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Conserved domains on  [gi|1356626832|gb|AVL06973|]
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thiamine pyrophosphokinase [Bacillus subtilis]

Protein Classification

thi_PPkinase family protein( domain architecture ID 11492381)

thi_PPkinase family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 5-210 6.54e-90

thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly eukaryotic thiamine pyrophosphokinase. However, it is now expanded to include also homologous enzymes, apparently functionally equivalent, from species that rely on thiamine pyrophosphokinase rather than thiamine-monophosphate kinase (TIGR01379) to produce the active TPP cofactor. This includes the thiamine pyrophosphokinase from Bacillus subtilis, previously designated YloS. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


:

Pssm-ID: 273588 [Multi-domain]  Cd Length: 205  Bit Score: 262.60  E-value: 6.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832   5 NIVAGGPkNLIPDLTGYTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTDLDL 84
Cdd:TIGR01378   1 LILAGGG-PDSELPLRLLKEHDLVIAADGGANHLLKLGLTPDLIVGDFDSIDEEELDFYKETGVKIIVFPPEKDTTDLEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  85 ALDWALEKQPDIIQIFGITGGRADHFLGNIQLLYRGVKTNIKIRLIDKQNHIQMFPPGEYDIEKDENKRYISFIPFSEDI 164
Cdd:TIGR01378  80 ALKYALERGADEITILGATGGRLDHTLANLNLLLEYAKRGIEVRLIDEQNVIRLLLPGKYQIFKEPKGTYISLLPFGGDV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1356626832 165 HELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILIMI 210
Cdd:TIGR01378 160 HGLTTKGLKYPLNNADLKFGGTRGISNEFIGNKATVSVDSGILLVI 205
 
Name Accession Description Interval E-value
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 5-210 6.54e-90

thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly eukaryotic thiamine pyrophosphokinase. However, it is now expanded to include also homologous enzymes, apparently functionally equivalent, from species that rely on thiamine pyrophosphokinase rather than thiamine-monophosphate kinase (TIGR01379) to produce the active TPP cofactor. This includes the thiamine pyrophosphokinase from Bacillus subtilis, previously designated YloS. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273588 [Multi-domain]  Cd Length: 205  Bit Score: 262.60  E-value: 6.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832   5 NIVAGGPkNLIPDLTGYTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTDLDL 84
Cdd:TIGR01378   1 LILAGGG-PDSELPLRLLKEHDLVIAADGGANHLLKLGLTPDLIVGDFDSIDEEELDFYKETGVKIIVFPPEKDTTDLEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  85 ALDWALEKQPDIIQIFGITGGRADHFLGNIQLLYRGVKTNIKIRLIDKQNHIQMFPPGEYDIEKDENKRYISFIPFSEDI 164
Cdd:TIGR01378  80 ALKYALERGADEITILGATGGRLDHTLANLNLLLEYAKRGIEVRLIDEQNVIRLLLPGKYQIFKEPKGTYISLLPFGGDV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1356626832 165 HELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILIMI 210
Cdd:TIGR01378 160 HGLTTKGLKYPLNNADLKFGGTRGISNEFIGNKATVSVDSGILLVI 205
ThiN COG1564
Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is ...
 2-211 6.46e-86

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


Pssm-ID: 441172 [Multi-domain]  Cd Length: 209  Bit Score: 252.79  E-value: 6.46e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832   2 KTINIVAGGPKNLIPDLTGYTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTD 81
Cdd:COG1564     1 MKALILAGGELPDPELLKELLEKADFIIAADGGALHLLELGIKPDLIIGDFDSISEEELEQYKEKGVEIIIFPPEKDETD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  82 LDLALDWALEKQPDIIQIFGITGGRADHFLGNIQLLYRGVKTNIKIRLIDKQNHIQMFPPGEYDIEKDENKrYISFIPFS 161
Cdd:COG1564    81 TELALRYALERGADEILILGATGGRLDHTLANLSLLARYAEKGIRIVLIDENNEIFLLPPGSLTLEGPPGT-YVSLIPLS 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1356626832 162 EDIHELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILIMIR 211
Cdd:COG1564   160 DPVTGLTLEGLKYPLDNATLTFGSSLGISNEAIGDEATISVESGILLVIL 209
TPK cd07995
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 4-212 4.40e-79

Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin pyrophosphokinase) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamine) to form the coenzyme thiamine pyrophosphate (TPP). TPP is required for central metabolic functions, and thiamine deficiency is associated with potentially fatal human diseases. The structure of thiamine pyrophosphokinase suggests that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 153431 [Multi-domain]  Cd Length: 208  Bit Score: 235.52  E-value: 4.40e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832   4 INIVAGGPKNLIPDLTGYTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTDLD 83
Cdd:cd07995     1 ALILLGGPLPDSPLLLKLWKKADLIIAADGGANHLLDLGIVPDLIIGDFDSISPEVLEYYKSKGVEIIHFPDEKDFTDFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  84 LALDWALEKQPDIIQIFGITGGRADHFLGNIQLLYRGVKTNIKIRLIDKQNHIQMFPPGEYDIEKDENKRYISFIPFSED 163
Cdd:cd07995    81 KALKLALERGADEIVILGATGGRLDHTLANLNLLLKYAKDGIKIVLIDEQNEIFLLLPGSHTLELEEEGKYVSLIPLGEV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1356626832 164 iHELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILIMIRS 212
Cdd:cd07995   161 -TGLTLKGLKYPLDNATLSFGSSLGTSNEFTGEKATVSVESGLLLVILS 208
TPK_catalytic pfam04263
Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). ...
 21-129 7.37e-30

Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 461242  Cd Length: 112  Bit Score: 106.82  E-value: 7.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  21 YTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTDLDLALDWALEKQPDIIQIF 100
Cdd:pfam04263   4 LWKNADLRICADGGANRLYRLGIKPDVIVGDFDSIRPEVREYYKSKGVEIIKTPADQDTTDLEKAIELALEKGVDEIVVL 83

                          90       100
                  ....*....|....*....|....*....
gi 1356626832 101 GITGGRADHFLGNIQLLYRGVKTNIKIRL 129
Cdd:pfam04263  84 GALGGRFDHTLANINLLYKLLKKGIKIVL 112
TPK_B1_binding smart00983
Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) ...
 142-208 2.46e-21

Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 214953 [Multi-domain]  Cd Length: 66  Bit Score: 83.39  E-value: 2.46e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1356626832  142 GEYDIEKDENKRYISFIPFSeDIHELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILI 208
Cdd:smart00983   1 GKHEILKLPDGKYCSLIPLG-DVAGLTTKGLKYPLENADLSFGSSLSTSNEFIGEPVTVSVESGKLL 66
PLN02714 PLN02714
thiamin pyrophosphokinase
 78-191 7.51e-08

thiamin pyrophosphokinase


Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 51.17  E-value: 7.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  78 DQTDLDLAL------DWALEKQPDIIQIFGITGGRADHFLGNIQLLYRgvKTNIKIRLIDKQNHIQMFPPG---EYDIEK 148
Cdd:PLN02714   88 DTTDLHKCIayirdsTPDLDKSNLCILVLGALGGRFDHEAGNINVLYR--FPDLRIVLLSDDCLIRLLPAThrhEIHIDS 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1356626832 149 DENKRYISFIPFSEDIHELTLTGFKYPLNNCHITLGSTLCISN 191
Cdd:PLN02714  166 SVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSN 208
 
Name Accession Description Interval E-value
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 5-210 6.54e-90

thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly eukaryotic thiamine pyrophosphokinase. However, it is now expanded to include also homologous enzymes, apparently functionally equivalent, from species that rely on thiamine pyrophosphokinase rather than thiamine-monophosphate kinase (TIGR01379) to produce the active TPP cofactor. This includes the thiamine pyrophosphokinase from Bacillus subtilis, previously designated YloS. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273588 [Multi-domain]  Cd Length: 205  Bit Score: 262.60  E-value: 6.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832   5 NIVAGGPkNLIPDLTGYTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTDLDL 84
Cdd:TIGR01378   1 LILAGGG-PDSELPLRLLKEHDLVIAADGGANHLLKLGLTPDLIVGDFDSIDEEELDFYKETGVKIIVFPPEKDTTDLEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  85 ALDWALEKQPDIIQIFGITGGRADHFLGNIQLLYRGVKTNIKIRLIDKQNHIQMFPPGEYDIEKDENKRYISFIPFSEDI 164
Cdd:TIGR01378  80 ALKYALERGADEITILGATGGRLDHTLANLNLLLEYAKRGIEVRLIDEQNVIRLLLPGKYQIFKEPKGTYISLLPFGGDV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1356626832 165 HELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILIMI 210
Cdd:TIGR01378 160 HGLTTKGLKYPLNNADLKFGGTRGISNEFIGNKATVSVDSGILLVI 205
ThiN COG1564
Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is ...
 2-211 6.46e-86

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


Pssm-ID: 441172 [Multi-domain]  Cd Length: 209  Bit Score: 252.79  E-value: 6.46e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832   2 KTINIVAGGPKNLIPDLTGYTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTD 81
Cdd:COG1564     1 MKALILAGGELPDPELLKELLEKADFIIAADGGALHLLELGIKPDLIIGDFDSISEEELEQYKEKGVEIIIFPPEKDETD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  82 LDLALDWALEKQPDIIQIFGITGGRADHFLGNIQLLYRGVKTNIKIRLIDKQNHIQMFPPGEYDIEKDENKrYISFIPFS 161
Cdd:COG1564    81 TELALRYALERGADEILILGATGGRLDHTLANLSLLARYAEKGIRIVLIDENNEIFLLPPGSLTLEGPPGT-YVSLIPLS 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1356626832 162 EDIHELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILIMIR 211
Cdd:COG1564   160 DPVTGLTLEGLKYPLDNATLTFGSSLGISNEAIGDEATISVESGILLVIL 209
TPK cd07995
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 4-212 4.40e-79

Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin pyrophosphokinase) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamine) to form the coenzyme thiamine pyrophosphate (TPP). TPP is required for central metabolic functions, and thiamine deficiency is associated with potentially fatal human diseases. The structure of thiamine pyrophosphokinase suggests that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 153431 [Multi-domain]  Cd Length: 208  Bit Score: 235.52  E-value: 4.40e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832   4 INIVAGGPKNLIPDLTGYTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTDLD 83
Cdd:cd07995     1 ALILLGGPLPDSPLLLKLWKKADLIIAADGGANHLLDLGIVPDLIIGDFDSISPEVLEYYKSKGVEIIHFPDEKDFTDFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  84 LALDWALEKQPDIIQIFGITGGRADHFLGNIQLLYRGVKTNIKIRLIDKQNHIQMFPPGEYDIEKDENKRYISFIPFSED 163
Cdd:cd07995    81 KALKLALERGADEIVILGATGGRLDHTLANLNLLLKYAKDGIKIVLIDEQNEIFLLLPGSHTLELEEEGKYVSLIPLGEV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1356626832 164 iHELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILIMIRS 212
Cdd:cd07995   161 -TGLTLKGLKYPLDNATLSFGSSLGTSNEFTGEKATVSVESGLLLVILS 208
TPK_catalytic pfam04263
Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). ...
 21-129 7.37e-30

Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 461242  Cd Length: 112  Bit Score: 106.82  E-value: 7.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  21 YTDEHTLWIGVDKGTVTLLDAGIIPVEAFGDFDSITEQERRRIEKAAPALHVYQAEKDQTDLDLALDWALEKQPDIIQIF 100
Cdd:pfam04263   4 LWKNADLRICADGGANRLYRLGIKPDVIVGDFDSIRPEVREYYKSKGVEIIKTPADQDTTDLEKAIELALEKGVDEIVVL 83

                          90       100
                  ....*....|....*....|....*....
gi 1356626832 101 GITGGRADHFLGNIQLLYRGVKTNIKIRL 129
Cdd:pfam04263  84 GALGGRFDHTLANINLLYKLLKKGIKIVL 112
TPK_B1_binding smart00983
Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) ...
 142-208 2.46e-21

Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 214953 [Multi-domain]  Cd Length: 66  Bit Score: 83.39  E-value: 2.46e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1356626832  142 GEYDIEKDENKRYISFIPFSeDIHELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGILI 208
Cdd:smart00983   1 GKHEILKLPDGKYCSLIPLG-DVAGLTTKGLKYPLENADLSFGSSLSTSNEFIGEPVTVSVESGKLL 66
TPK_B1_binding pfam04265
Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC: ...
 143-207 7.00e-21

Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 461244 [Multi-domain]  Cd Length: 66  Bit Score: 82.11  E-value: 7.00e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1356626832 143 EYDIEKDENK-RYISFIPFSEDIHELTLTGFKYPLNNCHITLGSTLCISNELIHSRGTFSFAKGIL 207
Cdd:pfam04265   1 EHTIKKEEGFgKYCSLIPLGGPVTGLTLKGLKYPLTNATLSFGGSLSTSNEFVEEEATISFDSGIL 66
PLN02714 PLN02714
thiamin pyrophosphokinase
 78-191 7.51e-08

thiamin pyrophosphokinase


Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 51.17  E-value: 7.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626832  78 DQTDLDLAL------DWALEKQPDIIQIFGITGGRADHFLGNIQLLYRgvKTNIKIRLIDKQNHIQMFPPG---EYDIEK 148
Cdd:PLN02714   88 DTTDLHKCIayirdsTPDLDKSNLCILVLGALGGRFDHEAGNINVLYR--FPDLRIVLLSDDCLIRLLPAThrhEIHIDS 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1356626832 149 DENKRYISFIPFSEDIHELTLTGFKYPLNNCHITLGSTLCISN 191
Cdd:PLN02714  166 SVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSN 208
 
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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