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Conserved domains on  [gi|768021790|ref|XP_011528062|]
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pyridoxal kinase isoform X4 [Homo sapiens]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 399)

carbohydrate kinase family protein that accepts a wide variety of substrates, including carbohydrates and aromatic small molecules, all being phosphorylated at a hydroxyl group; belongs to the ribokinase/pfkB sugar kinase superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
1-231 3.25e-100

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).


The actual alignment was detected with superfamily member TIGR00687:

Pssm-ID: 444735 [Multi-domain]  Cd Length: 287  Bit Score: 292.89  E-value: 3.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790    1 MNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:TIGR00687  72 LNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF--- 157
Cdd:TIGR00687 149 LELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpp 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021790  158 -VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 231
Cdd:TIGR00687 218 pVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
 
Name Accession Description Interval E-value
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
1-231 3.25e-100

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 292.89  E-value: 3.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790    1 MNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:TIGR00687  72 LNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF--- 157
Cdd:TIGR00687 149 LELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpp 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021790  158 -VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 231
Cdd:TIGR00687 218 pVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
3-237 1.07e-88

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 264.29  E-value: 1.07e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   3 KYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE 82
Cdd:PLN02978  86 FYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAE 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  83 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPspqgsNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGD 162
Cdd:PLN02978 162 QLTGIRIVTEEDAREACAILHAAGPSKVVITSIDID-----GKLLLVGSHRKEKGARP---EQFKIVIPKIPAYFTGTGD 233
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021790 163 LFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAqagEGVRPSPMQLELRMVQSKRDIEDPEIVVQAT 237
Cdd:PLN02978 234 LMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
2-199 8.74e-71

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 217.07  E-value: 8.74e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   2 NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYV-PEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:cd01173   71 LEYDAVLTGYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGKLYVvAEEIVPVYRDLLVPLADIITPNQFE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgsqRRRNPAGSVVMERIRMDIRKVD--AVFV 158
Cdd:cd01173  147 LELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADD------------DRIEMLGSTATEAWLVQRPKIPfpAYFN 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 768021790 159 GTGDLFAAMLLAWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 199
Cdd:cd01173  215 GTGDLFAALLLARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism];
3-201 4.08e-46

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism];


Pssm-ID: 225149 [Multi-domain]  Cd Length: 281  Bit Score: 154.74  E-value: 4.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   3 KYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE 82
Cdd:COG2240   73 ECDAVLTGYLGSAEQVRAIAGIVKAVKEANPNALYLCDPVMGD----PGGLYVAPEVAEAYRDELLPLADIITPNIFELE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  83 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDlpspqgsnylivlgsqRRRNPAGSVVMERIRMD-----IRKVDAVF 157
Cdd:COG2240  149 ILTGKPLNTLDDAVKAARKLGADGPKIVLVTSLS----------------RAGMSTGNFEMLGKSAElawhiSPLVPFIP 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768021790 158 VGTGDLFAAMLLAWTHKHPnNLKVACEKTVSTLHHVLQRTIQCA 201
Cdd:COG2240  213 NGTGDLFSALLLARLLEGL-SLTQALERATAAVYEVLQETQKLG 255
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
24-122 5.04e-17

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 77.14  E-value: 5.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   24 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 103
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152
                          90
                  ....*....|....*....
gi 768021790  104 SMGPDTVVITSSDLPSPQG 122
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEA 171
 
Name Accession Description Interval E-value
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
1-231 3.25e-100

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 292.89  E-value: 3.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790    1 MNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:TIGR00687  72 LNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF--- 157
Cdd:TIGR00687 149 LELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpp 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021790  158 -VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 231
Cdd:TIGR00687 218 pVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
3-237 1.07e-88

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 264.29  E-value: 1.07e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   3 KYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE 82
Cdd:PLN02978  86 FYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAE 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  83 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPspqgsNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGD 162
Cdd:PLN02978 162 QLTGIRIVTEEDAREACAILHAAGPSKVVITSIDID-----GKLLLVGSHRKEKGARP---EQFKIVIPKIPAYFTGTGD 233
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021790 163 LFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAqagEGVRPSPMQLELRMVQSKRDIEDPEIVVQAT 237
Cdd:PLN02978 234 LMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
2-239 2.20e-76

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 232.66  E-value: 2.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   2 NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEkVVPLADIITPNQFEA 81
Cdd:PTZ00344  76 SDYTYVLTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGD----DGKLYVKEEVVDAYRE-LIPYADVITPNQFEA 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  82 ELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLpsPQGSNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTG 161
Cdd:PTZ00344 151 SLLSGVEVKDLSDALEAIDWFHEQGIPVVVITSFRE--DEDPTHLRFLLSCRDKDTKNN---KRFTGKVPYIEGRYTGTG 225
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021790 162 DLFAAMLLAWTHKHPnnLKVACEKTVSTLHHVLQRTIqcakaQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL 239
Cdd:PTZ00344 226 DLFAALLLAFSHQHP--MDLAVGKAMGVLQDIIKATR-----ESGGSGSSSLMSRELRLIQSPRDLLNPETVFKVTPL 296
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
2-199 8.74e-71

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 217.07  E-value: 8.74e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   2 NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYV-PEDLLPVYKEKVVPLADIITPNQFE 80
Cdd:cd01173   71 LEYDAVLTGYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGKLYVvAEEIVPVYRDLLVPLADIITPNQFE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  81 AELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgsqRRRNPAGSVVMERIRMDIRKVD--AVFV 158
Cdd:cd01173  147 LELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADD------------DRIEMLGSTATEAWLVQRPKIPfpAYFN 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 768021790 159 GTGDLFAAMLLAWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 199
Cdd:cd01173  215 GTGDLFAALLLARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism];
3-201 4.08e-46

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism];


Pssm-ID: 225149 [Multi-domain]  Cd Length: 281  Bit Score: 154.74  E-value: 4.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   3 KYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE 82
Cdd:COG2240   73 ECDAVLTGYLGSAEQVRAIAGIVKAVKEANPNALYLCDPVMGD----PGGLYVAPEVAEAYRDELLPLADIITPNIFELE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  83 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDlpspqgsnylivlgsqRRRNPAGSVVMERIRMD-----IRKVDAVF 157
Cdd:COG2240  149 ILTGKPLNTLDDAVKAARKLGADGPKIVLVTSLS----------------RAGMSTGNFEMLGKSAElawhiSPLVPFIP 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768021790 158 VGTGDLFAAMLLAWTHKHPnNLKVACEKTVSTLHHVLQRTIQCA 201
Cdd:COG2240  213 NGTGDLFSALLLARLLEGL-SLTQALERATAAVYEVLQETQKLG 255
PRK05756 PRK05756
pyridoxal kinase PdxY;
5-239 1.44e-40

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 140.39  E-value: 1.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELL 84
Cdd:PRK05756  76 DAVLSGYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDP---EKGCIVAPGVAEFLRDRALPAADIITPNLFELEWL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  85 SGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLP-SPQGSNYLIVLgsqrrrNPAGSVVMERIRMDIRKVDavfVGTGDL 163
Cdd:PRK05756 153 SGRPVETLEDAVAAARALIARGPKIVLVTSLARAgYPADRFEMLLV------TADGAWHISRPLVDFMRQP---VGVGDL 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021790 164 FAAMLLAWtHKHPNNLKVACEKTVSTLHHVLQRTIQCakaqageGVRpspmqlELRMVQSKRDIEDPEIVVQATVL 239
Cdd:PRK05756 224 TSALFLAR-LLQGGSLEEALEHTTAAVYEVMARTKER-------GSY------ELQLVAAQDSIATPRAMFQARRL 285
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
7-200 6.95e-24

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 96.65  E-value: 6.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   7 VLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSG 86
Cdd:PRK08176  92 VTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSG---IYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTG 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  87 RKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGS-NYLIVLGSQRrrnpagsVVMERIRmdirkVDAVFVGTGDLFA 165
Cdd:PRK08176 169 KPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEmQVVVVTADSV-------NVISHPR-----VDTDLKGTGDLFC 236
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 768021790 166 AMLLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQC 200
Cdd:PRK08176 237 AELVSgLLKGKA--LTDAAHRAGLRVLEVMRYTQQA 270
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
4-171 1.57e-19

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: 82.91  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   4 YDYVLTGYTRDKsfLAMVVDIVQELKQQNPRlvYVCDPVLGDK-WDGEGsmyvpedllpvyKEKVVPLADIITPNQFEAE 82
Cdd:cd00287   58 ADAVVISGLSPA--PEAVLDALEEARRRGVP--VVLDPGPRAVrLDGEE------------LEKLLPGVDILTPNEEEAE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  83 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspQGSNYLIVLGSQRRRNPAGSVvmerirmdirKVDAV-FVGTG 161
Cdd:cd00287  122 ALTGRRDLEVKEAAEAAALLLSKGPKVVIVT-------LGEKGAIVATRGGTEVHVPAF----------PVKVVdTTGAG 184
                        170
                 ....*....|
gi 768021790 162 DLFAAMLLAW 171
Cdd:cd00287  185 DAFLAALAAG 194
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism];
21-113 1.89e-17

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism];


Pssm-ID: 223428 [Multi-domain]  Cd Length: 263  Bit Score: 78.78  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  21 VVDIVQELKQQNPRLVYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGR-KIHSQEEALRVM 99
Cdd:COG0351   86 IIEVVAEKLKKYGIGPVVLDPVMVAK---SGDPLLDEEAVEALREELLPLATVVTPNLPEAEALSGLpKIKTEEDMKEAA 162
                         90
                 ....*....|....
gi 768021790 100 DMLHSMGPDTVVIT 113
Cdd:COG0351  163 KLLHELGAKAVLIK 176
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
24-122 5.04e-17

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 77.14  E-value: 5.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   24 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 103
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152
                          90
                  ....*....|....*....
gi 768021790  104 SMGPDTVVITSSDLPSPQG 122
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEA 171
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
21-170 7.15e-14

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 69.00  E-value: 7.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  21 VVDIVQELKQQNPRLVYVCDPVL----GDkwdgegsmyvP---EDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQE 93
Cdd:PRK06427  87 IIETVAEALKRYPIPPVVLDPVMiaksGD----------PllaDDAVAALRERLLPLATLITPNLPEAEALTGLPIADTE 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021790  94 EALRVM-DMLHSMGPDTVVITSS-DLPSPQGSNYLIvlgsqrrrNPAGSVVMERIRMDIRKVDavfvGTGDLFAAMLLA 170
Cdd:PRK06427 157 DEMKAAaRALHALGCKAVLIKGGhLLDGEESVDWLF--------DGEGEERFSAPRIPTKNTH----GTGCTLSAAIAA 223
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
22-171 2.18e-11

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 61.98  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   22 VDIVQELKQQNPRLVYVCDPVLGDKWDgegsmyvpedLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDM 101
Cdd:pfam00294 143 EATLEELIEAAKNGGTFDPNLLDPLGA----------AREALLE-LLPLADLLKPNEEELEALTGAKLDDIEEALAALHK 211
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768021790  102 LHSMGPDTVVITSsdlpSPQGSnyLIVLGSQRRRNPAgsvvmerirmdIRKVDAV-FVGTGDLFAAMLLAW 171
Cdd:pfam00294 212 LLAKGIKTVIVTL----GADGA--LVVEGDGEVHVPA-----------VPKVKVVdTTGAGDSFVGGFLAG 265
PRK07105 PRK07105
pyridoxamine kinase; Validated
3-197 6.83e-11

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 60.70  E-value: 6.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   3 KYDYVLTGY---TRDksflamvVDIVQELKQ--QNPRLVYVCDPVLGDKwdgeGSMYVP--EDLLPVYKeKVVPLADIIT 75
Cdd:PRK07105  75 KFDAIYSGYlgsPRQ-------IQIVSDFIKyfKKKDLLVVVDPVMGDN----GKLYQGfdQEMVEEMR-KLIQKADVIT 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  76 PNQFEAELLSG---RKIHSQEEalRVMDMLH---SMGPDTVVITSSdlpsPQGSNYLIVLGSQRRRNpagsvvmERIRMD 149
Cdd:PRK07105 143 PNLTEACLLLDkpyLEKSYSEE--EIKQLLRklaDLGPKIVIITSV----PFEDGKIGVAYYDRATD-------RFWKVF 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768021790 150 IRKVDAVFVGTGDLFAAMLLAWTHkHPNNLKVACEKTVSTLHHVLQRT 197
Cdd:PRK07105 210 CKYIPAHYPGTGDIFTSVITGSLL-QGDSLPIALDRAVQFIEKGIRAT 256
PRK11142 PRK11142
ribokinase; Provisional
70-113 7.10e-11

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 60.65  E-value: 7.10e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 768021790  70 LADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVIT 113
Cdd:PRK11142 178 LVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLIT 221
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
65-170 9.16e-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: 60.26  E-value: 9.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  65 EKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM- 143
Cdd:cd01174  170 AELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT---------------LGAK------GALLAs 228
                         90       100       110
                 ....*....|....*....|....*....|
gi 768021790 144 --ERIRMDIRKVDAV-FVGTGDLFAAMLLA 170
Cdd:cd01174  229 ggEVEHVPAFKVKAVdTTGAGDTFIGALAA 258
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
38-133 1.56e-09

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 57.43  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  38 VCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH-SMGPDTVVITSSD 116
Cdd:PRK08573 101 VVDPVMIAK---SGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVeELGAEAVVVKGGH 177
                         90
                 ....*....|....*..
gi 768021790 117 LPSPQGSNYLIVLGSQR 133
Cdd:PRK08573 178 LEGEEAVDVLYHNGTFR 194
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism];
54-170 5.22e-08

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


Pssm-ID: 223598 [Multi-domain]  Cd Length: 311  Bit Score: 52.50  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  54 YVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRkihsQEEALRVMDMLHSMGPDTVVITssdlPSPQGSnyLIVLGSQR 133
Cdd:COG0524  167 PRPALWDRELLEELLALADILFPNEEEAELLTGL----EEDAEAAAALLLAKGVKTVVVT----LGAEGA--VVFTGGGE 236
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 768021790 134 RRNPagsvvmeriRMDIRKVDAV-FVGTGDLFAAMLLA 170
Cdd:COG0524  237 VTVP---------VPAAFKVKVVdTTGAGDAFAAGFLA 265
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
66-112 5.78e-08

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 51.99  E-value: 5.78e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 768021790  66 KVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVI 112
Cdd:PRK12413 125 QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVI 171
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
5-119 1.77e-07

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 51.31  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE-L 83
Cdd:PLN02898  80 DVVKTGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMVST---SGDVLAGPSILSALREELLPLATIVTPNVKEASaL 152
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 768021790  84 LSGRKIHSqeealrVMDM------LHSMGPDTVVITSSDLPS 119
Cdd:PLN02898 153 LGGDPLET------VADMrsaakeLHKLGPRYVLVKGGHLPD 188
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-113 9.92e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 48.50  E-value: 9.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEGSMYVPEDLlPVYKEKVVPLADIITPNQFEAELL 84
Cdd:PRK12616  76 DAMKTGMLPTVDIIELAADTIKEKQLKN----VVIDPVMVCK--GANEVLYPEHA-EALREQLAPLATVITPNLFEAGQL 148
                         90       100       110
                 ....*....|....*....|....*....|
gi 768021790  85 SGR-KIHSQEEALRVMDMLHSMGPDTVVIT 113
Cdd:PRK12616 149 SGMgEIKTVEQMKEAAKKIHELGAQYVVIT 178
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-112 2.14e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 47.27  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790   5 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEGSMYVPEDLLpVYKEKVVPLADIITPNQFEAELL 84
Cdd:PRK12412  74 DALKTGMLGSVEIIEMVAETIEKHNFKN----VVVDPVMVCK--GADEALHPETND-CLRDVLVPKALVVTPNLFEAYQL 146
                         90       100
                 ....*....|....*....|....*...
gi 768021790  85 SGRKIHSQEEALRVMDMLHSMGPDTVVI 112
Cdd:PRK12412 147 SGVKINSLEDMKEAAKKIHALGAKYVLI 174
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
24-208 4.50e-06

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 46.88  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  24 IVQELKQqnprLVYVCDPVL----GDKWDGEGSMyvpEDLLPVYKEKVVPLADIITPNQFEAELLSGRK-IHSQEEALRV 98
Cdd:PTZ00347 317 VIEKLKN----LPMVVDPVLvatsGDDLVAQKNA---DDVLAMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAA 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  99 MDMLhsmgpdtvvitssdlpSPQGSNYLIVLGSQRRRNP--AGSVVMERIRMDIRKVDAVFV------GTGDLFAAMLLA 170
Cdd:PTZ00347 390 AQAL----------------AQYGSRYVLVKGGHDLIDPeaCRDVLYDREKDRFYEFTANRIatinthGTGCTLASAISS 453
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 768021790 171 WTHKHpNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEG 208
Cdd:PTZ00347 454 FLARG-YTVPDAVERAIGYVHEAIVRSCGVPLGQGTNR 490
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
63-176 3.38e-04

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: 41.06  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  63 YKE---KVVPLADIITPNQFEAELLSGRKI-HSQEEALRVMdmlhSMGPDTVVITssdlpspQGSNYLIVLgSQRRRNPA 138
Cdd:cd01168  190 FKEallELLPYVDILFGNEEEAEALAEAETtDDLEAALKLL----ALRCRIVVIT-------QGAKGAVVV-EGGEVYPV 257
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 768021790 139 GSVVMERIrmdirkVDAvfVGTGDLFAA-MLLAWTHKHP 176
Cdd:cd01168  258 PAIPVEKI------VDT--NGAGDAFAGgFLYGLVQGEP 288
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
56-170 1.06e-03

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: 39.48  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  56 PEDLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQ-EEALRvmdmLHSMGPDTVVItssdlpspqgsnylivlgsqrR 134
Cdd:cd01166  172 AEEAREALEE-LLPYVDIVLPSEEEAEALLGDEDPTDaAERAL----ALALGVKAVVV---------------------K 225
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 768021790 135 RNPAGSVVM---ERIRMDIRKVDAV-FVGTGDLFAAMLLA 170
Cdd:cd01166  226 LGAEGALVYtggGRVFVPAYPVEVVdTTGAGDAFAAGFLA 265
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
22-182 7.09e-03

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: 36.74  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790  22 VDIVQELKQQNPRLVyvCDPvlgdkwDGEGsmyvpedLLPVYKEKVvplaDIITPNQFEAELLSGRKIHSQEEALRVMDM 101
Cdd:cd01164  148 AELVRLAREKGARVI--LDT------SGEA-------LLAALAAKP----FLIKPNREELEELFGRPLGDEEDVIAAARK 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021790 102 LHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVMER---IRMDIRKVDAV-FVGTGD-LFAAMLLAWTHKHP 176
Cdd:cd01164  209 LIERGAENVLVS---------------LGAD------GALLVTKdgvYRASPPKVKVVsTVGAGDsMVAGFVAGLAQGLS 267

                 ....*...
gi 768021790 177 --NNLKVA 182
Cdd:cd01164  268 leEALRLA 275
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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