|
Name |
Accession |
Description |
Interval |
E-value |
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
9-341 |
4.96e-152 |
|
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: 430.99 E-value: 4.96e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 9 EFVTTGMFIIDEIEFDGGKKIKDIIGGAGSFALIGARLWTSEPESQQLGMIVDKGSDFPQVILDELNDLHTGIVYRETPW 88
Cdd:cd01943 1 DFTTLGMFIIDEIEYPDSEPVTNVLGGAGTYAILGARLFLPPPLSRSISWIVDKGSDFPKSVEDELESWGTGMVFRRDPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 89 RKTTYGYNRLRDNGFRLFEYLTPKKPIRA-PDLLETGLIYAKTIHIITNPKTFVSVCEELAKY-----GNLKNRPKIVWE 162
Cdd:cd01943 81 RLTTRGLNIYDGNDRRFFKYLTPKKRIDVsDDLNSTPLIRSSCIHLICSPERCASIVDDIINLfkllkGNSPTRPKIVWE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 163 PTPESCLPENWHILQKALKYCDIFSPNEVDSANLLGIDISESKSRAKEFVS--AFQEFQIGHDSQGWVVLRNGSDGCLIG 240
Cdd:cd01943 161 PLPDSCDPENLEDLLQALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEAVlqALLFSGILQDPGGGVVLRCGKLGCYVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 241 ACTSstnatsdavvpvREILHLPSVQMKNGSVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHGLPAHT 320
Cdd:cd01943 241 SADS------------GPELWLPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGLPRLT 308
|
330 340
....*....|....*....|.
gi 1351604 321 KnSEGIDLWNGESVFQRLKEY 341
Cdd:cd01943 309 K-VEGEELWNGETVEERLKEY 328
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
8-315 |
1.05e-17 |
|
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: 82.24 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 8 VEFVTTGMFIIDEIEFDGGKKIKDIIGGAGSFALIGARLWTSEPesqqlGMI--VdkGSD-FPQVILDELNDLHTGIVY- 83
Cdd:COG0524 10 VDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARV-----ALVgaV--GDDpFGDFLLAELRAEGVDTSGv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 84 RETPWRKTTYGYNRLRDNGFRLFE-YLTPKKPIRAPDLLETGLIYAKTIHI-------ITNPKTFVSVCEELAKYGnlkn 155
Cdd:COG0524 83 RRDPGAPTGLAFILVDPDGERTIVfYRGANAELTPEDLDEALLAGADILHLggitlasEPPREALLAALEAARAAG---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 156 rPKIVWEPTPESCLPENWH-ILQKALKYCDIFSPNEVDSANLLGIDisesksRAKEFVSAFQEFQIGHdsqgwVVLRNGS 234
Cdd:COG0524 159 -VPVSLDPNYRPALWEPAReLLRELLALVDILFPNEEEAELLTGET------DPEEAAAALLARGVKL-----VVVTLGA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 235 DGCLIgactsstnATSDavvpvrEILHLPSVQMKngsVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQH 314
Cdd:COG0524 227 EGALL--------YTGG------EVVHVPAFPVE---VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRP 289
|
.
gi 1351604 315 G 315
Cdd:COG0524 290 G 290
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
160-315 |
3.51e-14 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 72.46 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 160 VWEPTPESCLPEnWHILQKALKYCDIFSPNEVDSANLLGIDISESKSRAKefvsAFQEFQIGHDSQgwVVLRNGSDGCLI 239
Cdd:PTZ00292 177 VFNPAPAPKLAE-VEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFK----ASKELQQLGVEN--VIITLGANGCLI 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351604 240 gaCTSSTNATsdavvpvreilHLPSVQMKngsVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHG 315
Cdd:PTZ00292 250 --VEKENEPV-----------HVPGKRVK---AVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
167-315 |
2.28e-12 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 66.60 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 167 SCLPENWHILQKALKYCDIFSPNE---VDSANLLGIDISESKSRAKEFVSAFQEfqighdsqgWVVLRNGSDGCLIgact 243
Cdd:pfam00294 165 DPLGAAREALLELLPLADLLKPNEeelEALTGAKLDDIEEALAALHKLLAKGIK---------TVIVTLGADGALV---- 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351604 244 sstnATSDAVVPVreilhlPSVQMKNgsVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHG 315
Cdd:pfam00294 232 ----VEGDGEVHV------PAVPKVK--VVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
9-341 |
4.96e-152 |
|
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: 430.99 E-value: 4.96e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 9 EFVTTGMFIIDEIEFDGGKKIKDIIGGAGSFALIGARLWTSEPESQQLGMIVDKGSDFPQVILDELNDLHTGIVYRETPW 88
Cdd:cd01943 1 DFTTLGMFIIDEIEYPDSEPVTNVLGGAGTYAILGARLFLPPPLSRSISWIVDKGSDFPKSVEDELESWGTGMVFRRDPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 89 RKTTYGYNRLRDNGFRLFEYLTPKKPIRA-PDLLETGLIYAKTIHIITNPKTFVSVCEELAKY-----GNLKNRPKIVWE 162
Cdd:cd01943 81 RLTTRGLNIYDGNDRRFFKYLTPKKRIDVsDDLNSTPLIRSSCIHLICSPERCASIVDDIINLfkllkGNSPTRPKIVWE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 163 PTPESCLPENWHILQKALKYCDIFSPNEVDSANLLGIDISESKSRAKEFVS--AFQEFQIGHDSQGWVVLRNGSDGCLIG 240
Cdd:cd01943 161 PLPDSCDPENLEDLLQALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEAVlqALLFSGILQDPGGGVVLRCGKLGCYVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 241 ACTSstnatsdavvpvREILHLPSVQMKNGSVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHGLPAHT 320
Cdd:cd01943 241 SADS------------GPELWLPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGLPRLT 308
|
330 340
....*....|....*....|.
gi 1351604 321 KnSEGIDLWNGESVFQRLKEY 341
Cdd:cd01943 309 K-VEGEELWNGETVEERLKEY 328
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
8-315 |
1.05e-17 |
|
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: 82.24 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 8 VEFVTTGMFIIDEIEFDGGKKIKDIIGGAGSFALIGARLWTSEPesqqlGMI--VdkGSD-FPQVILDELNDLHTGIVY- 83
Cdd:COG0524 10 VDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARV-----ALVgaV--GDDpFGDFLLAELRAEGVDTSGv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 84 RETPWRKTTYGYNRLRDNGFRLFE-YLTPKKPIRAPDLLETGLIYAKTIHI-------ITNPKTFVSVCEELAKYGnlkn 155
Cdd:COG0524 83 RRDPGAPTGLAFILVDPDGERTIVfYRGANAELTPEDLDEALLAGADILHLggitlasEPPREALLAALEAARAAG---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 156 rPKIVWEPTPESCLPENWH-ILQKALKYCDIFSPNEVDSANLLGIDisesksRAKEFVSAFQEFQIGHdsqgwVVLRNGS 234
Cdd:COG0524 159 -VPVSLDPNYRPALWEPAReLLRELLALVDILFPNEEEAELLTGET------DPEEAAAALLARGVKL-----VVVTLGA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 235 DGCLIgactsstnATSDavvpvrEILHLPSVQMKngsVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQH 314
Cdd:COG0524 227 EGALL--------YTGG------EVVHVPAFPVE---VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRP 289
|
.
gi 1351604 315 G 315
Cdd:COG0524 290 G 290
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
160-315 |
3.51e-14 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 72.46 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 160 VWEPTPESCLPEnWHILQKALKYCDIFSPNEVDSANLLGIDISESKSRAKefvsAFQEFQIGHDSQgwVVLRNGSDGCLI 239
Cdd:PTZ00292 177 VFNPAPAPKLAE-VEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFK----ASKELQQLGVEN--VIITLGANGCLI 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351604 240 gaCTSSTNATsdavvpvreilHLPSVQMKngsVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHG 315
Cdd:PTZ00292 250 --VEKENEPV-----------HVPGKRVK---AVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
121-287 |
1.89e-13 |
|
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: 68.28 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 121 LETGLIYAKTIHI-ITNPKTFVsvCEELAKYGNLKNRPkIVWEPTPESCLPENwHILQKALKYCDIFSPNEVDSANLLGI 199
Cdd:cd00287 51 VSVTLVGADAVVIsGLSPAPEA--VLDALEEARRRGVP-VVLDPGPRAVRLDG-EELEKLLPGVDILTPNEEEAEALTGR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 200 DISESKSRAKefvSAFQEFQIGhdsQGWVVLRNGSDGCLIgactsstnATSDavvpvREILHLPSVqmkNGSVLDTTGAG 279
Cdd:cd00287 127 RDLEVKEAAE---AAALLLSKG---PKVVIVTLGEKGAIV--------ATRG-----GTEVHVPAF---PVKVVDTTGAG 184
|
....*...
gi 1351604 280 NAFCGAAI 287
Cdd:cd00287 185 DAFLAALA 192
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
175-315 |
3.38e-13 |
|
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: 69.12 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 175 ILQKALKYCDIFSPNEVDSANLLGIDISESKSRAKefvsAFQEFQighdSQG--WVVLRNGSDGCLIgactsstnATSDA 252
Cdd:cd01174 168 LPAELLALVDILVPNETEAALLTGIEVTDEEDAEK----AARLLL----AKGvkNVIVTLGAKGALL--------ASGGE 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351604 253 VVpvreilHLPSVQMKngsVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHG 315
Cdd:cd01174 232 VE------HVPAFKVK---AVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPG 285
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
167-315 |
2.28e-12 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 66.60 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 167 SCLPENWHILQKALKYCDIFSPNE---VDSANLLGIDISESKSRAKEFVSAFQEfqighdsqgWVVLRNGSDGCLIgact 243
Cdd:pfam00294 165 DPLGAAREALLELLPLADLLKPNEeelEALTGAKLDDIEEALAALHKLLAKGIK---------TVIVTLGADGALV---- 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351604 244 sstnATSDAVVPVreilhlPSVQMKNgsVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHG 315
Cdd:pfam00294 232 ----VEGDGEVHV------PAVPKVK--VVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
175-315 |
5.01e-12 |
|
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: 65.68 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 175 ILQKALKYCDIFSPNEVDSANLLGI-DISESKSRAKEFvsafqEFQIGHdsqgwVVLRNGSDGCLIgactssTNATSDAV 253
Cdd:cd01166 178 ALEELLPYVDIVLPSEEEAEALLGDeDPTDAAERALAL-----ALGVKA-----VVVKLGAEGALV------YTGGGRVF 241
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351604 254 VPVREIlhlpsvqmkngSVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHG 315
Cdd:cd01166 242 VPAYPV-----------EVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
9-311 |
2.98e-09 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 57.03 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 9 EFVTTGMFIIDEIEFDGGKKIKdiIGGAGSFALIGARLWTSEPesqqlgMIVDK-GSDFPQVILDELNDLHTGIVYRETP 87
Cdd:cd01937 1 KIVIIGHVTIDEIVTNGSGVVK--PGGPATYASLTLSRLGLTV------KLVTKvGRDYPDKWSDLFDNGIEVISLLSTE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 88 wrkTTYGYNRLRDNGFRLFEYLTPKKPIrapdLLETGLIYAKTIHIITNPktfvsVCEELAkygnlknrPKIVWEPTPES 167
Cdd:cd01937 73 ---TTTFELNYTNEGRTRTLLAKCAAIP----DTESPLSTITAEIVILGP-----VPEEIS--------PSLFRKFAFIS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 168 CLPENW--------HILQKALKYCDIFSPNEVDSANLLgiDISESKSRAKEFvsafqefqiGHDSqgwVVLRNGSDGCLI 239
Cdd:cd01937 133 LDAQGFlrranqekLIKCVILKLHDVLKLSRVEAEVIS--TPTELARLIKET---------GVKE---IIVTDGEEGGYI 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351604 240 gactSSTNAtsdavvpvreILHLPSvqmKNGSVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVI 311
Cdd:cd01937 199 ----FDGNG----------KYTIPA---SKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
176-315 |
5.08e-09 |
|
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: 56.85 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 176 LQKALKYCDIFSPNEVDSANLLGIDISESKSRAKEFVSAFQEfqighdsqgWVVLRNGSDGCLIgactsstnATSDAVVP 255
Cdd:cd01168 194 LLELLPYVDILFGNEEEAEALAEAETTDDLEAALKLLALRCR---------IVVITQGAKGAVV--------VEGGEVYP 256
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351604 256 VREIlhlpsvqmKNGSVLDTTGAGNAFCGA---AILEyyrtGNIIEACAK-ATVAASFVIQQHG 315
Cdd:cd01168 257 VPAI--------PVEKIVDTNGAGDAFAGGflyGLVQ----GEPLEECIRlGSYAAAEVIQQLG 308
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
145-315 |
2.68e-06 |
|
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: 48.46 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 145 EELAKYGNlknrpKIVWEPTPEScLPENWHILQKALKYCDIFSPNEVDSANLLGIDISESKSRAKeFVSAfqefqighds 224
Cdd:cd01942 143 RELAAGGI-----TVSFDPGQEL-PRLSGEELEEILERADILFVNDYEAELLKERTGLSEAELAS-GVRV---------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 225 qgwVVLRNGSDGCLIgacTSSTNATSDAVVPVREilhlpsvqmkngsVLDTTGAGNAFCGAAILEYYRTGNIIEACAKAT 304
Cdd:cd01942 206 ---VVVTLGPKGAIV---FEDGEEVEVPAVPAVK-------------VVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGN 266
|
170
....*....|.
gi 1351604 305 VAASFVIQQHG 315
Cdd:cd01942 267 LAASLKVERRG 277
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
176-315 |
1.92e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 46.17 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 176 LQKALKYCDIFSPNEVD-----SANLLGI-DISESKSRAkefvSAFQEFQIGHDSQgwVVLRNGSDGCLIGACTSSTNat 249
Cdd:PTZ00247 208 LLQVLPYVDILFGNEEEaktfaKAMKWDTeDLKEIAARI----AMLPKYSGTRPRL--VVFTQGPEPTLIATKDGVTS-- 279
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351604 250 sdavVPVReilhlpsvQMKNGSVLDTTGAGNAFCGAAILEYYRTGNIIEACAKATVAASFVIQQHG 315
Cdd:PTZ00247 280 ----VPVP--------PLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNG 333
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
65-309 |
4.84e-05 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 44.55 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 65 DFPQVILDELNDLH---TGIVYRetPWRKTTYGYNRLRDNGFRLFEYLtpkKPIRAPDLLETGLIY-----AKTIHI--- 133
Cdd:cd01167 55 EFGDFLLETLKEAGvdtRGIQFD--PAAPTTLAFVTLDADGERSFEFY---RGPAADLLLDTELNPdllseADILHFgsi 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 134 --ITNP--KTFVSVCEELAKYGNLK----NRPKIVWEPTPESCLpenwhILQKALKYCDIFSPNEVDSANLLGIDISESK 205
Cdd:cd01167 130 alASEPsrSALLELLEAAKKAGVLIsfdpNLRPPLWRDEEEARE-----RIAELLELADIVKLSDEELELLFGEEDPEEI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 206 SRakefvsafqefQIGHDSQGWVVLRNGSDGCLIgactsSTNAtsdavvpvrEILHLPSVQMKngsVLDTTGAGNAFCGA 285
Cdd:cd01167 205 AA-----------LLLLFGLKLVLVTRGADGALL-----YTKG---------GVGEVPGIPVE---VVDTTGAGDAFVAG 256
|
250 260
....*....|....*....|....
gi 1351604 286 AILEYYRTGNIIEACAKATVAASF 309
Cdd:cd01167 257 LLAQLLSRGLLALDEDELAEALRF 280
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
104-306 |
4.38e-04 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 41.53 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 104 RLFEYLTPKKPIRAPDLLETgliyAKTIHIITN-PKtfvSVCEELAKYGNLKNRPkIVWEPTPESCLPEnwhiLQKALKY 182
Cdd:cd01941 109 DIYELLTPDFLRKIREALKE----AKPIVVDANlPE---EALEYLLALAAKHGVP-VAFEPTSAPKLKK----LFYLLHA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351604 183 CDIFSPNEVDSANLLGIDISESKSRAKEfvsafqefQIGHDSQGW--VVLRNGSDGCLIgactsstnatSDAVVPVrEIL 260
Cdd:cd01941 177 IDLLTPNRAELEALAGALIENNEDENKA--------AKILLLPGIknVIVTLGAKGVLL----------SSREGGV-ETK 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1351604 261 HLPSVQMKNgsVLDTTGAGNAFCG---AAILEYYRTGNIIE---ACAKATVA 306
Cdd:cd01941 238 LFPAPQPET--VVNVTGAGDAFVAglvAGLLEGMSLDDSLRfaqAAAALTLE 287
|
|
| |
