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Conserved domains on  [gi|31982229|ref|NP_032465|]
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ketohexokinase isoform 2 [Mus musculus]

Protein Classification

ketohexokinase( domain architecture ID 10112592)

ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose; it can also phosphorylate several other furanose sugars

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 ...
 5-295 1.52e-153

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: 430.67  E-value: 1.52e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVS 84
Cdd:cd01939   1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  85 QVtWQSQGDTPCSCCIVNNSNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQ 164
Cdd:cd01939  81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 165 KVRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDA 244
Cdd:cd01939 159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 31982229 245 FPPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 295
Cdd:cd01939 239 HKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 5-295 1.52e-153

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: 430.67  E-value: 1.52e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVS 84
Cdd:cd01939   1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  85 QVtWQSQGDTPCSCCIVNNSNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQ 164
Cdd:cd01939  81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 165 KVRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDA 244
Cdd:cd01939 159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 31982229 245 FPPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 295
Cdd:cd01939 239 HKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 5-289 1.21e-43

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: 150.81  E-value: 1.21e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVS 84
Cdd:COG0524   1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  85 QVTWQSQGDTPCSCCIVNNsNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEG------RNASEQVKMLQRIEEHNa 158
Cdd:COG0524  81 GVRRDPGAPTGLAFILVDP-DGERTIVFYRGANAELTPEDLDEALLAGADILHLGGitlasePPREALLAALEAARAAG- 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 159 kqplpqkVRVSV-------EIEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSR------VKKGAtlvca 224
Cdd:COG0524 159 -------VPVSLdpnyrpaLWEPARELLRELLALVDILFPNEEEAELLtGETDPEEAAAALLARgvklvvVTLGA----- 226

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982229 225 waeEGADALGpDGQLLHSDAFpPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKC 289
Cdd:COG0524 227 ---EGALLYT-GGEVVHVPAF-PVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVV 286
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 6-293 4.16e-28

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 109.74  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229     6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRwqRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSQ 85
Cdd:pfam00294   2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229    86 VTWQSQGDTpCSCCIVNNSNGSRTIILYDTNLPDVSAKDFEKV--DLTRFKWIHIEGRNASE-QVKMLQRIEE--HNAKQ 160
Cdd:pfam00294  80 VVIDEDTRT-GTALIEVDGDGERTIVFNRGAAADLTPEELEENedLLENADLLYISGSLPLGlPEATLEELIEaaKNGGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   161 PLPqkvRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQ---SAVEALRGLYSRVKKGA-TLVCAWAEEGADALGPD 236
Cdd:pfam00294 159 FDP---NLLDPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEGD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 31982229   237 GQLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:pfam00294 236 GEVHV-PAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
PTZ00292 PTZ00292
ribokinase; Provisional
 3-285 2.00e-12

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 66.68  E-value: 2.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229    3 EKQILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVD 82
Cdd:PTZ00292  15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   83 VSQVTWQSQGDTPCSCCIVNNSNGSRTIILydtnLPdvSAKDFEKVDLTRFKWIHIEGR------------NASEQVkmL 150
Cdd:PTZ00292  95 TSFVSRTENSSTGLAMIFVDTKTGNNEIVI----IP--GANNALTPQMVDAQTDNIQNIckylicqneiplETTLDA--L 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  151 QRIEEHNAK---QPLPQKVRVSVEIEKPreelfqLFSYGEVVFVSKdvakhlgfqsaVEA-------LRGLYSRVKKGAT 220
Cdd:PTZ00292 167 KEAKERGCYtvfNPAPAPKLAEVEIIKP------FLKYVSLFCVNE-----------VEAalitgmeVTDTESAFKASKE 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982229  221 LVCAWAEEGADALGPDGQLLHSDAFPPP-------RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:PTZ00292 230 LQQLGVENVIITLGANGCLIVEKENEPVhvpgkrvKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIA 301
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 40-285 1.24e-11

ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]


Pssm-ID: 274000 [Multi-domain]  Cd Length: 293  Bit Score: 63.77  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229    40 GGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSQVTWQSQGDTPCSCCIVNNsNGSRTIILYD-TNL- 117
Cdd:TIGR02152  31 GGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDD-TGENRIVVVAgANAe 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   118 --PDVSAKDFEKVDLTRFKWIHIEGR-NASEQVkmLQRIEEHN---------AKQPLPQKVRVSVEIEKPREElfqlfsy 185
Cdd:TIGR02152 110 ltPEDIDAAEALIAESDIVLLQLEIPlETVLEA--AKIAKKHGvkvilnpapAIKDLDDELLSLVDIITPNET------- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   186 gEVVFVSKDVAKHLgfQSAVEALRGLYSRVKKGATLvcawaeegadALGPDGQLLHSDA----FPPPRV--VDTLGAGDT 259
Cdd:TIGR02152 181 -EAEILTGIEVTDE--EDAEKAAEKLLEKGVKNVII----------TLGSKGALLVSKDesklIPAFKVkaVDTTAAGDT 247

                         250       260
                  ....*....|....*....|....*.
gi 31982229   260 FNASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:TIGR02152 248 FNGAFAVALAEGKSLEDAIRFANAAA 273
 
Name Accession Description Interval E-value
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 5-295 1.52e-153

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: 430.67  E-value: 1.52e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVS 84
Cdd:cd01939   1 AVLCVGLTVLDFITTVDKYPFEDSDQRTTNGRWQRGGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  85 QVtWQSQGDTPCSCCIVNNSNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQRIEEHNAKQPlPQ 164
Cdd:cd01939  81 HC-YRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGRNPDETLRMMQHIEEHNNRRP-EI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 165 KVRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLYSRVKKGATLVCAWAEEGADALGPDGQLLHSDA 244
Cdd:cd01939 159 RITISVEVEKPREELLELAAYCDVVFVSKDWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGALGPDGEYVHSPA 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 31982229 245 FPPPRVVDTLGAGDTFNASVIFSLSKG-NSMQEALRFGCQVAGKKCGLQGFD 295
Cdd:cd01939 239 HKPIRVVDTLGAGDTFNAAVIYALNKGpDDLSEALDFGNRVASQKCTGVGFD 290
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 5-289 1.21e-43

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: 150.81  E-value: 1.21e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVS 84
Cdd:COG0524   1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  85 QVTWQSQGDTPCSCCIVNNsNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEG------RNASEQVKMLQRIEEHNa 158
Cdd:COG0524  81 GVRRDPGAPTGLAFILVDP-DGERTIVFYRGANAELTPEDLDEALLAGADILHLGGitlasePPREALLAALEAARAAG- 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 159 kqplpqkVRVSV-------EIEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSR------VKKGAtlvca 224
Cdd:COG0524 159 -------VPVSLdpnyrpaLWEPARELLRELLALVDILFPNEEEAELLtGETDPEEAAAALLARgvklvvVTLGA----- 226

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31982229 225 waeEGADALGpDGQLLHSDAFpPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKC 289
Cdd:COG0524 227 ---EGALLYT-GGEVVHVPAF-PVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVV 286
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 5-296 2.62e-30

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: 115.47  E-value: 2.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVS 84
Cdd:cd01945   1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  85 QVTWQSQGDTPCSccIVNNSNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEGRNASEQVKMLQriEEHNAKQPLPq 164
Cdd:cd01945  81 FIVVAPGARSPIS--SITDITGDRATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPEAALHLAQ--EARARGIPIP- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 165 kVRVSVEIEKPREELFQLFSYgevVFVSKDVAKHLGFQSAVEALRGLYSRvkkGATLVCAWA-EEGADALGPDGQLLHSD 243
Cdd:cd01945 156 -LDLDGGGLRVLEELLPLADH---AICSENFLRPNTGSADDEALELLASL---GIPFVAVTLgEAGCLWLERDGELFHVP 228

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 31982229 244 AFpPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCglQGFDG 296
Cdd:cd01945 229 AF-PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKC--RGLGG 278
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 6-293 4.16e-28

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 109.74  E-value: 4.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229     6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRwqRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSQ 85
Cdd:pfam00294   2 VVVIGEANIDLIGNVEGLPGELVRVSTVEKG--PGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229    86 VTWQSQGDTpCSCCIVNNSNGSRTIILYDTNLPDVSAKDFEKV--DLTRFKWIHIEGRNASE-QVKMLQRIEE--HNAKQ 160
Cdd:pfam00294  80 VVIDEDTRT-GTALIEVDGDGERTIVFNRGAAADLTPEELEENedLLENADLLYISGSLPLGlPEATLEELIEaaKNGGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   161 PLPqkvRVSVEIEKPREELFQLFSYGEVVFVSKDVAKHLGFQ---SAVEALRGLYSRVKKGA-TLVCAWAEEGADALGPD 236
Cdd:pfam00294 159 FDP---NLLDPLGAAREALLELLPLADLLKPNEEELEALTGAkldDIEEALAALHKLLAKGIkTVIVTLGADGALVVEGD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 31982229   237 GQLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:pfam00294 236 GEVHV-PAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSG 291
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 5-293 1.03e-23

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: 98.03  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIinvvdkYPEEDtDRRCLSQRWQR--GGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVD 82
Cdd:cd01166   1 DVVTIGEVMVDL------SPPGG-GRLEQADSFRKffGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  83 VSQVTwQSQGDTPCSCCIVNNSNGSRTIIlYDTN---LPDVSAKDFEKVDLTRFKWIHIEG----RNASEQVKMLQRIEE 155
Cdd:cd01166  74 TSHVR-VDPGRPTGLYFLEIGAGGERRVL-YYRAgsaASRLTPEDLDEAALAGADHLHLSGitlaLSESAREALLEALEA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 156 HNAKQplpqkVRVSVEI---------EKPREELFQLFSYGEVVFVSK-DVAKHLGFQSAVEALRGLYSRVKKGATLVCAW 225
Cdd:cd01166 152 AKARG-----VTVSFDLnyrpklwsaEEAREALEELLPYVDIVLPSEeEAEALLGDEDPTDAAERALALALGVKAVVVKL 226

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982229 226 AEEGADALGPDGQLlHSDAFPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:cd01166 227 GAEGALVYTGGGRV-FVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPG 292
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 6-288 4.98e-20

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: 87.37  E-value: 4.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLApghvADF----LVADFRQRGV 81
Cdd:cd01942   2 VAVVGHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVG----EDFhgrlYLEELREEGV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  82 DVSQVTWQSQGDTPCSCCIVNNSNgSRTIILY----DTNLPDVSAKDFEKVDLtrfkwIHIEGRnaseqvkmlqRIEEHN 157
Cdd:cd01942  78 DTSHVRVVDEDSTGVAFILTDGDD-NQIAYFYpgamDELEPNDEADPDGLADI-----VHLSSG----------PGLIEL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 158 AKQPLPQKVRVSV----EIEK-PREELFQLFSYGEVVFVSKDVAKHL----GFQSAVEALRGLYSRVKKGAtlvcawaeE 228
Cdd:cd01942 142 ARELAAGGITVSFdpgqELPRlSGEELEEILERADILFVNDYEAELLkertGLSEAELASGVRVVVVTLGP--------K 213

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 229 GADALGPDGQLLHsDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKK 288
Cdd:cd01942 214 GAIVFEDGEEVEV-PAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLK 272
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 3-293 1.14e-18

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: 84.20  E-value: 1.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   3 EKQILCVGLVVLDIINVVDKYPEEDTD----RRCLSQRWQR-------------GGNASNSCTVLSLLGARCAFMGSLAP 65
Cdd:cd01168   1 RYDVLGLGNALVDILAQVDDAFLEKLGlkkgDMILADMEEQeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  66 GHVADFLVADFRQRGVDVSQVTWQSQGDTPCSCCIvnNSNGSRTiilYDTNL---PDVSAKDFEKVDLTRFKWIHIEG-- 140
Cdd:cd01168  81 DKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLV--TPDAERT---MCTYLgaaNELSPDDLDWSLLAKAKYLYLEGyl 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 141 RNASEQV--KMLQRIEEHNakqplpqkVRVSV------EIEKPREELFQLFSYGEVVFVSKDVAKHLGFQ----SAVEAL 208
Cdd:cd01168 156 LTVPPEAilLAAEHAKENG--------VKIALnlsapfIVQRFKEALLELLPYVDILFGNEEEAEALAEAettdDLEAAL 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 209 RGLYSRVKkgaTLVCAWAEEGAdALGPDGQLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKK 288
Cdd:cd01168 228 KLLALRCR---IVVITQGAKGA-VVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEV 303


                ....*
gi 31982229 289 CGLQG 293
Cdd:cd01168 304 IQQLG 308
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 18-293 2.89e-17

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: 79.71  E-value: 2.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  18 NVVDKYPEEDTDRRclsqrwqrGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSQVTwQSQGDTPCS 97
Cdd:cd01940   8 NVVDKYLHLGKMYP--------GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCR-VKEGENAVA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  98 CciVNNSNGSRTIILYDTN-----LPDvsAKDFEKvdLTRFKWIHI-EGRNASEQVKMLQriEEHNAKQPLPQKVRVSVE 171
Cdd:cd01940  79 D--VELVDGDRIFGLSNKGgvareHPF--EADLEY--LSQFDLVHTgIYSHEGHLEKALQ--ALVGAGALISFDFSDRWD 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 172 IEkpreELFQLFSYGEVVFVSkdvAKHLGFQSAVEALRGLYSRvkkGATLVCAwaeegadALGPDGQLLHSDAF---PPP 248
Cdd:cd01940 151 DD----YLQLVCPYVDFAFFS---ASDLSDEEVKAKLKEAVSR---GAKLVIV-------TRGEDGAIAYDGAVfysVAP 213

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 31982229 249 R---VVDTLGAGDTFNASVIFS-LSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:cd01940 214 RpveVVDTLGAGDSFIAGFLLSlLAGGTAIAEAMRQGAQFAAKTCGHEG 262
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 5-293 7.22e-17

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: 78.83  E-value: 7.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIInvvdkyPEEDTDrrclSQRWQR--GGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVD 82
Cdd:cd01167   1 KVVCFGEALIDFI------PEGSGA----PETFTKapGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  83 VSQVtwQSQGDTPCSCCIVN-NSNGSRTIILYDTNLPDVSA-KDFEKVDLTRFKWIH------IEGRNASEQVKMLQRIE 154
Cdd:cd01167  71 TRGI--QFDPAAPTTLAFVTlDADGERSFEFYRGPAADLLLdTELNPDLLSEADILHfgsialASEPSRSALLELLEAAK 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 155 EHNAKqplpqkvrVSVEI----------EKPREELFQLFSYGEVVFVSKDVAKHLGFQSAVEALRGLysrvkkgatlvca 224
Cdd:cd01167 149 KAGVL--------ISFDPnlrpplwrdeEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAAL------------- 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 225 WAEEGADAL----GPDGQLLHSDAF------PPPRVVDTLGAGDTFNASVIFSLSKGNSMQ-------EALRFGCQVAGK 287
Cdd:cd01167 208 LLLFGLKLVlvtrGADGALLYTKGGvgevpgIPVEVVDTTGAGDAFVAGLLAQLLSRGLLAldedelaEALRFANAVGAL 287


                ....*.
gi 31982229 288 KCGLQG 293
Cdd:cd01167 288 TCTKAG 293
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 6-286 1.89e-13

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: 68.99  E-value: 1.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGnASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSq 85
Cdd:cd01944   2 VLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  86 vTWQSQGDTPCSCCIVNNSNGSRTIILYDTNLPDVSAKDFEKVDLTRFKWIHIEG-----RNASEQVkMLQRIEEHNAKQ 160
Cdd:cd01944  80 -LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDYVYLSGytlasENASKVI-LLEWLEALPAGT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 161 PL-----PqkvRVSveiEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSRVKKGATLVCAWAEEGADALG 234
Cdd:cd01944 158 TLvfdpgP---RIS---DIPDTILQALMAKRPIWSCNREEAAIFaERGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRL 231

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 31982229 235 PDGQLLHSDAFPPpRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAG 286
Cdd:cd01944 232 PDGNTHIIPGFKV-KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAA 282
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 14-281 7.09e-13

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: 67.56  E-value: 7.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  14 LDIINVVDKyPEEDTDRRCLSQRWQRGG---NASNsctVLSLLGARCAFMGsLAPGHVADFLVADFRQRGVDVSQVTwqS 90
Cdd:cd01164  11 IDLTIELDQ-LQPGEVNRVSSTRKDAGGkgiNVAR---VLKDLGVEVTALG-FLGGFTGDFFEALLKEEGIPDDFVE--V 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  91 QGDTPCSCCIVNNSNGSrtiilYDTNL--PDVSAKDFEKVdLTRFK-------WIHIEG---RNASEQ--VKMLQRIEEH 156
Cdd:cd01164  84 AGETRINVKIKEEDGTE-----TEINEpgPEISEEELEAL-LEKLKallkkgdIVVLSGslpPGVPADfyAELVRLAREK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 157 NAK-------QPLPQKVRVSVEIEKP-REELFQLFSygevvfvskdvAKHLGFQSAVEALRGLysrVKKGATLVCAwaee 228
Cdd:cd01164 158 GARvildtsgEALLAALAAKPFLIKPnREELEELFG-----------RPLGDEEDVIAAARKL---IERGAENVLV---- 219

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 31982229 229 gadALGPDGQLL-HSDAF-----PPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFG 281
Cdd:cd01164 220 ---SLGADGALLvTKDGVyraspPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 6-287 1.34e-12

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: 66.29  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSq 85
Cdd:cd01947   2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  86 VTWQSQGdTPCSCCIVNNsNGSRTIilydTNLPDVSAKDFEKVDLTRFKWIHIegrNASEQVKMLQRIEEHNAKQPLPQK 165
Cdd:cd01947  81 VAWRDKP-TRKTLSFIDP-NGERTI----TVPGERLEDDLKWPILDEGDGVFI---TAAAVDKEAIRKCRETKLVILQVT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 166 VRVSVEIEKPREELFQLFSYGEVVFVSKDVAKhlgfqsaVEALRGL-YSRVKKGatlvcawaEEGAdALGPDGQLLHSDA 244
Cdd:cd01947 152 PRVRVDELNQALIPLDILIGSRLDPGELVVAE-------KIAGPFPrYLIVTEG--------ELGA-ILYPGGRYNHVPA 215

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 31982229 245 FPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGK 287
Cdd:cd01947 216 KKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAI 257
PTZ00292 PTZ00292
ribokinase; Provisional
 3-285 2.00e-12

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 66.68  E-value: 2.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229    3 EKQILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVD 82
Cdd:PTZ00292  15 EPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   83 VSQVTWQSQGDTPCSCCIVNNSNGSRTIILydtnLPdvSAKDFEKVDLTRFKWIHIEGR------------NASEQVkmL 150
Cdd:PTZ00292  95 TSFVSRTENSSTGLAMIFVDTKTGNNEIVI----IP--GANNALTPQMVDAQTDNIQNIckylicqneiplETTLDA--L 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  151 QRIEEHNAK---QPLPQKVRVSVEIEKPreelfqLFSYGEVVFVSKdvakhlgfqsaVEA-------LRGLYSRVKKGAT 220
Cdd:PTZ00292 167 KEAKERGCYtvfNPAPAPKLAEVEIIKP------FLKYVSLFCVNE-----------VEAalitgmeVTDTESAFKASKE 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31982229  221 LVCAWAEEGADALGPDGQLLHSDAFPPP-------RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:PTZ00292 230 LQQLGVENVIITLGANGCLIVEKENEPVhvpgkrvKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIA 301
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
31-281 5.80e-12

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 64.77  E-value: 5.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  31 RCLSQRWQRGGNASNSCTVLSLLGARCAFMGSLApGHVADFLVADFRQRGVDVSQVtwQSQGDTPCSCCIVNNSNGSRTI 110
Cdd:COG1105  26 RASEVRLDPGGKGINVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFV--PIEGETRINIKIVDPSDGTETE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 111 IlydtNL--PDVSAKDFEKV------DLTRFKWIHIEG---RNASEQ--VKMLQRIEEHNAK-------QPLPQKVRVSV 170
Cdd:COG1105 103 I----NEpgPEISEEELEALlerleeLLKEGDWVVLSGslpPGVPPDfyAELIRLARARGAKvvldtsgEALKAALEAGP 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 171 EIEKP-REELFQLFSygevvfvsKDVAkhlGFQSAVEALRGLysrVKKGATLVCAwaeegadALGPDGQLL-------HS 242
Cdd:COG1105 179 DLIKPnLEELEELLG--------RPLE---TLEDIIAAAREL---LERGAENVVV-------SLGADGALLvtedgvyRA 237

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 31982229 243 DAfPPPRVVDTLGAGDTFNASVIFSLSKGNSMQEALRFG 281
Cdd:COG1105 238 KP-PKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLA 275
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 40-285 1.24e-11

ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]


Pssm-ID: 274000 [Multi-domain]  Cd Length: 293  Bit Score: 63.77  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229    40 GGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSQVTWQSQGDTPCSCCIVNNsNGSRTIILYD-TNL- 117
Cdd:TIGR02152  31 GGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDD-TGENRIVVVAgANAe 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   118 --PDVSAKDFEKVDLTRFKWIHIEGR-NASEQVkmLQRIEEHN---------AKQPLPQKVRVSVEIEKPREElfqlfsy 185
Cdd:TIGR02152 110 ltPEDIDAAEALIAESDIVLLQLEIPlETVLEA--AKIAKKHGvkvilnpapAIKDLDDELLSLVDIITPNET------- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   186 gEVVFVSKDVAKHLgfQSAVEALRGLYSRVKKGATLvcawaeegadALGPDGQLLHSDA----FPPPRV--VDTLGAGDT 259
Cdd:TIGR02152 181 -EAEILTGIEVTDE--EDAEKAAEKLLEKGVKNVII----------TLGSKGALLVSKDesklIPAFKVkaVDTTAAGDT 247

                         250       260
                  ....*....|....*....|....*.
gi 31982229   260 FNASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:TIGR02152 248 FNGAFAVALAEGKSLEDAIRFANAAA 273
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 40-286 7.53e-11

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: 61.41  E-value: 7.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  40 GGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSQVTwQSQGDTPCSCCIVNNSNGSRTIILY------ 113
Cdd:cd01174  36 GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVE-VVVGAPTGTAVITVDESGENRIVVVpgange 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 114 -DTNLPDVSAKDFEKVD--LTRFKwIHIEgrnASEQVkmLQRIEEHNAK--------QPLPQKVRVSVEIEKPRE-ELFQ 181
Cdd:cd01174 115 lTPADVDAALELIAAADvlLLQLE-IPLE---TVLAA--LRAARRAGVTvilnpapaRPLPAELLALVDILVPNEtEAAL 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 182 LFsyGEVVfvskdvakhLGFQSAVEALRGLYSRVKKgaTLVCAWAEEGADALGPDGQLLHsdAFPPPRVVDTLGAGDTFN 261
Cdd:cd01174 189 LT--GIEV---------TDEEDAEKAARLLLAKGVK--NVIVTLGAKGALLASGGEVEHV--PAFKVKAVDTTGAGDTFI 253

                       250       260
                ....*....|....*....|....*
gi 31982229 262 ASVIFSLSKGNSMQEALRFGCQVAG 286
Cdd:cd01174 254 GALAAALARGLSLEEAIRFANAAAA 278
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 5-288 3.96e-09

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: 56.55  E-value: 3.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDII-NVVDKYPEEDTdrrcLSQRWQR--GGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGV 81
Cdd:cd01941   1 EIVVIGAANIDLRgKVSGSLVPGTS----NPGHVKQspGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  82 DVSQVtwQSQGDTPCSCCIVNNSNGSRTIILYDTNLPD-VSAKDFEKV--DLTRFKWIHIEGrNASEQVkmLQRI----E 154
Cdd:cd01941  77 NVRGI--VFEGRSTASYTAILDKDGDLVVALADMDIYElLTPDFLRKIreALKEAKPIVVDA-NLPEEA--LEYLlalaA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 155 EHNakqplpqkVRVSVEIEK-PR-EELFQLFSYGEVVFVSKDVAKHLgfqsAVEALRGLYSRVKKGATLVCAWAEEGADA 232
Cdd:cd01941 152 KHG--------VPVAFEPTSaPKlKKLFYLLHAIDLLTPNRAELEAL----AGALIENNEDENKAAKILLLPGIKNVIVT 219

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982229 233 LGPDGQLLHSDA-------FPPP---RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGcQVAGKK 288
Cdd:cd01941 220 LGAKGVLLSSREggvetklFPAPqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA-QAAAAL 284
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 6-268 1.03e-08

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: 54.02  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   6 ILCVGLVVLDIINVVDKYPEEDTDRRCLSQRWQRGGNASNSCTVLSLLGARCAFMGslapghvadflvadfrqrgvdvsq 85
Cdd:cd00287   2 VLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------------ 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  86 vtwqsqgdtpcsccivnnsngsrtiilydtnlpdvsakdfekvdltrFKWIHIEGRNAS--EQVKMLQRIEEHNakqplp 163
Cdd:cd00287  58 -----------------------------------------------ADAVVISGLSPApeAVLDALEEARRRG------ 84

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 164 qkVRVSVE-----IEKPREELFQLFSYGEVVFVSKDVAKHLGFQ---SAVEALRGLYSRVKKGATLVCAWAEEGADAL-G 234
Cdd:cd00287  85 --VPVVLDpgpraVRLDGEELEKLLPGVDILTPNEEEAEALTGRrdlEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVaT 162

                       250       260       270
                ....*....|....*....|....*....|....
gi 31982229 235 PDGQLLHSDAFPPpRVVDTLGAGDTFNASVIFSL 268
Cdd:cd00287 163 RGGTEVHVPAFPV-KVVDTTGAGDAFLAALAAGL 195
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 40-282 1.96e-07

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 51.72  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   40 GGNASNSCTVLSL-LGARCAFMGSLAPGHVADFLVADFRQRGVDVSQVTwQSQGDTPCSCCIVNNSnGSRTIILYDTNLP 118
Cdd:PLN02379  86 GGSVANTIRGLSAgFGVSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLR-AKKGPTAQCVCLVDAL-GNRTMRPCLSSAV 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  119 DVSAKDFEKVDLTRFKWIHIE-GRNASEQVKMLQRIeehnAKQplpQKVRVSVE------IEKPREELFQLFSYGEV--V 189
Cdd:PLN02379 164 KLQADELTKEDFKGSKWLVLRyGFYNLEVIEAAIRL----AKQ---EGLSVSLDlasfemVRNFRSPLLQLLESGKIdlC 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  190 FVSKDVAKHL---GFQSAVEALRGLYSRVkkgatlvCAWAeegADALGPDG-------QLLHSDAFPPPRVVDTLGAGDT 259
Cdd:PLN02379 237 FANEDEARELlrgEQESDPEAALEFLAKY-------CNWA---VVTLGSKGciarhgkEVVRVPAIGETNAVDATGAGDL 306

                        250       260
                 ....*....|....*....|...
gi 31982229  260 FNASVIFSLSKGNSMQEALRFGC 282
Cdd:PLN02379 307 FASGFLYGLIKGLSLEECCKVGA 329
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 18-293 5.61e-07

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 49.74  E-value: 5.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   18 NVVDKYPEEDtdrrclsqRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFLVADFRQRGVDVSQVtwqSQGDTPCS 97
Cdd:PRK09813   9 NCVDIYPQLG--------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHV---HTKHGVTA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   98 CCIVNNSNGSRTIILYDTN-LPDVSAKDFEKVDLTRFKWIH--IEGrNASEQvkmLQRIEEHNakqplpqkVRVSVEI-E 173
Cdd:PRK09813  78 QTQVELHDNDRVFGDYTEGvMADFALSEEDYAWLAQYDIVHaaIWG-HAEDA---FPQLHAAG--------KLTAFDFsD 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  174 KPREELFQ-LFSYGEVVFVSKDvakhlgfqSAVEALRG-LYSRVKKGATLVCA-WAEEGAdaLGPDGQLLHSDAFPPPRV 250
Cdd:PRK09813 146 KWDSPLWQtLVPHLDYAFASAP--------QEDEFLRLkMKAIVARGAGVVIVtLGENGS--IAWDGAQFWRQAPEPVTV 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 31982229  251 VDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCGLQG 293
Cdd:PRK09813 216 VDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 202-286 1.60e-05

ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 45.57  E-value: 1.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 202 QSAVEALRGLYSRVKKGATLVCAwAEEGADALGPDGQLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFG 281
Cdd:COG2870 221 EELVAAAAELLERLGLEALLVTR-GEEGMTLFDADGPPHHLPAQARE-VFDVTGAGDTVIATLALALAAGASLEEAAELA 298


                ....*
gi 31982229 282 CQVAG 286
Cdd:COG2870 299 NLAAG 303
PRK11142 PRK11142
ribokinase; Provisional
 233-281 2.09e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 45.25  E-value: 2.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 31982229  233 LGPDGQLLHSDAF----PPPRV--VDTLGAGDTFNASVIFSLSKGNSMQEALRFG 281
Cdd:PRK11142 222 LGSRGVWLSENGEgqrvPGFRVqaVDTIAAGDTFNGALVTALLEGKPLPEAIRFA 276
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 172-282 5.47e-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: 5.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 172 IEKPREELFQLFSYGEVVFVSKDVAKHL-GFQSAVEALRGLYSRVKKgaTLVCAWAEEGAdALGPDGQLLHSDAFPPPRV 250
Cdd:cd01946 150 ISIKPEKLKKVLAKVDVVIINDGEARQLtGAANLVKAARLILAMGPK--ALIIKRGEYGA-LLFTDDGYFAAPAYPLESV 226

                        90       100       110
                ....*....|....*....|....*....|...
gi 31982229 251 VDTLGAGDTFNASVIFSL-SKGNSMQEALRFGC 282
Cdd:cd01946 227 FDPTGAGDTFAGGFIGYLaSQKDTSEANMRRAI 259
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 227-290 6.52e-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: 43.70  E-value: 6.52e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982229 227 EEGADALGPDGQLLHSDAFPPPrVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKKCG 290
Cdd:cd01172 228 EEGMTLFERDGEVQHIPALAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVG 290
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 5-288 1.09e-04

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: 42.77  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229   5 QILCVGLVVLDIINVVDkypeedtdrrclSQRWQRGGNASNSCTVLSLLGARCAFMGSLAPGHVADFlvADFRQRGVDVs 84
Cdd:cd01937   1 KIVIIGHVTIDEIVTNG------------SGVVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKW--SDLFDNGIEV- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  85 qvtwqsqgdtpcsccIVNNSNGSRTIILYDTNLPDVsakdfekvdltrfKWIHIEGRNASEQVKMLQRIE-EHNAKQPLP 163
Cdd:cd01937  66 ---------------ISLLSTETTTFELNYTNEGRT-------------RTLLAKCAAIPDTESPLSTITaEIVILGPVP 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229 164 QKV-RVSVEIEKP---------------REELFQLFSYGEVVFVSKDVAKHLgfQSAVEALRGLysRVKKGATLVCAWAE 227
Cdd:cd01937 118 EEIsPSLFRKFAFisldaqgflrranqeKLIKCVILKLHDVLKLSRVEAEVI--STPTELARLI--KETGVKEIIVTDGE 193

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982229 228 EGA---DALGPDgqllhsdAFPPPR--VVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVAGKK 288
Cdd:cd01937 194 EGGyifDGNGKY-------TIPASKkdVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKF 252
fruK PRK09513
1-phosphofructokinase; Provisional
 219-285 1.97e-03

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 39.29  E-value: 1.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982229  219 ATLVCAWAEEGADALGPDGQLLhsdAFPPP-RVVDTLGAGDTFNASVIFSLSKGNSMQEALRFGCQVA 285
Cdd:PRK09513 218 AHVVISLGAEGALWVNASGEWI---AKPPAcDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVS 282
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 202-276 3.01e-03

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 38.76  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982229  202 QSAVEALRGLYSR----VKKGATLVCAWAEegadalgpdGQLLHsdaFPPPRV--VDTLGAGDTFNASVIFSLSKGNSMQ 275
Cdd:PRK09434 201 EDAIYALADRYPIalllVTLGAEGVLVHTR---------GQVQH---FPAPSVdpVDTTGAGDAFVAGLLAGLSQAGLWT 268


                 .
gi 31982229  276 E 276
Cdd:PRK09434 269 D 269
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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