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Conserved domains on  [gi|1958749771|ref|XP_038957917|]
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methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial isoform X3 [Rattus norvegicus]

Protein Classification

biotin carboxylase domain-containing protein( domain architecture ID 1903193)

biotin carboxylase domain-containing protein similar to Blastocladiella emersonii acetyl-coenzyme-A carboxylase converts acetyl-CoA to malonyl-CoA, which is converted to malonyl-acyl carrier protein (ACP), the building block of the fatty acid moieties of bacterial membrane lipids

PubMed:  31023230

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA super family cl44129
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
45-315 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG4770:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 537.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:COG4770    82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:COG4770   162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:COG4770   242 APSPALTEELRERMGEAAVRAAKAVGYVGAG 272
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
45-315 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 537.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:COG4770    82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:COG4770   162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:COG4770   242 APSPALTEELRERMGEAAVRAAKAVGYVGAG 272
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 45-315 2.25e-156

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 446.94  E-value: 2.25e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08591    2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK08591   82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08591  162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:PRK08591  242 APSPAITEELRRKIGEAAVKAAKAIGYRGAG 272
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 45-315 2.06e-128

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 375.64  E-value: 2.06e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAG 272
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 45-152 8.74e-65

Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.


Pssm-ID: 425585 [Multi-domain]  Cd Length: 108  Bit Score: 200.79  E-value: 8.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTA 152
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
45-315 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 537.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:COG4770    82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:COG4770   162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:COG4770   242 APSPALTEELRERMGEAAVRAAKAVGYVGAG 272
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 45-315 2.25e-156

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 446.94  E-value: 2.25e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08591    2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK08591   82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08591  162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:PRK08591  242 APSPAITEELRRKIGEAAVKAAKAIGYRGAG 272
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 45-315 8.45e-145

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 417.51  E-value: 8.45e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK06111    2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK06111   82 YGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK06111  162 GGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:PRK06111  242 APSPFLDEETRKAMGERAVQAAKAIGYTNAG 272
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
47-315 8.33e-141

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 408.99  E-value: 8.33e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  47 KVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGYG 126
Cdd:PRK08654    4 KILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 127 FLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGG 206
Cdd:PRK08654   84 FLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 207 GGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAP 286
Cdd:PRK08654  164 GGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAP 243

                         250       260
                  ....*....|....*....|....*....
gi 1958749771 287 APGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:PRK08654  244 SPIMTPELRERMGEAAVKAAKAINYENAG 272
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 45-315 1.57e-139

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 424.49  E-value: 1.57e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771   45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:COG1038      4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIHP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  124 GYGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:COG1038     84 GYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:COG1038    164 AGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVE 243

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958749771  284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:COG1038    244 IAPAPNLDEELREAICEAAVKLAKAVGYVNAG 275
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
45-315 1.69e-133

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 388.69  E-value: 1.69e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK05586    2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK05586   82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK05586  162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:PRK05586  242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAG 272
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 45-315 7.33e-132

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 404.52  E-value: 7.33e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771   45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ-QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:PRK12999     5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIHP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  124 GYGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:PRK12999    85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKAS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK12999   165 AGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVE 244

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958749771  284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:PRK12999   245 IAPAPGLSEELRERICEAAVKLARAVGYVNAG 276
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 45-315 2.06e-128

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 375.64  E-value: 2.06e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAG 272
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
45-315 6.27e-119

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 352.48  E-value: 6.27e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPsQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK07178    2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQS-DECLKEhAGKIGYPVMIKAI 203
Cdd:PRK07178   81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADlDEALAE-AERIGYPVMLKAT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK07178  160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958749771 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:PRK07178  240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAG 271
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 45-317 5.02e-113

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 337.56  E-value: 5.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQqSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08463    2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHG-NDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:PRK08463   81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlNSESMEEIKIFARKIGYPVILKAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:PRK08463  161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958749771 284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGAL 317
Cdd:PRK08463  241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTI 274
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 43-317 4.93e-112

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 334.42  E-value: 4.93e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  43 GSITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIH 122
Cdd:PRK12833    3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 123 PGYGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKA 202
Cdd:PRK12833   83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 203 IRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHgNAVYLFERDCSVQRRHQKII 282
Cdd:PRK12833  163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKIL 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958749771 283 EEAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAGAL 317
Cdd:PRK12833  242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTL 276
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
45-315 3.56e-111

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 331.71  E-value: 3.56e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:PRK08462    4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIR 204
Cdd:PRK08462   84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 205 GGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEE 284
Cdd:PRK08462  164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958749771 285 APAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:PRK08462  244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAG 274
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 47-315 6.63e-111

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 349.13  E-value: 6.63e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771   47 KVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQ---QSYLAMEKIIQVAKSSAAQAIHP 123
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  124 GYGFLSENMEFAELCKQEGIIFIGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAI 203
Cdd:TIGR01235   81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  204 RGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIE 283
Cdd:TIGR01235  161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958749771  284 EAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:TIGR01235  241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAG 272
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 45-152 8.74e-65

Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.


Pssm-ID: 425585 [Multi-domain]  Cd Length: 108  Bit Score: 200.79  E-value: 8.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  45 ITKVLIANRGEIACRVIRTARKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPG 124
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 1958749771 125 YGFLSENMEFAELCKQEGIIFIGPPSTA 152
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 159-315 9.21e-62

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 196.76  E-value: 9.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 159 KSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDD 238
Cdd:pfam02786   2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958749771 239 AMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIDPEVRRRLGEAAVRAAKAVNYVGAG 315
Cdd:pfam02786  82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 116-315 7.35e-42

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 146.94  E-value: 7.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 116 SAAQAIHPGYGF---LSEN----MEFAELCKQEGIIfiGPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLK 188
Cdd:COG0439     7 AAAAELARETGIdavLSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEE--AL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 189 EHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKSFNDDAMLIEKFVDTpRHVEVQVFGdHHGNAVYlf 268
Cdd:COG0439    83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RDGEVVV-- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958749771 269 erdCSVQRRHQK---IIE---EAPAPgIDPEVRRRLGEAAVRAAKAVNYV-GAG 315
Cdd:COG0439   159 ---CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRrGAF 208
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 159-310 9.13e-18

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 82.46  E-value: 9.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 159 KSTSKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfnDD 238
Cdd:COG1181    96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 239 AMLIEKFVDtPRHVEVQVFGDHH-----------GNAVYLFErdcsVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVRAAK 307
Cdd:COG1181   170 KVLVEEFID-GREVTVGVLGNGGpralppieivpENGFYDYE----AKYTDGGTEYICPAR-LPEELEERIQELALKAFR 243


                  ...
gi 1958749771 308 AVN 310
Cdd:COG1181   244 ALG 246
ddl PRK01966
D-alanine--D-alanine ligase;
159-310 2.39e-13

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 70.15  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 159 KSTSKSIMAAAGVPVVEGY--HGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfn 236
Cdd:PRK01966  124 KILTKRLLAAAGIPVAPYVvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------ 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 237 DDAMLIEKFVDtPRHVEVqvfgdhhgnAVYLFERDCSV------------------QRRHQKIIeeaPAPgIDPEVRRRL 298
Cdd:PRK01966  198 DRKVLVEQGIK-GREIEC---------AVLGNDPKASVpgeivkpddfydyeakylDGSAELII---PAD-LSEELTEKI 263

                         170
                  ....*....|..
gi 1958749771 299 GEAAVRAAKAVN 310
Cdd:PRK01966  264 RELAIKAFKALG 275
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 163-313 6.85e-12

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 65.87  E-value: 6.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 163 KSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEKEFQeqlesarrEAKKSFNDDAML 241
Cdd:COG0026    94 KAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGyDGKGQVVIKSAADLE--------AAWAALGGGPCI 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749771 242 IEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHqkIIEE--APApGIDPEVRRRLGEAAVRAAKAVNYVG 313
Cdd:COG0026   164 LEEFVPFERELSVIVARSPDGEVATypVVE---NVHRNG--ILDEsiAPA-RISEALAAEAEEIAKRIAEALDYVG 233
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 165-309 4.14e-11

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 61.56  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 165 IMAAAGVPVV-------EGYHGNDqsDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREakksfnD 237
Cdd:pfam07478   1 LLKAAGLPVVpfvtftrADWKLNP--KEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------D 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958749771 238 DAMLIEKFVDTpRHVEVQVFGDHHGNAVYLFER--DCSVQRRHQKIIEEA-----PApGIDPEVRRRLGEAAVRAAKAV 309
Cdd:pfam07478  73 EKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKAL 149
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 162-310 5.68e-10

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 59.74  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 162 SKSIMAAAGVPVVEGYHGNdqSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARReakksfNDDAML 241
Cdd:PRK01372  102 TKLVWQAAGLPTPPWIVLT--REEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFK------YDDEVL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 242 IEKFVDTpRHVEVQVFGDH--------HGNAVYLFE----RDCSvqrrhQKIIeeaPApGIDPEVRRRLGEAAVRAAKAV 309
Cdd:PRK01372  174 VEKYIKG-RELTVAVLGGKalpvieivPAGEFYDYEakylAGGT-----QYIC---PA-GLPAEIEAELQELALKAYRAL 243


                  .
gi 1958749771 310 N 310
Cdd:PRK01372  244 G 244
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 132-313 1.42e-09

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 58.41  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 132 MEFAELCKQEGIIFIGPPStAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGM 211
Cdd:COG0189    71 LALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD--LRAFLEELGGPVVLKPLDGSGGRGV 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 212 RIIRSEKEFQEQLesarrEAKKSFNDDAMLIEKFVDTPRHVEVQVF--GdhhGNAVYLFER-----DCSVQRRHQKIIEE 284
Cdd:COG0189   148 FLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLvvG---GEPVAAIRRipaegEFRTNLARGGRAEP 219

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958749771 285 APapgIDPEVRrrlgEAAVRAAKAV--NYVG 313
Cdd:COG0189   220 VE---LTDEER----ELALRAAPALglDFAG 243
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 132-313 1.44e-09

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 59.51  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 132 MEFAELCKQEGIIFIGPPSTAI-----RDMgikstSKSIMAAAGVPVVEGYHGNDQsDECLKEhAGKIGYPVMIKAIRGG 206
Cdd:COG0458    88 VELEEAGILEGVKILGTSPDAIdlaedREL-----FKELLDKLGIPQPKSGTATSV-EEALAI-AEEIGYPVIVRPSYVL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 207 GGKGMRIIRSEKEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLferdCSVQrrHqkiIEEA- 285
Cdd:COG0458   161 GGRGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAg 227

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958749771 286 ----------PAPGIDPEVRRRLGEAAVRAAKAVNYVG 313
Cdd:COG0458   228 vhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVG 265
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 163-313 4.60e-09

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 57.47  E-value: 4.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 163 KSIMAAAGVPVVEgYHG-NDQSDecLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEKEFQeqlesarrEAKKSFNDDAM 240
Cdd:PRK06019  105 KQFLDKLGIPVAP-FAVvDSAED--LEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLE--------AAWALLGSVPC 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958749771 241 LIEKFVDTPRHVEVQVFGDHHGNAVY--LFErdcSVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVRAAKAVNYVG 313
Cdd:PRK06019  174 ILEEFVPFEREVSVIVARGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISAELQAQAEEIASRIAEELDYVG 244
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 165-313 1.17e-08

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 56.90  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  165 IMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESArreakkSFNDDAMLIEK 244
Cdd:PRK12815   677 LLDELGLPHVPGLTATDEEE--AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN------ASQLYPILIDQ 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  245 FVDTpRHVEVQVFGDhhGNAVYL---FErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVN 310
Cdd:PRK12815   749 FIDG-KEYEVDAISD--GEDVTIpgiIE--------H---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLG 814


                   ...
gi 1958749771  311 YVG 313
Cdd:PRK12815   815 FRG 817
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 167-313 1.37e-08

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 53.80  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 167 AAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEkefqEQLESARREAKksfnDDAMLIEKF 245
Cdd:pfam02222   1 QKLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGyDGKGQYVVRSE----ADLPQAWEELG----DGPVIVEEF 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958749771 246 VDTPRHVEVQVFGDHHGnAVYLFErdcSVQRRHQK---IIEEAPAPgIDPEVRRRLGEAAVRAAKAVNYVG 313
Cdd:pfam02222  71 VPFDRELSVLVVRSVDG-ETAFYP---VVETIQEDgicRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVG 136
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 163-246 1.20e-07

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 53.62  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 163 KSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRI-IRSEkefqEQLESARREAKKSFNDdaML 241
Cdd:PRK14016  219 KRLLAAAGVPVPEGRVVTSAED--AWEAAEEIGYPVVVKPLDGNHGRGVTVnITTR----EEIEAAYAVASKESSD--VI 290


                  ....*
gi 1958749771 242 IEKFV 246
Cdd:PRK14016  291 VERYI 295
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 147-311 6.37e-07

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 51.39  E-value: 6.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 147 GPPSTAIRDMGIKSTSKSIMAAAGVPVVEGYHGNDQSDecLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLES 226
Cdd:PRK02186   96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAV--ALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 227 ARREAKKSFnddamLIEKFVDTPRHvEVQVFGDHHGNAVylferdCSVQRRHQ-------KIIEEAPAPgIDPEVRRRLG 299
Cdd:PRK02186  174 LRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQV------LGITRKHLgppphfvEIGHDFPAP-LSAPQRERIV 240

                         170
                  ....*....|..
gi 1958749771 300 EAAVRAAKAVNY 311
Cdd:PRK02186  241 RTVLRALDAVGY 252
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 182-313 7.32e-07

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 51.15  E-value: 7.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  182 QSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLEsarrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHH 261
Cdd:TIGR01369  691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGE 766

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749771  262 GNAVY-LFErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNYVG 313
Cdd:TIGR01369  767 EVLIPgIME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKG 819
carB PRK05294
carbamoyl-phosphate synthase large subunit;
191-313 3.90e-05

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 45.86  E-value: 3.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  191 AGKIGYPVMIkaiRGG---GGKGMRIIRSEKEfqeqLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDhhGNAVYL 267
Cdd:PRK05294   700 AEEIGYPVLV---RPSyvlGGRAMEIVYDEEE----LERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLI 770

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  268 ---FErdcsvqrrHqkiIEEA-----------PAPGIDPEVRRRLGEAAVRAAKAVNYVG 313
Cdd:PRK05294   771 ggiME--------H---IEEAgvhsgdsacslPPQTLSEEIIEEIREYTKKLALELNVVG 819
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
 148-315 1.18e-04

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 43.90  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 148 PPSTAIRDMGIKSTSKSIMAAAGVPVVEgyHGNDQSDECLKEHAGKIGYPVMIKAIRGG-GGKGMRIIRSEKEfqeqLES 226
Cdd:PLN02948  111 PKSSTIRIIQDKYAQKVHFSKHGIPLPE--FMEIDDLESAEKAGDLFGYPLMLKSRRLAyDGRGNAVAKTEED----LSS 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 227 ArrEAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAV-Y-LFErdcSVQRRHQKIIEEAPAPgIDPEVRRRLGEAAVR 304
Cdd:PLN02948  185 A--VAALGGFERGLYAEKWAPFVKELAVMVARSRDGSTRcYpVVE---TIHKDNICHVVEAPAN-VPWKVAKLATDVAEK 258

                         170
                  ....*....|.
gi 1958749771 305 AAKAVNyvGAG 315
Cdd:PLN02948  259 AVGSLE--GAG 267
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 87-265 2.30e-04

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 43.06  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771   87 MADEAYsIGPAPSQqsylAMEKIIQVAKssaAQAIHPGYG---FLSENMEFAEL--CKQEGIIFIGPPSTAIRDMGIKST 161
Cdd:TIGR01369   59 MADKVY-IEPLTPE----AVEKIIEKER---PDAILPTFGgqtALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDREL 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  162 SKSIMAAAGVPVVEGYHGNDQsDECLkEHAGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKKsfndDAML 241
Cdd:TIGR01369  131 FREAMKEIGEPVPESEIAHSV-EEAL-AAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVL 204

                          170       180
                   ....*....|....*....|....
gi 1958749771  242 IEKFVDTPRHVEVQVFGDHHGNAV 265
Cdd:TIGR01369  205 VEKSLAGWKEIEYEVMRDSNDNCI 228
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 135-247 8.55e-04

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439921 [Multi-domain]  Cd Length: 422  Bit Score: 41.15  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 135 AELCKQEGI--IFIGP--P-----STAIRDMGI---------------KSTSKSIMAAAGVPVVEgYHGNDQSDEClKEH 190
Cdd:COG0151    55 VAFAKEENIdlVVVGPeaPlvagiVDAFRAAGIpvfgpskaaaqlegsKAFAKEFMARYGIPTAA-YRVFTDLEEA-LAY 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958749771 191 AGKIGYPVMIKAIRGGGGKGMRIIRSEKEfqeqlesARREAKKSFNDDAM-------LIEKFVD 247
Cdd:COG0151   133 LEEQGAPIVVKADGLAAGKGVVVAETLEE-------ALAAVDDMLADGKFgdagarvVIEEFLE 189
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 87-314 1.31e-03

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 40.25  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771  87 MADEAYSIgpaPSQQSYLAMEKIIQVAKSSAAQAIHPGY----GFLSENM-EFAElckqEGIIFIGPPSTAIRDMGIKST 161
Cdd:PRK12767   42 FADKFYVV---PKVTDPNYIDRLLDICKKEKIDLLIPLIdpelPLLAQNRdRFEE----IGVKVLVSSKEVIEICNDKWL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 162 SKSIMAAAGVPVVEGYHGNDQSDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEkefqEQLESARREAKKsfnddaML 241
Cdd:PRK12767  115 TYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDK----EELEFLLEYVPN------LI 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958749771 242 IEKFVDTPRhVEVQVFGDHHGNAVylferdCSVQRRHQKIIEEAPAPGI---DPEVRrrlgEAAVRAAKAVNYVGA 314
Cdd:PRK12767  185 IQEFIEGQE-YTVDVLCDLNGEVI------SIVPRKRIEVRAGETSKGVtvkDPELF----KLAERLAEALGARGP 249
PurT COG0027
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ...
 187-247 2.66e-03

Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439798 [Multi-domain]  Cd Length: 393  Bit Score: 39.34  E-value: 2.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958749771 187 LKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEkefqEQLESARREAKKS--FNDDAMLIEKFVD 247
Cdd:COG0027   141 LRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----ADIEAAWEYAQEGgrGGAGRVIVEGFVD 199
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 194-267 3.04e-03

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 38.03  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958749771 194 IGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARRE--------AKKSFNDDAMLIEKFVDTPrHVEVQVFGDHHGNAV 265
Cdd:pfam13535   1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEieqwkemyPEAVVDGGSFLVEEYIEGE-EFAVDAYFDENGEPV 79


                  ..
gi 1958749771 266 YL 267
Cdd:pfam13535  80 IL 81
PLN02735 PLN02735
carbamoyl-phosphate synthase
 191-265 4.55e-03

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 38.99  E-value: 4.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958749771  191 AGKIGYPVMIKAIRGGGGKGMRIIRSEKEFQEQLESARREAKksfnDDAMLIEKFVDTPRHVEVQVFGDHHGNAV 265
Cdd:PLN02735   733 AKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDP----ERPVLVDKYLSDATEIDVDALADSEGNVV 803
purT PRK09288
formate-dependent phosphoribosylglycinamide formyltransferase;
183-233 5.55e-03

formate-dependent phosphoribosylglycinamide formyltransferase;


Pssm-ID: 236454 [Multi-domain]  Cd Length: 395  Bit Score: 38.58  E-value: 5.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958749771 183 SDECLKEHAGKIGYPVMIKAIRGGGGKGMRIIRSEkefqEQLESARREAKK 233
Cdd:PRK09288  137 SLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSP----EDIEKAWEYAQE 183
 
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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