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Conserved domains on  [gi|6320806|ref|NP_010885|]
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putative pyridoxal kinase BUD16 [Saccharomyces cerevisiae S288C]

Protein Classification

pyridoxal kinase( domain architecture ID 10100273)

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

CATH:  3.40.1190.20
EC:  2.7.1.35
Gene Ontology:  GO:0005524|GO:0016310|GO:0008478|GO:0008270|GO:0030170
PubMed:  14722069|2162645|10024608|8382990
SCOP:  3001268

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 3-266 2.33e-106

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: 310.29  E-value: 2.33e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    3 RLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGldKVFGTITRETDLKELLSGLFDN-FSQDYQALLS 81
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYG--TWTGFVLSAEELEDLLEGLEALgLLLEYDAVLT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   82 GYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLYV-SEDVIPEYRKLALSpkqLVDIITPNQFELEILYGGEI 160
Cdd:cd01173  79 GYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVP---LADIITPNQFELELLTGKKI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806  161 KTKEHLKKALKKLHQT-IPVIIVTSCDckmFDDKDFIYCVASMeGKTPIVYRVPFID--SYFTGVGDLFSALLLDRVYKI 237
Cdd:cd01173 156 NDLEDAKAAARALHAKgPKTVVVTSVE---LADDDRIEMLGST-ATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLLKG 231

                       250       260
                ....*....|....*....|....*....
gi 6320806  238 LSnptttlkFEDQVNNVLNVIQKVLKITR 266
Cdd:cd01173 232 KS-------LAEALEKALNFVHEVLEATY 253
 
Name Accession Description Interval E-value
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 3-266 2.33e-106

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: 310.29  E-value: 2.33e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    3 RLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGldKVFGTITRETDLKELLSGLFDN-FSQDYQALLS 81
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYG--TWTGFVLSAEELEDLLEGLEALgLLLEYDAVLT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   82 GYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLYV-SEDVIPEYRKLALSpkqLVDIITPNQFELEILYGGEI 160
Cdd:cd01173  79 GYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVP---LADIITPNQFELELLTGKKI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806  161 KTKEHLKKALKKLHQT-IPVIIVTSCDckmFDDKDFIYCVASMeGKTPIVYRVPFID--SYFTGVGDLFSALLLDRVYKI 237
Cdd:cd01173 156 NDLEDAKAAARALHAKgPKTVVVTSVE---LADDDRIEMLGST-ATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLLKG 231

                       250       260
                ....*....|....*....|....*....
gi 6320806  238 LSnptttlkFEDQVNNVLNVIQKVLKITR 266
Cdd:cd01173 232 KS-------LAEALEKALNFVHEVLEATY 253
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 2-299 3.93e-79

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 242.68  E-value: 3.93e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806     2 PRLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGldKVFGTITRETDLKELLSGLFDN-FSQDYQALL 80
Cdd:PTZ00344   5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYP--VIKGHRLDLNELITLMDGLRANnLLSDYTYVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    81 SGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLYVSEDVIPEYRKLAlspkQLVDIITPNQFELEILYGGEI 160
Cdd:PTZ00344  83 TGYINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAYRELI----PYADVITPNQFEASLLSGVEV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   161 KTKEHLKKALKKLH-QTIPVIIVTScdCKMFDDKD---FIYCVASMEGKTPIVYR--VPFIDSYFTGVGDLFSALLLDRv 234
Cdd:PTZ00344 159 KDLSDALEAIDWFHeQGIPVVVITS--FREDEDPThlrFLLSCRDKDTKNNKRFTgkVPYIEGRYTGTGDLFAALLLAF- 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320806   235 ykilsnpTTTLKFEDQVNNVLNVIQKVLKITRSYasgkmkAKMGSALEMKEmELRLIESRDIYET 299
Cdd:PTZ00344 236 -------SHQHPMDLAVGKAMGVLQDIIKATRES------GGSGSSSLMSR-ELRLIQSPRDLLN 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-231 3.08e-62

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 198.45  E-value: 3.08e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    1 MPRLLATQSHVVHGYVGNKAATFPLQCLGwdVDCC--NSVQFSNHTGYGldKVFGTITRETDLKELLSGLFD-NFSQDYQ 77
Cdd:COG2240   1 MKRVLSIQSHVVYGHVGNSAAVPPLSALG--VEVWplPTVLLSNHTGYG--TFTGRDLPTDDIADILDGWKElGVLLEFD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   78 ALLSGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLY-VSEDVIPEYRKLALspkQLVDIITPNQFELEILY 156
Cdd:COG2240  77 AVLSGYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLV---PLADIITPNLTELALLT 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320806  157 GGEIKTKEHLKKALKKLHQTIP-VIIVTSCDCkMFDDKDFIYCVASMEGKTPIVYRvPFIDSYFTGVGDLFSALLL 231
Cdd:COG2240 154 GRPYETLEEALAAARALLALGPkIVVVTSVPL-DDTPADKIGNLAVTADGAWLVET-PLLPFSPNGTGDLFAALLL 227
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 1-274 1.17e-51

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: 171.94  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806      1 MPRLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGldKVFGTITRETDLKELLSGL--FDNFSQdYQA 78
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYG--KWTGQVLPPDELHELVEGLeaINKLNQ-CDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806     79 LLSGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQ-LYVSEDVIPEYRKLALSpkqLVDIITPNQFELEILYG 157
Cdd:TIGR00687  78 VLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKgCYVAPDLLEVYREKAIP---VADIITPNQFELELLTG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    158 GEIKTKEHLKKALKKLHQTIPVIIVTS--CDCKMFDDKDFIYCVASMEGKTPIvyRVPFIDSYF--TGVGDLFSALLLDR 233
Cdd:TIGR00687 155 RRINTEEEALAAADALIAMGPDIVLVThlIRAGSQRDRSFEGLVATQEGRWHI--SRPLAVFDPppVGTGDLIAALLLAT 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 6320806    234 vykiLSNPTTtlkFEDQVNNVLNVIQKVLKITRSYASGKMK 274
Cdd:TIGR00687 233 ----LLHGNS---LKEALEKTVSAVYHVLRTTIQLGKYELQ 266
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 112-228 8.88e-10

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: 57.88  E-value: 8.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    112 DPVM--GDEGQLyVSEDVIPEYRKLALSpkqLVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQT-IPVIIVTSCDCK 188
Cdd:pfam08543  92 DPVMvaKSGDSL-LDDEAIEALKEELLP---LATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALgAKAVLIKGGHLE 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6320806    189 MFDD--KDFIYcvasmEGKTPIVYRVPFIDSYFT-GVGDLFSA 228
Cdd:pfam08543 168 GEEAvvTDVLY-----DGGGFYTLEAPRIPTKNThGTGCTLSA 205
 
Name Accession Description Interval E-value
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 3-266 2.33e-106

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: 310.29  E-value: 2.33e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    3 RLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGldKVFGTITRETDLKELLSGLFDN-FSQDYQALLS 81
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYG--TWTGFVLSAEELEDLLEGLEALgLLLEYDAVLT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   82 GYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLYV-SEDVIPEYRKLALSpkqLVDIITPNQFELEILYGGEI 160
Cdd:cd01173  79 GYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVP---LADIITPNQFELELLTGKKI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806  161 KTKEHLKKALKKLHQT-IPVIIVTSCDckmFDDKDFIYCVASMeGKTPIVYRVPFID--SYFTGVGDLFSALLLDRVYKI 237
Cdd:cd01173 156 NDLEDAKAAARALHAKgPKTVVVTSVE---LADDDRIEMLGST-ATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLLKG 231

                       250       260
                ....*....|....*....|....*....
gi 6320806  238 LSnptttlkFEDQVNNVLNVIQKVLKITR 266
Cdd:cd01173 232 KS-------LAEALEKALNFVHEVLEATY 253
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 2-299 3.93e-79

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 242.68  E-value: 3.93e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806     2 PRLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGldKVFGTITRETDLKELLSGLFDN-FSQDYQALL 80
Cdd:PTZ00344   5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYP--VIKGHRLDLNELITLMDGLRANnLLSDYTYVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    81 SGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLYVSEDVIPEYRKLAlspkQLVDIITPNQFELEILYGGEI 160
Cdd:PTZ00344  83 TGYINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAYRELI----PYADVITPNQFEASLLSGVEV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   161 KTKEHLKKALKKLH-QTIPVIIVTScdCKMFDDKD---FIYCVASMEGKTPIVYR--VPFIDSYFTGVGDLFSALLLDRv 234
Cdd:PTZ00344 159 KDLSDALEAIDWFHeQGIPVVVITS--FREDEDPThlrFLLSCRDKDTKNNKRFTgkVPYIEGRYTGTGDLFAALLLAF- 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320806   235 ykilsnpTTTLKFEDQVNNVLNVIQKVLKITRSYasgkmkAKMGSALEMKEmELRLIESRDIYET 299
Cdd:PTZ00344 236 -------SHQHPMDLAVGKAMGVLQDIIKATRES------GGSGSSSLMSR-ELRLIQSPRDLLN 286
PLN02978 PLN02978
pyridoxal kinase
 2-295 8.02e-67

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 211.52  E-value: 8.02e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806     2 PRLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGLDKvfGTITRETDLKELLSGLFDNFSQDYQALLS 81
Cdd:PLN02978  15 GRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFK--GQVLDGEQLWALIEGLEANGLLFYTHLLT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    82 GYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLYVSEDVIPEYRKLALSpkqLVDIITPNQFELEILYGGEIK 161
Cdd:PLN02978  93 GYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVP---LATMLTPNQFEAEQLTGIRIV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   162 TKEHLKKALKKLHQTIP-VIIVTSCDckmFDDKdfIYCVASM---EGKTPIVY--RVPFIDSYFTGVGDLFSALLLDRVY 235
Cdd:PLN02978 170 TEEDAREACAILHAAGPsKVVITSID---IDGK--LLLVGSHrkeKGARPEQFkiVIPKIPAYFTGTGDLMAALLLGWSH 244

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320806   236 KILSNptttlkFEDQVNNVLNVIQKVLKIT-RSYASGKMKAKMGSAlemkemELRLIESRD 295
Cdd:PLN02978 245 KYPDN------LDKAAELAVSSLQAVLRRTlADYKRAGADPKSSSL------ELRLVQSQD 293
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-231 3.08e-62

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 198.45  E-value: 3.08e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    1 MPRLLATQSHVVHGYVGNKAATFPLQCLGwdVDCC--NSVQFSNHTGYGldKVFGTITRETDLKELLSGLFD-NFSQDYQ 77
Cdd:COG2240   1 MKRVLSIQSHVVYGHVGNSAAVPPLSALG--VEVWplPTVLLSNHTGYG--TFTGRDLPTDDIADILDGWKElGVLLEFD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   78 ALLSGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLY-VSEDVIPEYRKLALspkQLVDIITPNQFELEILY 156
Cdd:COG2240  77 AVLSGYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLV---PLADIITPNLTELALLT 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320806  157 GGEIKTKEHLKKALKKLHQTIP-VIIVTSCDCkMFDDKDFIYCVASMEGKTPIVYRvPFIDSYFTGVGDLFSALLL 231
Cdd:COG2240 154 GRPYETLEEALAAARALLALGPkIVVVTSVPL-DDTPADKIGNLAVTADGAWLVET-PLLPFSPNGTGDLFAALLL 227
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 1-274 1.17e-51

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: 171.94  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806      1 MPRLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGldKVFGTITRETDLKELLSGL--FDNFSQdYQA 78
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYG--KWTGQVLPPDELHELVEGLeaINKLNQ-CDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806     79 LLSGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQ-LYVSEDVIPEYRKLALSpkqLVDIITPNQFELEILYG 157
Cdd:TIGR00687  78 VLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKgCYVAPDLLEVYREKAIP---VADIITPNQFELELLTG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    158 GEIKTKEHLKKALKKLHQTIPVIIVTS--CDCKMFDDKDFIYCVASMEGKTPIvyRVPFIDSYF--TGVGDLFSALLLDR 233
Cdd:TIGR00687 155 RRINTEEEALAAADALIAMGPDIVLVThlIRAGSQRDRSFEGLVATQEGRWHI--SRPLAVFDPppVGTGDLIAALLLAT 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 6320806    234 vykiLSNPTTtlkFEDQVNNVLNVIQKVLKITRSYASGKMK 274
Cdd:TIGR00687 233 ----LLHGNS---LKEALEKTVSAVYHVLRTTIQLGKYELQ 266
PRK05756 PRK05756
pyridoxal kinase PdxY;
1-295 1.15e-49

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 166.58  E-value: 1.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806     1 MPRLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGldKVFGTITRETDLKELLSGLFD-NFSQDYQAL 79
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYG--KWTGCVMPPSHLTEIVQGIADiGWLGECDAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    80 LSGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQ-LYVSEDViPEY-RKLALSpkqLVDIITPNQFELEILYG 157
Cdd:PRK05756  79 LSGYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKgCIVAPGV-AEFlRDRALP---AADIITPNLFELEWLSG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   158 GEIKTKEHLKKALKKLHQTIP-VIIVTSCDCKMFDDKDFIYCVASMEG----KTPivyRVPFIDSYfTGVGDLFSALLLD 232
Cdd:PRK05756 155 RPVETLEDAVAAARALIARGPkIVLVTSLARAGYPADRFEMLLVTADGawhiSRP---LVDFMRQP-VGVGDLTSALFLA 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320806   233 RVYKILSNPTTtlkFEDQVNNVLNVIQKvlkitrsyasgkmkakmgsALEMKEMELRLIESRD 295
Cdd:PRK05756 231 RLLQGGSLEEA---LEHTTAAVYEVMAR-------------------TKERGSYELQLVAAQD 271
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
6-230 1.98e-22

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 94.34  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806     6 ATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSN--H--TGYGldkvfGTITRE------TDLKE--LLSGLfdnfs 73
Cdd:PRK08176  20 AVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNtpHypTFYG-----GAIPDEwfsgylRALQErdALRQL----- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    74 qdyQALLSGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQ-LYVSEDVIPEYRKLALSpkqLVDIITPNQFEL 152
Cdd:PRK08176  90 ---RAVTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSgIYVKPDLPEAYRQHLLP---LAQGLTPNIFEL 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320806   153 EILYGGEIKTKEHLKKALKK-LHQTIPVIIVTSCDCKmfDDKDFIYCVASMEGKTpIVYRVPFIDSYFTGVGDLFSALL 230
Cdd:PRK08176 164 EILTGKPCRTLDSAIAAAKSlLSDTLKWVVITSAAGN--EENQEMQVVVVTADSV-NVISHPRVDTDLKGTGDLFCAEL 239
PRK07105 PRK07105
pyridoxamine kinase; Validated
 41-268 8.44e-15

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 73.03  E-value: 8.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    41 SNHTGYGLDKVFgtitreTDLKELLSGLFDNFSQ---DYQALLSGYLPNKNSVRCMGTYYAKFKEanPEMIWLMDPVMGD 117
Cdd:PRK07105  44 SSHTGGFQNPSI------IDLTDGMQAFLTHWKSlnlKFDAIYSGYLGSPRQIQIVSDFIKYFKK--KDLLVVVDPVMGD 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   118 EGQLY--VSEDVIPEYRKLAlspkQLVDIITPNQFELEIL----YGGEIKTKEHLKKALKKLHQTIP-VIIVTScdckmf 190
Cdd:PRK07105 116 NGKLYqgFDQEMVEEMRKLI----QKADVITPNLTEACLLldkpYLEKSYSEEEIKQLLRKLADLGPkIVIITS------ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   191 ddkdfiycVASMEGKTPIVY------RV-----PFIDSYFTGVGDLFSALLLDRVYKILSnptttlkFEDQVNNVLNVIQ 259
Cdd:PRK07105 186 --------VPFEDGKIGVAYydratdRFwkvfcKYIPAHYPGTGDIFTSVITGSLLQGDS-------LPIALDRAVQFIE 250


                 ....*....
gi 6320806   260 KVLKITRSY 268
Cdd:PRK07105 251 KGIRATLGL 259
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 112-228 8.88e-10

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: 57.88  E-value: 8.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    112 DPVM--GDEGQLyVSEDVIPEYRKLALSpkqLVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQT-IPVIIVTSCDCK 188
Cdd:pfam08543  92 DPVMvaKSGDSL-LDDEAIEALKEELLP---LATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALgAKAVLIKGGHLE 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6320806    189 MFDD--KDFIYcvasmEGKTPIVYRVPFIDSYFT-GVGDLFSA 228
Cdd:pfam08543 168 GEEAvvTDVLY-----DGGGFYTLEAPRIPTKNThGTGCTLSA 205
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
65-228 4.04e-08

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 53.51  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    65 LSGLFDNFSQDyqALLSGYLPNKNSVRCMGTYYAKFKEANPemiwLMDPVMGDEGqlyVSEDVIPEYRKL---ALSPkqL 141
Cdd:PRK12616  66 LSTIVDGIGVD--AMKTGMLPTVDIIELAADTIKEKQLKNV----VIDPVMVCKG---ANEVLYPEHAEAlreQLAP--L 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   142 VDIITPNQFELEILYG-GEIKTKEHLKKALKKLHQTIPVIIVTSCDCKMFDDK--DFIYcvasmEGKTPIVYRVPFIDSY 218
Cdd:PRK12616 135 ATVITPNLFEAGQLSGmGEIKTVEQMKEAAKKIHELGAQYVVITGGGKLKHEKavDVLY-----DGETAEVLESEMIDTP 209

                        170
                 ....*....|.
gi 6320806   219 FT-GVGDLFSA 228
Cdd:PRK12616 210 YThGAGCTFSA 220
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 126-231 6.62e-08

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 53.12  E-value: 6.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    126 DVIPEYRKLALSPKQLVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQT-IPVIIVTScdckmfDDKDFIYCVASMEG 204
Cdd:pfam00294 165 DPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKgIKTVIVTL------GADGALVVEGDGEV 238

                          90       100
                  ....*....|....*....|....*..
gi 6320806    205 KTPIVYRVPFIDSyfTGVGDLFSALLL 231
Cdd:pfam00294 239 HVPAVPKVKVVDT--TGAGDSFVGGFL 263
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
49-175 8.70e-08

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 52.37  E-value: 8.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    49 DKVFGTITRETDL-KELLSGLFDnfsQDYQALLSGYLPNKNsvrcMGTYYAKFKEANPEMIWLMDPVmgdegqLYVSE-- 125
Cdd:PRK12413  46 EKGFEVFPVDKEIfQQQLDSLKD---VPFSAIKIGLLPNVE----IAEQALDFIKGHPGIPVVLDPV------LVCKEth 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6320806   126 DV-IPEYRKLALSPKQLVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQ 175
Cdd:PRK12413 113 DVeVSELRQELIQFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYD 163
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
77-228 3.08e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 47.66  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806    77 QALLSGYLPNKNSVRCMGTYYAKFKEANPemiwLMDPVMGDEGQlyvSEDVIPE----YRKLaLSPKQLVdiITPNQFEL 152
Cdd:PRK12412  74 DALKTGMLGSVEIIEMVAETIEKHNFKNV----VVDPVMVCKGA---DEALHPEtndcLRDV-LVPKALV--VTPNLFEA 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320806   153 EILYGGEIKTKEHLKKALKKLHQTIPVIIVTSCDCKMFDDK--DFIYcvasmEGKTPIVYRVPFIDSYFT-GVGDLFSA 228
Cdd:PRK12412 144 YQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKLGTETaiDVLY-----DGETFDLLESEKIDTTNThGAGCTYSA 217
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 142-243 5.25e-06

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


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 47.31  E-value: 5.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806  142 VDIITPNQFELEILYGGEIKTKEHLKKALKKLHQT-IPVIIVTscdckmFDDKDfIYCVASMEGKTPIVYRVPFIDSY-- 218
Cdd:cd01941 177 IDLLTPNRAELEALAGALIENNEDENKAAKILLLPgIKNVIVT------LGAKG-VLLSSREGGVETKLFPAPQPETVvn 249

                        90       100
                ....*....|....*....|....*
gi 6320806  219 FTGVGDLFSALLldrVYKILSNPTT 243
Cdd:cd01941 250 VTGAGDAFVAGL---VAGLLEGMSL 271
PRK11142 PRK11142
ribokinase; Provisional
 140-230 2.53e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 45.25  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   140 QLVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQT-IPVIIVTSCDCKMFddkdfiycvASMEGKTPIV--YRVPFID 216
Cdd:PRK11142 177 ALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKgIETVLITLGSRGVW---------LSENGEGQRVpgFRVQAVD 247

                         90
                 ....*....|....*
gi 6320806   217 SyfTGVGDLFS-ALL 230
Cdd:PRK11142 248 T--IAAGDTFNgALV 260
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 140-183 1.41e-04

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: 42.92  E-value: 1.41e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6320806  140 QLVDIITPNQFELEILYGGEIKTKEHLKKALKKLH-QTIPVIIVT 183
Cdd:cd01174 174 ALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLaKGVKNVIVT 218
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 141-231 1.65e-04

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: 41.70  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806  141 LVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQT-IPVIIVT--SCDCKMFDDKDfiycvasMEGKTPIVYRVPfIDS 217
Cdd:cd00287 109 GVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKgPKVVIVTlgEKGAIVATRGG-------TEVHVPAFPVKV-VDT 180

                        90
                ....*....|....
gi 6320806  218 yfTGVGDLFSALLL 231
Cdd:cd00287 181 --TGAGDAFLAALA 192
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 140-228 2.37e-04

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: 42.18  E-value: 2.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806  140 QLVDIITPNQFELEILYGgeiktKEHLKKALKKLHQ-TIPVIIVT--SCDCKMFDDKDFIYCVAsmegktpivYRVPFID 216
Cdd:COG0524 184 ALVDILFPNEEEAELLTG-----ETDPEEAAAALLArGVKLVVVTlgAEGALLYTGGEVVHVPA---------FPVEVVD 249

                        90
                ....*....|..
gi 6320806  217 SyfTGVGDLFSA 228
Cdd:COG0524 250 T--TGAGDAFAA 259
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
112-228 3.25e-04

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 42.02  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320806   112 DPVM-GDEGQLYVSEDVIPEYRKLALSpkqLVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQTI--PVIIVTSCDCK 188
Cdd:PRK08573 103 DPVMiAKSGAPLLREDAVDALIKRLLP---LATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEELgaEAVVVKGGHLE 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6320806   189 MFDDKDFIYCVASMEgktpiVYRVPFIDSYFT-GVGDLFSA 228
Cdd:PRK08573 180 GEEAVDVLYHNGTFR-----EFRAPRVESGCThGTGCSFSA 215
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
142-183 3.47e-04

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 41.66  E-value: 3.47e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6320806  142 VDIITPNQFELEILYGGEIKTKEHLKKALKKLHQT-IPVIIVT 183
Cdd:COG1105 178 PDLIKPNLEELEELLGRPLETLEDIIAAARELLERgAENVVVS 220
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 112-175 5.95e-04

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 40.88  E-value: 5.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320806   112 DPVM----GDEGqlyVSEDVIPEYRKLALsPkqLVDIITPNQFELEILYGGEIKTKEH-LKKALKKLHQ 175
Cdd:PRK06427 106 DPVMiaksGDPL---LADDAVAALRERLL-P--LATLITPNLPEAEALTGLPIADTEDeMKAAARALHA 168
 
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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