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Conserved domains on  [gi|887234222|ref|NP_001297454|]
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ketohexokinase isoform 3 [Mus musculus]

Protein Classification

Ketohexokinase domain-containing protein (domain architecture ID 10112592)

Ketohexokinase domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
5-250 1.31e-128

Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.


:

Pssm-ID: 238914 [Multi-domain]  Cd Length: 290  Bit Score: 365.58  E-value: 1.31e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVAE-------------- 70
Cdd:cd01939    1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFEsllddfqsrgidis 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  71 ------------------------------NLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQK 120
Cdd:cd01939   81 hcyrkdidepassyiirsraggrttivndnNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 121 VRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDAF 200
Cdd:cd01939  160 ITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAH 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 887234222 201 PPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 250
Cdd:cd01939  240 KPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
5-250 1.31e-128

Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.


Pssm-ID: 238914 [Multi-domain]  Cd Length: 290  Bit Score: 365.58  E-value: 1.31e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVAE-------------- 70
Cdd:cd01939    1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFEsllddfqsrgidis 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  71 ------------------------------NLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQK 120
Cdd:cd01939   81 hcyrkdidepassyiirsraggrttivndnNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 121 VRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDAF 200
Cdd:cd01939  160 ITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAH 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 887234222 201 PPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 250
Cdd:cd01939  240 KPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism];
6-248 6.77e-17

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism];


Pssm-ID: 223598 [Multi-domain]  Cd Length: 311  Bit Score: 78.31  E-value: 6.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   6 ILCVGLVVLDII-NVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSL--------------------- 63
Cdd:COG0524    2 VVVIGEANVDLIaQVVDRLPEPGETVLGDFFKVAGGGKGANVAVALARLGAKVALIGAVgdddfgeflleelrkegvdts 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  64 ---------------------------APGHVAENLPdvsAKDFEKVDLTRFKWIHIEGRNASEQV----KMLQRIEEHN 112
Cdd:COG0524   82 hvvtdegattglalilvdedgertfvfYRGAAALLLT---PEDLDEDELAGADVLHISGIQLEIPPeallAALELAKAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 113 AKQPL---PQKVRvsveieKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALG 189
Cdd:COG0524  159 VTVSFdlnPRPAL------WDRELLEELLALADILFPNEEEAELLTGLEEDAEAAAALLLAKGVKTVVVTLGAEGAVVFT 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 190 PDG-QLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 248
Cdd:COG0524  233 GGGeVTVPVPAAFKVKVVDTTGAGDAFAAGFLAGLLEGKSLEEALRFANAAAALAVTRPG 292
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
9-248 7.72e-13

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 395230 [Multi-domain]  Cd Length: 289  Bit Score: 66.60  E-value: 7.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222    9 VGLVVLDIINVVDKYPEEDTDRRCLSQRwqRGGNASNSCTVLSLLGARCAFMG-------------SLAPGHV------- 68
Cdd:pfam00294   1 IGEANIDLIGTVEGLEGELVRVGTVTKG--PGGKGANVAVALARLGGDVAFIGavgddqfgefllqELKKEGVdtdyvvi 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   69 ---------------------AENLPDVSAKDFEKVD-----LTRFKWIHIEGRNASE-QVKMLQRIEE--HNAKQPLPq 119
Cdd:pfam00294  79 dedtrtgtalievdgdgertiVFNRGAAADLTPEELEenedlLENADLLYISGSLPLGlPEATLEELIEaaKNGGTFDP- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  120 kvRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQS------AVEALRGLYSRVKkgaTLVCAWAEEGADALGPDGQ 193
Cdd:pfam00294 158 --NLLDPLGADLEALLELLPLADLLKPNEEELEALTGAKlddiedALAALHKLAKGVK---TVVVTLGADGALYVEGDGE 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 887234222  194 LLHsDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 248
Cdd:pfam00294 233 VHV-PAVPKVKVVDTTGAGDSFVGGFLAALLEGKSLEEALRFANAVAALVVQKTG 286
PRK11142 PRK11142
ribokinase; Provisional
188-236 1.63e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 44.86  E-value: 1.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 887234222 188 LGPDGQLLHSDAF----PPPRV--VDTLGAGDTFNASVIFSLSKGNSMQEALRFG 236
Cdd:PRK11142 222 LGSRGVWLSENGEgqrvPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
5-250 1.31e-128

Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.


Pssm-ID: 238914 [Multi-domain]  Cd Length: 290  Bit Score: 365.58  E-value: 1.31e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVAE-------------- 70
Cdd:cd01939    1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFEsllddfqsrgidis 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  71 ------------------------------NLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQK 120
Cdd:cd01939   81 hcyrkdidepassyiirsraggrttivndnNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EIR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 121 VRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDAF 200
Cdd:cd01939  160 ITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPAH 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 887234222 201 PPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 250
Cdd:cd01939  240 KPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
5-251 2.09e-20

Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .


Pssm-ID: 238920 [Multi-domain]  Cd Length: 284  Bit Score: 87.35  E-value: 2.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVAENL------------ 72
Cdd:cd01945    1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLIlaelaaegvdts 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  73 -------------------------------PDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQriEEHNAKQPLPqkV 121
Cdd:cd01945   81 fivvapgarspissitditgdratisitaidTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQ--EARARGIPIP--L 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 122 RVSVEIEKPREELFQLFSYgevVFVSKDVAKHLGFQSAVEALRGLYSRvkkGATLVCAWA-EEGADALGPDGQLLHSDAF 200
Cdd:cd01945  157 DLDGGGLRVLEELLPLADH---AICSENFLRPNTGSADDEALELLASL---GIPFVAVTLgEAGCLWLERDGELFHVPAF 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 887234222 201 PPpRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCglQGFDG 251
Cdd:cd01945  231 PV-EVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKC--RGLGG 278
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism];
6-248 6.77e-17

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism];


Pssm-ID: 223598 [Multi-domain]  Cd Length: 311  Bit Score: 78.31  E-value: 6.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   6 ILCVGLVVLDII-NVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSL--------------------- 63
Cdd:COG0524    2 VVVIGEANVDLIaQVVDRLPEPGETVLGDFFKVAGGGKGANVAVALARLGAKVALIGAVgdddfgeflleelrkegvdts 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  64 ---------------------------APGHVAENLPdvsAKDFEKVDLTRFKWIHIEGRNASEQV----KMLQRIEEHN 112
Cdd:COG0524   82 hvvtdegattglalilvdedgertfvfYRGAAALLLT---PEDLDEDELAGADVLHISGIQLEIPPeallAALELAKAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 113 AKQPL---PQKVRvsveieKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALG 189
Cdd:COG0524  159 VTVSFdlnPRPAL------WDRELLEELLALADILFPNEEEAELLTGLEEDAEAAAALLLAKGVKTVVVTLGAEGAVVFT 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 190 PDG-QLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 248
Cdd:COG0524  233 GGGeVTVPVPAAFKVKVVDTTGAGDAFAAGFLAGLLEGKSLEEALRFANAAAALAVTRPG 292
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
6-223 1.56e-14

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: 69.82  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGslapghvaenlpdvsakdfekvdl 85
Cdd:cd00287    2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  86 trFKWIHIEGRNAS--EQVKMLQRIEEHNakqplpqkVRVSVE-----IEKPREELFQLFSYGEVVFVSKDVAKHLGFQ- 157
Cdd:cd00287   58 --ADAVVISGLSPApeAVLDALEEARRRG--------VPVVLDpgpraVRLDGEELEKLLPGVDILTPNEEEAEALTGRr 127
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887234222 158 --SAVEALRGLYSRVKKGATLVCAWAEEGADAL-GPDGQLLHSDAFpPPRVVDTLGAGDTFNASVIFSL 223
Cdd:cd00287  128 dlEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVaTRGGTEVHVPAF-PVKVVDTTGAGDAFLAALAAGL 195
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
6-243 4.94e-14

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: 69.65  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAP------------------GH 67
Cdd:cd01942    2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEdfhgrlyleelreegvdtSH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  68 VAENLPDVSAKDFEKVD-----LTRFKWIHIEG--RNASEQVKMLQRI--------EEHNAKQPLPQKVRVSV----EIE 128
Cdd:cd01942   82 VRVVDEDSTGVAFILTDgddnqIAYFYPGAMDElePNDEADPDGLADIvhlssgpgLIELARELAAGGITVSFdpgqELP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 129 K-PREELFQLFSYGEVVFVSKDVAKHL----GFQSAVEALRGLYSRVKKGAtlvcawaeEGADALGPDGQLLHsDAFPPP 203
Cdd:cd01942  162 RlSGEELEEILERADILFVNDYEAELLkertGLSEAELASGVRVVVVTLGP--------KGAIVFEDGEEVEV-PAVPAV 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 887234222 204 RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKK 243
Cdd:cd01942  233 KVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
9-248 7.72e-13

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 395230 [Multi-domain]  Cd Length: 289  Bit Score: 66.60  E-value: 7.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222    9 VGLVVLDIINVVDKYPEEDTDRRCLSQRwqRGGNASNSCTVLSLLGARCAFMG-------------SLAPGHV------- 68
Cdd:pfam00294   1 IGEANIDLIGTVEGLEGELVRVGTVTKG--PGGKGANVAVALARLGGDVAFIGavgddqfgefllqELKKEGVdtdyvvi 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   69 ---------------------AENLPDVSAKDFEKVD-----LTRFKWIHIEGRNASE-QVKMLQRIEE--HNAKQPLPq 119
Cdd:pfam00294  79 dedtrtgtalievdgdgertiVFNRGAAADLTPEELEenedlLENADLLYISGSLPLGlPEATLEELIEaaKNGGTFDP- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  120 kvRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQS------AVEALRGLYSRVKkgaTLVCAWAEEGADALGPDGQ 193
Cdd:pfam00294 158 --NLLDPLGADLEALLELLPLADLLKPNEEELEALTGAKlddiedALAALHKLAKGVK---TVVVTLGADGALYVEGDGE 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 887234222  194 LLHsDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 248
Cdd:pfam00294 233 VHV-PAVPKVKVVDTTGAGDSFVGGFLAALLEGKSLEEALRFANAVAALVVQKTG 286
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
127-248 7.56e-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: 63.75  E-value: 7.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 127 IEKPREELFQLFSYGEVVFVSK-DVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLlHSDAFPPPrV 205
Cdd:cd01166  172 AEEAREALEELLPYVDIVLPSEeEAEALLGDEDPTDAAERALALALGVKAVVVKLGAEGALVYTGGGRV-FVPAYPVE-V 249
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 887234222 206 VDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 248
Cdd:cd01166  250 VDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
188-241 2.51e-10

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: 59.10  E-value: 2.51e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 188 LGPDGQLLHSD----AFPPPRV--VDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAG 241
Cdd:cd01174  219 LGAKGALLASGgeveHVPAFKVkaVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
18-248 7.59e-09

Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.


Pssm-ID: 238915 [Multi-domain]  Cd Length: 264  Bit Score: 54.67  E-value: 7.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  18 NVVDKYPEEDTDRRclsqrwqrGGNASNSCTVLSLLGARCAFMGSLAPGHVAENLPDVSAKDFEKVDLTRFKwihiEGRN 97
Cdd:cd01940    8 NVVDKYLHLGKMYP--------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK----EGEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  98 ASEQVKMLQ--RIEEHNAKQPLPQKVRVSVEIEKPR----------------EELFQLFSYGEVVfVSKDVAKH------ 153
Cdd:cd01940   76 AVADVELVDgdRIFGLSNKGGVAREHPFEADLEYLSqfdlvhtgiysheghlEKALQALVGAGAL-ISFDFSDRwdddyl 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 154 --------LGFQSAVE--------ALRGLYSRvkkGATLVCAwaeegadALGPDGQLLHSDAF---PPPR---VVDTLGA 211
Cdd:cd01940  155 qlvcpyvdFAFFSASDlsdeevkaKLKEAVSR---GAKLVIV-------TRGEDGAIAYDGAVfysVAPRpveVVDTLGA 224
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 887234222 212 GDTFNASVIFS-LSKGNSMQEALRFGCQVAGKKCGLQG 248
Cdd:cd01940  225 GDSFIAGFLLSlLAGGTAIAEAMRQGAQFAAKTCGHEG 262
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
3-248 2.16e-08

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: 53.77  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   3 EKQILCVGLVVLDIINVVDKYPEEDTD----RRCLSQRWQR-------------GGNASNSCTVLSLLGARCAFMGS--- 62
Cdd:cd01168    1 RYDVLGLGNALVDILAQVDDAFLEKLGlkkgDMILADMEEQeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRvgd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  63 ----------------LAPGHVAENLP------------------------DVSAKDFEKVDLTRFKWIHIEG--RNASE 100
Cdd:cd01168   81 dklgdfllkdlraagvDTRYQVQPDGPtgtcavlvtpdaertmctylgaanELSPDDLDWSLLAKAKYLYLEGylLTVPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 101 QV--KMLQRIEEHNakqplpqkVRVSV------EIEKPREELFQLFSYGEVVFVSKDVAKHLGFQ----SAVEALRGLYS 168
Cdd:cd01168  161 EAilLAAEHAKENG--------VKIALnlsapfIVQRFKEALLELLPYVDILFGNEEEAEALAEAettdDLEAALKLLAL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 169 RVKkgaTLVCAWAEEGAdALGPDGQLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 248
Cdd:cd01168  233 RCR---IVVITQGAKGA-VVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
180-248 5.20e-08

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: 52.64  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 180 WAEEGADAL----GPDGQLLHSDAF------PPPRVVDTLGAGDTFNASVIFSLSKGNSMQ-------EALRFGCQVAGK 242
Cdd:cd01167  208 LLLFGLKLVlvtrGADGALLYTKGGvgevpgIPVEVVDTTGAGDAFVAGLLAQLLSRGLLAldedelaEALRFANAVGAL 287

                 ....*.
gi 887234222 243 KCGLQG 248
Cdd:cd01167  288 TCTKAG 293
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
73-236 8.45e-08

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 51.76  E-value: 8.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  73 PDVSAKDFEKVdLTRFK-------WIHIEG---RNASEQ--VKMLQRIEEHNAK-------QPLPQKVRVSVEIEKP-RE 132
Cdd:cd01164  108 PEISEEELEAL-LEKLKallkkgdIVVLSGslpPGVPADfyAELVRLAREKGARvildtsgEALLAALAAKPFLIKPnRE 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 133 ELFQLFSygevvfvskdvAKHLGFQSAVEALRGLysrVKKGATLVCAwaeegadALGPDGQLL-HSDAF-----PPPRVV 206
Cdd:cd01164  187 ELEELFG-----------RPLGDEEDVIAAARKL---IERGAENVLV-------SLGADGALLvTKDGVyraspPKVKVV 245
                        170       180       190
                 ....*....|....*....|....*....|
gi 887234222 207 DTLGAGDTFNASVIFSLSKGNSMQEALRFG 236
Cdd:cd01164  246 STVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
182-242 4.05e-06

Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238922 [Multi-domain]  Cd Length: 265  Bit Score: 46.64  E-value: 4.05e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 887234222 182 EEGAdALGPDGQLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGK 242
Cdd:cd01947  199 ELGA-ILYPGGRYNHVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAI 257
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
156-241 4.51e-06

YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 46.65  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 156 FQSAVEA-LRGLYSRVKkgATLVCAWAEEGADALGPDGQLLHSDAFPPpRVVDTLGAGDTFNASVIFSLSKGNSMQEALR 234
Cdd:cd01944  199 GDPAAEAsALRIYAKTA--APVVVRLGSNGAWIRLPDGNTHIIPGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVL 275

                 ....*..
gi 887234222 235 FGCQVAG 241
Cdd:cd01944  276 LANAAAA 282
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
188-243 7.00e-06

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: 46.15  E-value: 7.00e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 887234222 188 LGPDGQLLHSDA-------FPPP---RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGcQVAGKK 243
Cdd:cd01941  220 LGAKGVLLSSREggvetklFPAPqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA-QAAAAL 284
PRK11142 PRK11142
ribokinase; Provisional
188-236 1.63e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 44.86  E-value: 1.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 887234222 188 LGPDGQLLHSDAF----PPPRV--VDTLGAGDTFNASVIFSLSKGNSMQEALRFG 236
Cdd:PRK11142 222 LGSRGVWLSENGEgqrvPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
5-243 2.43e-05

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: 44.31  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222   5 QILCVGLVVLDIINVVDkypeedtdrrclSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVA----ENLPDVSAKDF 80
Cdd:cd01937    1 KIVIIGHVTIDEIVTNG------------SGVVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDkwsdLFDNGIEVISL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  81 EKVDLTRFKWIHI-EGRNASEQVKMLQRIEEHNAKQ----------PLPQKV-RVSVEIEKP---------------REE 133
Cdd:cd01937   69 LSTETTTFELNYTnEGRTRTLLAKCAAIPDTESPLStitaeivilgPVPEEIsPSLFRKFAFisldaqgflrranqeKLI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 134 LFQLFSYGEVVFVSKDVAKHLgfQSAVEALRGLysRVKKGATLVCAWAEEGA---DALGPDgqllhsdAFPPPR--VVDT 208
Cdd:cd01937  149 KCVILKLHDVLKLSRVEAEVI--STPTELARLI--KETGVKEIIVTDGEEGGyifDGNGKY-------TIPASKkdVVDP 217
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 887234222 209 LGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKK 243
Cdd:cd01937  218 TGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKF 252
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
127-237 3.71e-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: 43.99  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 127 IEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSRVKKgaTLVCAWAEEGAdALGPDGQLLHSDAFPPPRV 205
Cdd:cd01946  150 ISIKPEKLKKVLAKVDVVIINDGEARQLtGAANLVKAARLILAMGPK--ALIIKRGEYGA-LLFTDDGYFAAPAYPLESV 226
                         90       100       110
                 ....*....|....*....|....*....|...
gi 887234222 206 VDTLGAGDTFNASVIFSL-SKGNSMQEALRFGC 237
Cdd:cd01946  227 FDPTGAGDTFAGGFIGYLaSQKDTSEANMRRAI 259
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
166-248 5.35e-05

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 43.19  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 166 LYSRVKKGATLVCA-WAEEGAdaLGPDGQLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKC 244
Cdd:PRK09813 177 MKAIVARGAGVVIVtLGENGS--IAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTI 254

                 ....
gi 887234222 245 GLQG 248
Cdd:PRK09813 255 QYHG 258
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
182-245 5.64e-05

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: 43.32  E-value: 5.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887234222 182 EEGADALGPDGQLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCG 245
Cdd:cd01172  228 EEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVG 290
PTZ00292 PTZ00292
ribokinase; Provisional
3-63 4.91e-04

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 40.49  E-value: 4.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 887234222   3 EKQILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSL 63
Cdd:PTZ00292  15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMV 75
FruK COG1105
Fructose-1-phosphate kinase or kinase (PfkB) [Carbohydrate transport and metabolism];
188-236 5.18e-04

Fructose-1-phosphate kinase or kinase (PfkB) [Carbohydrate transport and metabolism];


Pssm-ID: 224030 [Multi-domain]  Cd Length: 310  Bit Score: 40.66  E-value: 5.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 887234222 188 LGPDGQLL-HSDAF-----PPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFG 236
Cdd:COG1105  222 LGADGALLvTAEGVyfaspPKVQVVSTVGAGDSMVAGFLAGLLKGKSLEEALRFA 276
fruK PRK09513
1-phosphofructokinase; Provisional
174-240 1.36e-03

1-phosphofructokinase; Provisional


Pssm-ID: 181923  Cd Length: 312  Bit Score: 39.29  E-value: 1.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 887234222 174 ATLVCAWAEEGADALGPDGQLLhsdAFPPP-RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVA 240
Cdd:PRK09513 218 AHVVISLGAEGALWVNASGEWI---AKPPAcDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVS 282
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
157-231 2.22e-03

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 38.38  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 157 QSAVEALRGLYSR----VKKGATLVCAWAEegadalgpdGQLLHsdaFPPPRV--VDTLGAGDTFNASVIFSLSKGNSMQ 230
Cdd:PRK09434 201 EDAIYALADRYPIalllVTLGAEGVLVHTR---------GQVQH---FPAPSVdpVDTTGAGDAFVAGLLAGLSQAGLWT 268

                 .
gi 887234222 231 E 231
Cdd:PRK09434 269 D 269
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
75-237 7.84e-03

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005  Cd Length: 367  Bit Score: 37.08  E-value: 7.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222  75 VSAKDFEKVDLTRFKWIHIE-GRNASEQVKMLQRIeehnAKQplpQKVRVSVE------IEKPREELFQLFSYGEV--VF 145
Cdd:PLN02379 165 LQADELTKEDFKGSKWLVLRyGFYNLEVIEAAIRL----AKQ---EGLSVSLDlasfemVRNFRSPLLQLLESGKIdlCF 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887234222 146 VSKDVAKHL---GFQSAVEALRGLYSRVkkgatlvCAWAeegADALGPDG-------QLLHSDAFPPPRVVDTLGAGDTF 215
Cdd:PLN02379 238 ANEDEARELlrgEQESDPEAALEFLAKY-------CNWA---VVTLGSKGciarhgkEVVRVPAIGETNAVDATGAGDLF 307
                        170       180
                 ....*....|....*....|..
gi 887234222 216 NASVIFSLSKGNSMQEALRFGC 237
Cdd:PLN02379 308 ASGFLYGLIKGLSLEECCKVGA 329
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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