPAYHFKtQSKVLDPTGGGNSFLGGFAVSYALTKSLDIASICGNIAAGAIIEQFGIPRYD-- 326
Cdd:cd01943 235 LGCYVGS---ADSGPELWLPAYHTK-STKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGLPRLTkv 310
|
330
....*....|....*...
gi 6319865 327 PIAKTWNGITFLDRLKFY 344
Cdd:cd01943 311 EGEELWNGETVEERLKEY 328
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
69-321 |
2.26e-09 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 57.97 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 69 GSD-FPKEVIREIDSWGTDVRF--RDD-------FSRLTTKG---LNYYEGSDDlrkfkfltpkkQINVDDwistFGQKI 135
Cdd:COG0524 60 GDDpFGDFLLAELRAEGVDTSGvrRDPgaptglaFILVDPDGertIVFYRGANA-----------ELTPED----LDEAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 136 IDEMHAFHL---LCSGSRCLDIINDLLRVKSSKGTKpiVIWEPFPDLCDFD-HQNDIKSVMQRNDvtvILSPNAEESSRL 211
Cdd:COG0524 125 LAGADILHLggiTLASEPPREALLAALEAARAAGVP--VSLDPNYRPALWEpARELLRELLALVD---ILFPNEEEAELL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 212 FGLsskepTSLEECLALAHRFDDfmdenNMCILRCGALGSISVSekfkNGRTYdHFPAYHFKtqskVLDPTGGGNSFLGG 291
Cdd:COG0524 200 TGE-----TDPEEAAAALLARGV-----KLVVVTLGAEGALLYT----GGEVV-HVPAFPVE----VVDTTGAGDAFAAG 260
|
250 260 270
....*....|....*....|....*....|
gi 6319865 292 FAVSYALTKSLDIASICGNIAAGAIIEQFG 321
Cdd:COG0524 261 FLAGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
144-321 |
3.40e-09 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 57.35 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 144 LLCSGSRClDIINDLLRVKSSKGTKPIVIWEPFPDLCDfdhqnDIKSVMQRNDvtvILSPNAEESSRLFGLSSKEPtslE 223
Cdd:pfam00294 136 SLPLGLPE-ATLEELIEAAKNGGTFDPNLLDPLGAARE-----ALLELLPLAD---LLKPNEEELEALTGAKLDDI---E 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 224 ECLALAHRFDDFMDENnmCILRCGALGSISVSekfkNGRTYdHFPAYhFKTqsKVLDPTGGGNSFLGGFAVSYALTKSLD 303
Cdd:pfam00294 204 EALAALHKLLAKGIKT--VIVTLGADGALVVE----GDGEV-HVPAV-PKV--KVVDTTGAGDSFVGGFLAGLLAGKSLE 273
|
170
....*....|....*...
gi 6319865 304 IASICGNIAAGAIIEQFG 321
Cdd:pfam00294 274 EALRFANAAAALVVQKSG 291
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
274-332 |
3.43e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 48.48 E-value: 3.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319865 274 TQSKVLDPTGGGNSFLGGFAVSYALTKSLDIASICGNIAAGAIIEQFG--IPRYdPIAKTW 332
Cdd:PTZ00247 286 DQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGctYPEK-PPFLPW 345
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
13-344 |
7.71e-148 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 420.59 E-value: 7.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 13 LVITNGMFIIDDIERSKYnIHYKNVPGGGGTFAILGACIISsGNVTSKGLKWIVDRGSDFPKEVIREIDSWGTDVRFRDD 92
Cdd:cd01943 1 DFTTLGMFIIDEIEYPDS-EPVTNVLGGAGTYAILGARLFL-PPPLSRSISWIVDKGSDFPKSVEDELESWGTGMVFRRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 93 FSRLTTKGLNYYEGsDDLRKFKFLTPKKQINVDDWISTFGQKIIDEMHAFHLLCS-GSRCLDIINDLLRVKSSKGTKPIV 171
Cdd:cd01943 79 PGRLTTRGLNIYDG-NDRRFFKYLTPKKRIDVSDDLNSTPLIRSSCIHLICSPERcASIVDDIINLFKLLKGNSPTRPKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 172 IWEPFPDLCDFDHQNDIKsvmQRNDVTVILSPNAEESSRLFGLSSKEPTSLEECLA---LAHRFDDFMDENNMCILRCGA 248
Cdd:cd01943 158 VWEPLPDSCDPENLEDLL---QALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEAvlqALLFSGILQDPGGGVVLRCGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 249 LGSISVSekfKNGRTYDHFPAYHFKtQSKVLDPTGGGNSFLGGFAVSYALTKSLDIASICGNIAAGAIIEQFGIPRYD-- 326
Cdd:cd01943 235 LGCYVGS---ADSGPELWLPAYHTK-STKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGLPRLTkv 310
|
330
....*....|....*...
gi 6319865 327 PIAKTWNGITFLDRLKFY 344
Cdd:cd01943 311 EGEELWNGETVEERLKEY 328
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
136-297 |
1.70e-22 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 93.70 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 136 IDEMHAFHLLCSGSRCLDIINDLLRVKsskgtkPIVIWEPFPDLCDFDHQNdiksVMQRNDVTVILSPNAEESSRLFGLS 215
Cdd:cd00287 58 ADAVVISGLSPAPEAVLDALEEARRRG------VPVVLDPGPRAVRLDGEE----LEKLLPGVDILTPNEEEAEALTGRR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 216 SKEPTSLEECLALAHrfddfMDENNMCILRCGALGSISVSEkfknGRTYDHFPAYHfktqSKVLDPTGGGNSFLGGFAVS 295
Cdd:cd00287 128 DLEVKEAAEAAALLL-----SKGPKVVIVTLGEKGAIVATR----GGTEVHVPAFP----VKVVDTTGAGDAFLAALAAG 194
|
..
gi 6319865 296 YA 297
Cdd:cd00287 195 LA 196
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
69-321 |
2.26e-09 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 57.97 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 69 GSD-FPKEVIREIDSWGTDVRF--RDD-------FSRLTTKG---LNYYEGSDDlrkfkfltpkkQINVDDwistFGQKI 135
Cdd:COG0524 60 GDDpFGDFLLAELRAEGVDTSGvrRDPgaptglaFILVDPDGertIVFYRGANA-----------ELTPED----LDEAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 136 IDEMHAFHL---LCSGSRCLDIINDLLRVKSSKGTKpiVIWEPFPDLCDFD-HQNDIKSVMQRNDvtvILSPNAEESSRL 211
Cdd:COG0524 125 LAGADILHLggiTLASEPPREALLAALEAARAAGVP--VSLDPNYRPALWEpARELLRELLALVD---ILFPNEEEAELL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 212 FGLsskepTSLEECLALAHRFDDfmdenNMCILRCGALGSISVSekfkNGRTYdHFPAYHFKtqskVLDPTGGGNSFLGG 291
Cdd:COG0524 200 TGE-----TDPEEAAAALLARGV-----KLVVVTLGAEGALLYT----GGEVV-HVPAFPVE----VVDTTGAGDAFAAG 260
|
250 260 270
....*....|....*....|....*....|
gi 6319865 292 FAVSYALTKSLDIASICGNIAAGAIIEQFG 321
Cdd:COG0524 261 FLAGLLEGLDLEEALRFANAAAALVVTRPG 290
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
144-321 |
3.40e-09 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 57.35 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 144 LLCSGSRClDIINDLLRVKSSKGTKPIVIWEPFPDLCDfdhqnDIKSVMQRNDvtvILSPNAEESSRLFGLSSKEPtslE 223
Cdd:pfam00294 136 SLPLGLPE-ATLEELIEAAKNGGTFDPNLLDPLGAARE-----ALLELLPLAD---LLKPNEEELEALTGAKLDDI---E 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 224 ECLALAHRFDDFMDENnmCILRCGALGSISVSekfkNGRTYdHFPAYhFKTqsKVLDPTGGGNSFLGGFAVSYALTKSLD 303
Cdd:pfam00294 204 EALAALHKLLAKGIKT--VIVTLGADGALVVE----GDGEV-HVPAV-PKV--KVVDTTGAGDSFVGGFLAGLLAGKSLE 273
|
170
....*....|....*...
gi 6319865 304 IASICGNIAAGAIIEQFG 321
Cdd:pfam00294 274 EALRFANAAAALVVQKSG 291
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
71-316 |
6.86e-07 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 50.27 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 71 DFPKEVIREIDSWGTDVRF-RDDFSRLTtkGLNYYEgSDDLRKFKFLT-----PKKQINVDDwistFGQKIIDEMHAFHL 144
Cdd:cd01166 58 PFGRFILAELRREGVDTSHvRVDPGRPT--GLYFLE-IGAGGERRVLYyragsAASRLTPED----LDEAALAGADHLHL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 145 ----LCSGSRCLDIINDLLRVKSSKGTKpiVIWEP--FPDLCDFDH-QNDIKSVMQRNDvtvILSPNAEESSRLFGLSSk 217
Cdd:cd01166 131 sgitLALSESAREALLEALEAAKARGVT--VSFDLnyRPKLWSAEEaREALEELLPYVD---IVLPSEEEAEALLGDED- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 218 EPTSLEECLALAHRFDdfmdennMCILRCGALGSIsvsekFKNGRTYDHFPAYHFKtqskVLDPTGGGNSFLGGFAVSYA 297
Cdd:cd01166 205 PTDAAERALALALGVK-------AVVVKLGAEGAL-----VYTGGGRVFVPAYPVE----VVDTTGAGDAFAAGFLAGLL 268
|
250
....*....|....*....
gi 6319865 298 LTKSLDIASICGNiAAGAI 316
Cdd:cd01166 269 EGWDLEEALRFAN-AAAAL 286
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
200-321 |
7.47e-07 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 50.25 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 200 ILSPNAEESSRLFGLSSKEPTSLEECLALAHRFDDFmdeNNMCILRcGALGSISVSEkfknGRTYDHFPAYHfktqSKVL 279
Cdd:cd01172 184 LLTPNEKEAREALGDEINDDDELEAAGEKLLELLNL---EALLVTL-GEEGMTLFER----DGEVQHIPALA----KEVY 251
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6319865 280 DPTGGGNSFLGGFAVSYALTKSLDIASICGNIAAGAIIEQFG 321
Cdd:cd01172 252 DVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVG 293
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
177-326 |
1.37e-06 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 49.53 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 177 PDLCDFdHQNDIKSVMQRNDvtvILSPNAEESSRLFGLSSKEptSLEECLALAHrfddfmdennmciLRC-------GAL 249
Cdd:cd01168 184 PFIVQR-FKEALLELLPYVD---ILFGNEEEAEALAEAETTD--DLEAALKLLA-------------LRCrivvitqGAK 244
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319865 250 GSISVSekfkNGRTYdHFPAYhfkTQSKVLDPTGGGNSFLGGFAvsYALT--KSLDIASICGNIAAGAIIEQFGiPRYD 326
Cdd:cd01168 245 GAVVVE----GGEVY-PVPAI---PVEKIVDTNGAGDAFAGGFL--YGLVqgEPLEECIRLGSYAAAEVIQQLG-PRLP 312
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
274-332 |
3.43e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 48.48 E-value: 3.43e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6319865 274 TQSKVLDPTGGGNSFLGGFAVSYALTKSLDIASICGNIAAGAIIEQFG--IPRYdPIAKTW 332
Cdd:PTZ00247 286 DQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGctYPEK-PPFLPW 345
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
279-354 |
7.34e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 47.11 E-value: 7.34e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319865 279 LDPTGGGNSFLGGFAVsyALTKSLDI--ASICGNIAAGAIIEQFGIPRYDpiaktwngITFLDRLKFYLSQSGLQYNI 354
Cdd:PLN02630 234 VDPTGAGDSFLGGFVA--GLVQGLAVpdAALLGNYFGSLAVEQVGIPKFD--------LRQLQRVKDEVQRRKMQCEL 301
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
200-321 |
2.32e-05 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 45.62 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 200 ILSPNAEESSRLFGLsskePTSLEECLALAHRFDDFMDENNMCI-LrcGALGSIsvsekFKNGRTYDHFPAYhfktQSKV 278
Cdd:cd01174 178 ILVPNETEAALLTGI----EVTDEEDAEKAARLLLAKGVKNVIVtL--GAKGAL-----LASGGEVEHVPAF----KVKA 242
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 6319865 279 LDPTGGGNSFLGGFAVSYALTKSLDIASICGNIAAGAIIEQFG 321
Cdd:cd01174 243 VDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPG 285
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
192-321 |
2.36e-05 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 45.38 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319865 192 MQRNDVTVILSPnaeeSSRLFGLSSKEptsLEECLALAHRFddFMDENNMCILR--------------------CGALGS 251
Cdd:cd01942 145 LAAGGITVSFDP----GQELPRLSGEE---LEEILERADIL--FVNDYEAELLKertglseaelasgvrvvvvtLGPKGA 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319865 252 ISvsekFKNGRTYdHFPAYHfktQSKVLDPTGGGNSFLGGFAvsYALTKSLDIASIC--GNIAAGAIIEQFG 321
Cdd:cd01942 216 IV----FEDGEEV-EVPAVP---AVKVVDTTGAGDAFRAGFL--YGLLRGYDLEESLrlGNLAASLKVERRG 277
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
268-324 |
9.06e-05 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 43.61 E-value: 9.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319865 268 PAYHFKTqskVLDPTGGGNSFLGGFAVSYALTKSLDIAS-----ICGNIAAGAIIEQFGIPR 324
Cdd:cd01946 219 PAYPLES---VFDPTGAGDTFAGGFIGYLASQKDTSEANmrraiIYGSAMASFCVEDFGTKR 277
|
|
| |
