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Conserved domains on  [gi|489531760|ref|WP_003436492|]
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bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase [Clostridioides difficile]

Protein Classification

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase( domain architecture ID 10001245)

bifunctional enzyme, phosphomethylpyrimidine (HMP-P) kinase/hydroxymethylpyrimidine (HMP) kinase; bifunctional hydroxymethylpyrimidine (HMP) kinase/phosphomethylpyrimidine (HMP-P) kinase catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P

CATH:  3.40.1190.20
EC:  2.7.4.7|2.7.1.49
Gene Symbol:  thiD
Gene Ontology:  GO:0005524|GO:0016310|GO:0042724|GO:0008902|GO:0008972|GO:0009228|GO:0005829
PubMed:  8382990|11839308
SCOP:  3001268

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-261 1.35e-150

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


:

Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 420.21  E-value: 1.35e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQ 168
Cdd:COG0351   81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 169 LGPKFVLMKGGHLDG-EAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRS 247
Cdd:COG0351  161 LGAKAVLVKGGHLPGdEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAA 240

                        250
                 ....*....|....
gi 489531760 248 FDIGHGVGPVHHFY 261
Cdd:COG0351  241 LRLGMGHGPVNHFA 254
 
Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-261 1.35e-150

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 420.21  E-value: 1.35e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQ 168
Cdd:COG0351   81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 169 LGPKFVLMKGGHLDG-EAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRS 247
Cdd:COG0351  161 LGAKAVLVKGGHLPGdEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAA 240

                        250
                 ....*....|....
gi 489531760 248 FDIGHGVGPVHHFY 261
Cdd:COG0351  241 LRLGMGHGPVNHFA 254
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 9-261 3.07e-139

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 392.18  E-value: 3.07e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:PRK06427   8 LTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGMLASAEI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHN-VDDMKRVGEEIL 167
Cdd:PRK06427  88 IETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADtEDEMKAAARALH 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 168 QLGPKFVLMKGGHL--DGEAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIK 245
Cdd:PRK06427 168 ALGCKAVLIKGGHLldGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKDYVTRAIR 247

                        250
                 ....*....|....*.
gi 489531760 246 RSFDIGHGVGPVHHFY 261
Cdd:PRK06427 248 HALEIGQGHGPVNHFA 263
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 15-258 7.71e-134

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: 377.59  E-value: 7.71e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   15 DSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEIILEIVE 94
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   95 NLKKYNPKyLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQLGPKFV 174
Cdd:pfam08543  81 KLDKYGVP-VVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  175 LMKGGHLDGE---AVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRSFDIG 251
Cdd:pfam08543 160 LIKGGHLEGEeavVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLG 239


                  ....*..
gi 489531760  252 HGVGPVH 258
Cdd:pfam08543 240 KGHGPVN 246
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 9-247 3.49e-129

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 365.67  E-value: 3.49e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:cd01169    3 LTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSAEI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQ 168
Cdd:cd01169   83 IEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKALLA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 169 LGPKFVLMKGGHL-DGEAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRS 247
Cdd:cd01169  163 LGAKAVLIKGGHLpGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIRNA 242
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 9-260 7.93e-127

hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 272904 [Multi-domain]  Cd Length: 254  Bit Score: 360.07  E-value: 7.93e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760    9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:TIGR00097   2 LTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQ 168
Cdd:TIGR00097  82 VEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLRE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  169 LGPKFVLMKGGHLDG-EAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRS 247
Cdd:TIGR00097 162 LGPKAVLIKGGHLEGdQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIRYG 241

                         250
                  ....*....|...
gi 489531760  248 FDIGHGVGPVHHF 260
Cdd:TIGR00097 242 LNIGHGHGPLNHF 254
 
Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-261 1.35e-150

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 420.21  E-value: 1.35e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQ 168
Cdd:COG0351   81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 169 LGPKFVLMKGGHLDG-EAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRS 247
Cdd:COG0351  161 LGAKAVLVKGGHLPGdEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAA 240

                        250
                 ....*....|....
gi 489531760 248 FDIGHGVGPVHHFY 261
Cdd:COG0351  241 LRLGMGHGPVNHFA 254
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 9-261 3.07e-139

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 392.18  E-value: 3.07e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:PRK06427   8 LTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGMLASAEI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHN-VDDMKRVGEEIL 167
Cdd:PRK06427  88 IETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADtEDEMKAAARALH 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 168 QLGPKFVLMKGGHL--DGEAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIK 245
Cdd:PRK06427 168 ALGCKAVLIKGGHLldGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKDYVTRAIR 247

                        250
                 ....*....|....*.
gi 489531760 246 RSFDIGHGVGPVHHFY 261
Cdd:PRK06427 248 HALEIGQGHGPVNHFA 263
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 15-258 7.71e-134

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: 377.59  E-value: 7.71e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   15 DSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEIILEIVE 94
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   95 NLKKYNPKyLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQLGPKFV 174
Cdd:pfam08543  81 KLDKYGVP-VVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  175 LMKGGHLDGE---AVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRSFDIG 251
Cdd:pfam08543 160 LIKGGHLEGEeavVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLG 239


                  ....*..
gi 489531760  252 HGVGPVH 258
Cdd:pfam08543 240 KGHGPVN 246
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 9-247 3.49e-129

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 365.67  E-value: 3.49e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:cd01169    3 LTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSAEI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQ 168
Cdd:cd01169   83 IEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKALLA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 169 LGPKFVLMKGGHL-DGEAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRS 247
Cdd:cd01169  163 LGAKAVLIKGGHLpGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIRNA 242
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 9-260 7.93e-127

hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 272904 [Multi-domain]  Cd Length: 254  Bit Score: 360.07  E-value: 7.93e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760    9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:TIGR00097   2 LTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQ 168
Cdd:TIGR00097  82 VEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLRE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  169 LGPKFVLMKGGHLDG-EAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRS 247
Cdd:TIGR00097 162 LGPKAVLIKGGHLEGdQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIRYG 241

                         250
                  ....*....|...
gi 489531760  248 FDIGHGVGPVHHF 260
Cdd:TIGR00097 242 LNIGHGHGPLNHF 254
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-257 6.49e-98

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 293.94  E-value: 6.49e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   6 IPT-LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVS 84
Cdd:PRK08573   2 IPVaLTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  85 SPEIILEIVENLKKYN-PkyLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVG 163
Cdd:PRK08573  82 NREIIEAVAKTVSKYGfP--LVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 164 EEIL-QLGPKFVLMKGGHLDG-EAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYIT 241
Cdd:PRK08573 160 KYIVeELGAEAVVVKGGHLEGeEAVDVLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFIT 239

                        250
                 ....*....|....*.
gi 489531760 242 EAIKRSFDIGHGVGPV 257
Cdd:PRK08573 240 MAIKYGVKIGKGHCPV 255
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 2-262 8.76e-93

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 282.43  E-value: 8.76e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   2 SNYKIP-TLTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKI 80
Cdd:PLN02898   5 SPMKVPhVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  81 GMVSSPEIILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITG-IKIHNVDDM 159
Cdd:PLN02898  85 GMLPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGgDPLETVADM 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 160 KRVGEEILQLGPKFVLMKGGHL--DGEAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSK 237
Cdd:PLN02898 165 RSAAKELHKLGPRYVLVKGGHLpdSLDAVDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAK 244

                        250       260
                 ....*....|....*....|....*...
gi 489531760 238 IYITEAIKRSFDIGHGV---GPVHHFYK 262
Cdd:PLN02898 245 RYVETALEYSKDIGIGNgaqGPFNHLFF 272
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
9-261 5.16e-76

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 240.08  E-value: 5.16e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:PRK14713  33 LSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGDAEV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAkENLIKYLIPLAYIITPNIPEAEEITGikihnvDDMKRVGEEILQ 168
Cdd:PRK14713 113 IDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDA-EAALRELVPRADLITPNLPELAVLLG------EPPATTWEEALA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 169 LGPKF-------VLMKGGHLDGEAV-DILVGKN-IFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIY 239
Cdd:PRK14713 186 QARRLaaetgttVLVKGGHLDGQRApDALVGPDgAVTEVPGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAW 265

                        250       260
                 ....*....|....*....|....
gi 489531760 240 ITEAIKRS--FDIGHGVGPVHHFY 261
Cdd:PRK14713 266 LHGAIAAGaaLQVGTGNGPVDHFH 289
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 3-259 9.05e-74

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 233.32  E-value: 9.05e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   3 NYKIPT-LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIG 81
Cdd:PTZ00347 227 PMKIPTvLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLG 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  82 MVSSPEIILEIVENLKKYNpkyLVVDPVMISKSGYYLLKPEAKENLIK----YLIPLAYIITPNIPEAEEITGIK-IHNV 156
Cdd:PTZ00347 307 LVPTARQLEIVIEKLKNLP---MVVDPVLVATSGDDLVAQKNADDVLAmykeRIFPMATIITPNIPEAERILGRKeITGV 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 157 DDMKRVGEEILQLGPKFVLMKGGH--LDGEA-VDILVG--KNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITE 231
Cdd:PTZ00347 384 YEARAAAQALAQYGSRYVLVKGGHdlIDPEAcRDVLYDreKDRFYEFTANRIATINTHGTGCTLASAISSFLARGYTVPD 463

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489531760 232 AVNLSKIYITEAIKRSFDIGHGVG---PVHH 259
Cdd:PTZ00347 464 AVERAIGYVHEAIVRSCGVPLGQGtnrPLVH 494
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
9-259 5.34e-72

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 221.77  E-value: 5.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFA--VEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSP 86
Cdd:PRK12412   5 LTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNGWAhnVFPIPASTLKPQLETTIEGVGVDALKTGMLGSV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  87 EIILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEI 166
Cdd:PRK12412  85 EIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 167 LQLGPKFVLMKGGHLDG--EAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAI 244
Cdd:PRK12412 165 HALGAKYVLIKGGSKLGteTAIDVLYDGETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKTAKEFITAAI 244

                        250
                 ....*....|....*
gi 489531760 245 KRSFDIGHGVGPVHH 259
Cdd:PRK12412 245 RYSFKINEYVGPTHH 259
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-259 4.05e-66

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 206.82  E-value: 4.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   1 MSNYKipTLTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVF--AVEDLNKKIIKKQIEAVFEDIPPRAV 78
Cdd:PRK12616   1 MSMHK--ALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWdhQVFPIDTDTIRAQLSTIVDGIGVDAM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  79 KIGMVSSPEIILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGI-KIHNVD 157
Cdd:PRK12616  79 KTGMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMgEIKTVE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 158 DMKRVGEEILQLGPKFVLMKGG-HLDGE-AVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNL 235
Cdd:PRK12616 159 QMKEAAKKIHELGAQYVVITGGgKLKHEkAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYA 238

                        250       260
                 ....*....|....*....|....
gi 489531760 236 SKIYITEAIKRSFDIGHGVGPVHH 259
Cdd:PRK12616 239 AKEFITAAIKESFPLNQYVGPTKH 262
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 9-260 3.03e-56

multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 192.11  E-value: 3.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:PRK09517 245 LSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLGSADT 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKyLIPLAYIITPNIPEAEEITGIKihNVDDMkrvgEEILQ 168
Cdd:PRK09517 325 VDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALRR-LAVHVDVVTPNIPELAVLCGEA--PAITM----DEAIA 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 169 LGPKF-------VLMKGGHLDGE-AVDILV--GKNIFKVyKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKI 238
Cdd:PRK09517 398 QARGFarthgtiVIVKGGHLTGDlADNAVVrpDGSVHQV-ENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATR 476

                        250       260
                 ....*....|....*....|....
gi 489531760 239 YITEAIKRSFD--IGHGVGPVHHF 260
Cdd:PRK09517 477 WLNEALRHADHlaVGSGNGPVDHG 500
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-251 1.17e-54

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 176.79  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   1 MSNYKIptLTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKG--VFAVEdlnKKIIKKQIEAvFEDIPPRAV 78
Cdd:PRK12413   1 MKTNYI--LAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKGfeVFPVD---KEIFQQQLDS-LKDVPFSAI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  79 KIGMVSSPEIILEIVENLKKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLiPLAYIITPNIPEAEEITGIKIHNVDD 158
Cdd:PRK12413  75 KIGLLPNVEIAEQALDFIKGHPGIPVVLDPVLVCKETHDVEVSELRQELIQFF-PYVTVITPNLVEAELLSGKEIKTLED 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 159 MKRVGEEILQLGPKFVLMKGGH-LDGE-AVDILVGKNIFKVYKSERIDKKNThGTGCTLSSAITSYLALGYEITEAVNLS 236
Cdd:PRK12413 154 MKEAAKKLYDLGAKAVVIKGGNrLSQKkAIDLFYDGKEFVILESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEAVKNS 232

                        250
                 ....*....|....*
gi 489531760 237 KIYITEAIKRSFDIG 251
Cdd:PRK12413 233 KDFVYQAIQQSDQYG 247
COG1992 COG1992
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ...
 17-259 5.06e-44

Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];


Pssm-ID: 441595 [Multi-domain]  Cd Length: 432  Bit Score: 154.14  E-value: 5.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  17 SGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEIIlEIVENL 96
Cdd:COG1992    1 GGGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTATIV-EVVAVV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  97 KKYNPKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQLGPKFVL- 175
Cdd:COG1992   80 VKSRDKPLVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVEELLLPTIRSLLAEARAARLALQEEGADALg 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 176 MKGGHLDGEA-VDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRSFDIGHGV 254
Cdd:COG1992  160 VKGGHVSGDAvVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYGLLVGKGV 239


                 ....*
gi 489531760 255 GPVHH 259
Cdd:COG1992  240 GPVNH 244
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 9-251 9.72e-38

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 135.12  E-value: 9.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   9 LTIAGSDSSGGAGIQADLKTFSAIGTYGMSVITAITAQNTKGVFAVEDLNKKIIKKQIEAVFEDIPPRAVKIGMVSSPEI 88
Cdd:PTZ00493   8 LSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLYSKKI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  89 ILEIVENL----KKYNPKYLVV-DPVMISKSGYYLLkpeakENL--IKY----LIPLAYIITPNIPEAEEITGIKIHNVD 157
Cdd:PTZ00493  88 ISLVHNYItnmnKKRGKKLLVVfDPVFVSSSGCLLV-----ENLeyIKFaldlICPISCIITPNFYECKVILEALDCQMD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 158 DMKRVGEEILQLGPKFV-----LMKGGHLDGE--------AVDILVGKNI-------------------FKVYK--SERI 203
Cdd:PTZ00493 163 LSKANMTELCKLVTEKLninacLFKSCNVGENsaeenevyAVDHLCIRNVgsyptgekqqidaggvtylYDVYKlrSKRK 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 489531760 204 DKKNTHGTGCTLSSAITSYLALGYEITEAVNLSKIYITEAIKRSFDIG 251
Cdd:PTZ00493 243 PGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPFG 290
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 76-252 4.73e-27

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: 105.62  E-value: 4.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  76 RAVKIGMVSSPE---IILEIVENLKKYNPKYLV-VDPVM-ISKSGYYLLKPEAkENLIKYLIPLAYIITPNIPEAEEITG 150
Cdd:COG2240   76 DAVLSGYLGSAEqgdIIADFVARVKAANPDALYlCDPVMgDNGKGYYVFPGIA-EFIMRRLVPLADIITPNLTELALLTG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 151 IKIHNVDDMKRVGEEILQLGPKFVLMKGGHLDGEAVD----ILVGKNIFKVYKSERIDKKnTHGTGCTLSSAITSYLALG 226
Cdd:COG2240  155 RPYETLEEALAAARALLALGPKIVVVTSVPLDDTPADkignLAVTADGAWLVETPLLPFS-PNGTGDLFAALLLAHLLRG 233

                        170       180
                 ....*....|....*....|....*.
gi 489531760 227 YEITEAVNLSKIYITEAIKRSFDIGH 252
Cdd:COG2240  234 KSLEEALERAAAFVYEVLERTAAAGS 259
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 87-249 9.66e-25

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: 98.81  E-value: 9.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  87 EIILEIVENLKKYNPKYL-VVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEE 165
Cdd:cd01173   88 EAVAEIVKRLKEKNPNLLyVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 166 ILQLGPKFVLMKGGHLDGEAVDILVG---KNIFKVYKseRIDKKNTH--GTGCTLSSAITSYLALGYEITEAVNLSKIYI 240
Cdd:cd01173  168 LHAKGPKTVVVTSVELADDDRIEMLGstaTEAWLVQR--PKIPFPAYfnGTGDLFAALLLARLLKGKSLAEALEKALNFV 245


                 ....*....
gi 489531760 241 TEAIKRSFD 249
Cdd:cd01173  246 HEVLEATYE 254
PRK05756 PRK05756
pyridoxal kinase PdxY;
65-181 2.06e-15

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 74.14  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  65 QIEAVFEDIPPR-------AVKIGMVSSPEI---ILEIVENLKKYNPKYL-VVDPVM-ISKSGYYLlKPEAKENLIKYLI 132
Cdd:PRK05756  58 HLTEIVQGIADIgwlgecdAVLSGYLGSAEQgeaILDAVRRVKAANPQALyFCDPVMgDPEKGCIV-APGVAEFLRDRAL 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489531760 133 PLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQLGPKFVLMKggHL 181
Cdd:PRK05756 137 PAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT--SL 183
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 87-177 1.04e-13

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: 69.47  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   87 EIILEIVENLKKYNPKYL-VVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEE 165
Cdd:TIGR00687  90 AMVVGIVRQVKQANPQALyVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADA 169

                          90
                  ....*....|..
gi 489531760  166 ILQLGPKFVLMK 177
Cdd:TIGR00687 170 LIAMGPDIVLVT 181
PLN02978 PLN02978
pyridoxal kinase
 80-191 1.40e-12

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 66.30  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  80 IGMVSSPEIILEIVENLKKYNPKYL-VVDPVMISKSGYYLlKPEAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDD 158
Cdd:PLN02978  95 IGSVSFLRTVLRVVKKLRSVNPNLTyVCDPVLGDEGKLYV-PPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEED 173

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489531760 159 MKRVGEEILQLGPKFVLMKGGHLDGEAvdILVG 191
Cdd:PLN02978 174 AREACAILHAAGPSKVVITSIDIDGKL--LLVG 204
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 76-224 6.35e-12

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: 62.88  E-value: 6.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  76 RAVKI-GMVSSPEIILEIVENLKKYNPKYlVVDPVMISKSGYYLLKPEakenlikyLIPLAYIITPNIPEAEEITGIKIH 154
Cdd:cd00287   59 DAVVIsGLSPAPEAVLDALEEARRRGVPV-VLDPGPRAVRLDGEELEK--------LLPGVDILTPNEEEAEALTGRRDL 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489531760 155 NVDDMKRVGEEILQLGPKFVLMKGghldGEAVDILV--GKNIFKVyKSERIDKKNTHGTGCTLSSAITSYLA 224
Cdd:cd00287  130 EVKEAAEAAALLLSKGPKVVIVTL----GEKGAIVAtrGGTEVHV-PAFPVKVVDTTGAGDAFLAALAAGLA 196
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
76-247 4.64e-10

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 58.51  E-value: 4.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  76 RAVKIGMVSSPE---IILEIVENLKKYNPKYLV-VDPVMIS-KSGYYLlKPEAKENLIKYLIPLAYIITPNIPEAEEITG 150
Cdd:PRK08176  90 RAVTTGYMGSASqikILAEWLTALRADHPDLLImVDPVIGDiDSGIYV-KPDLPEAYRQHLLPLAQGLTPNIFELEILTG 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 151 IKIHNVDDMKRVGEEILQLGPKFVLMK---GGHLDGEAVDILVGKNIFKVYKSERIDkKNTHGTGCTLSSAITSYLALGY 227
Cdd:PRK08176 169 KPCRTLDSAIAAAKSLLSDTLKWVVITsaaGNEENQEMQVVVVTADSVNVISHPRVD-TDLKGTGDLFCAELVSGLLKGK 247

                        170       180
                 ....*....|....*....|
gi 489531760 228 EITEAVNLSKIYITEAIKRS 247
Cdd:PRK08176 248 ALTDAAHRAGLRVLEVMRYT 267
PRK07105 PRK07105
pyridoxamine kinase; Validated
 11-249 8.99e-10

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 58.00  E-value: 8.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  11 IAGSDSS--GGAGIQADLKTFSAIGTYGMSVITAITAQNTKGV--FAVEDLN---KKIIK--KQIEAVFEdipprAVKIG 81
Cdd:PRK07105   8 AAIHDLSgfGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFqnPSIIDLTdgmQAFLThwKSLNLKFD-----AIYSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  82 MVSSP---EIILEIVENLKKYNpKYLVVDPVMISKSGYYLLKPEAKENLIKYLIPLAYIITPNIPEA-----EEITGIKI 153
Cdd:PRK07105  83 YLGSPrqiQIVSDFIKYFKKKD-LLVVVDPVMGDNGKLYQGFDQEMVEEMRKLIQKADVITPNLTEAcllldKPYLEKSY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 154 hNVDDMKRVGEEILQLGPKFVLMKGGHLDGEAVDILV---GKNIFKVYKSERIdkkNTH--GTGCTLSSAITSYLALGYE 228
Cdd:PRK07105 162 -SEEEIKQLLRKLADLGPKIVIITSVPFEDGKIGVAYydrATDRFWKVFCKYI---PAHypGTGDIFTSVITGSLLQGDS 237

                        250       260
                 ....*....|....*....|.
gi 489531760 229 ITEAVNLSKIYITEAIKRSFD 249
Cdd:PRK07105 238 LPIALDRAVQFIEKGIRATLG 258
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 76-256 1.02e-09

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 57.78  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  76 RAVKIGMVSSPEI---ILEIVENLKKYNPK-YLVVDPVMISKSGYYLlkpeaKENLI---KYLIPLAYIITPNIPEAEEI 148
Cdd:PTZ00344  79 TYVLTGYINSADIlreVLATVKEIKELRPKlIFLCDPVMGDDGKLYV-----KEEVVdayRELIPYADVITPNQFEASLL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 149 TGIKIHNVDDMKRVGEEILQLGPKFVLMKGGHLDGEAVD-ILVGKNIFKVYKS--------ERIDKKNThGTGCTLSSAI 219
Cdd:PTZ00344 154 SGVEVKDLSDALEAIDWFHEQGIPVVVITSFREDEDPTHlRFLLSCRDKDTKNnkrftgkvPYIEGRYT-GTGDLFAALL 232

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489531760 220 TSYlALGYEITEAVNLSKIYITEAIKRSFDiGHGVGP 256
Cdd:PTZ00344 233 LAF-SHQHPMDLAVGKAMGVLQDIIKATRE-SGGSGS 267
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 85-233 1.62e-09

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 57.35  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760   85 SPEIILEIVENLKKYNpkyLVVDPVMISKSGyyllkpeAKENLIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGE 164
Cdd:pfam00294 141 LPEATLEELIEAAKNG---GTFDPNLLDPLG-------AAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALH 210

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489531760  165 EILQLGPKFVLMKgghLDGEAVDILVGKNIFKVYKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAV 233
Cdd:pfam00294 211 KLLAKGIKTVIVT---LGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEAL 276
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 127-233 2.35e-08

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: 53.71  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 127 LIKYLIPLAYIITPNIPEAEEITGIKIHNVDDMKRVGEEILQLGPKFVLMKGGHlDGeavDILVGKNIFKVYKSERIDKK 206
Cdd:cd01174  168 LPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGA-KG---ALLASGGEVEHVPAFKVKAV 243

                         90       100
                 ....*....|....*....|....*..
gi 489531760 207 NTHGTGCTLSSAITSYLALGYEITEAV 233
Cdd:cd01174  244 DTTGAGDTFIGALAAALARGLSLEEAI 270
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 85-235 1.73e-06

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: 48.34  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  85 SPEIILEIVENLKKYNPKyLVVDPvmisksGYYLLKPEAKENLIKYLIPLAYIITPNIPEAEEITGIkihnvDDMKRVGE 164
Cdd:COG0524  143 PREALLAALEAARAAGVP-VSLDP------NYRPALWEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAA 210

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489531760 165 EILQLGPKFVLMKGGhldGEAVDILVGKNIFKVyKSERIDKKNTHGTGCTLSSAITSYLALGYEITEAVNL 235
Cdd:COG0524  211 ALLARGVKLVVVTLG---AEGALLYTGGEVVHV-PAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRF 277
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 85-233 3.80e-05

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: 44.23  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760  85 SPEIILEIVENLKkyNPKYLVVD-----PVM--ISKSGYYLLKPEAKE-----NLIKYLIPLAYI--ITPNIPEAEEITG 150
Cdd:cd01941  115 TPDFLRKIREALK--EAKPIVVDanlpeEALeyLLALAAKHGVPVAFEptsapKLKKLFYLLHAIdlLTPNRAELEALAG 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 151 IKIHNVDDMKRVGEEILQLGPKFVLMKGGHlDGEAVDILVGKNIFKVYKSERIDK-KNTHGTGCTLSSAITSYLALGYEI 229
Cdd:cd01941  193 ALIENNEDENKAAKILLLPGIKNVIVTLGA-KGVLLSSREGGVETKLFPAPQPETvVNVTGAGDAFVAGLVAGLLEGMSL 271


                 ....
gi 489531760 230 TEAV 233
Cdd:cd01941  272 DDSL 275
PRK11142 PRK11142
ribokinase; Provisional
 137-175 5.50e-04

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 40.62  E-value: 5.50e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 489531760 137 IITPNIPEAEEITGIKIHNVDDMKRVGEEILQLGPKFVL 175
Cdd:PRK11142 181 IITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVL 219
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 135-236 8.10e-04

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: 40.24  E-value: 8.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531760 135 AYIITPNIPEAEEITGIKIHNVDDMKRVGEEIL-QLGPKFVLMKGG------HLDGEAVDIL--VGKNIFKVYkseridk 205
Cdd:cd01172  182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLeLLNLEALLVTLGeegmtlFERDGEVQHIpaLAKEVYDVT------- 254

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489531760 206 knthGTGCTLSSAITSYLALGYEITEAVNLS 236
Cdd:cd01172  255 ----GAGDTVIATLALALAAGADLEEAAFLA 281
 
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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