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Conserved domains on  [gi|446515525|ref|WP_000592871|]
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MULTISPECIES: acetyl-CoA carboxylase biotin carboxylase subunit [Bacillus]

Protein Classification

acetyl-CoA carboxylase biotin carboxylase subunit( domain architecture ID 11483369)

acetyl-CoA carboxylase biotin carboxylase subunit catalyzes the carboxylation of the carrier protein

EC:  6.-.-.-
Gene Ontology:  GO:0005524|GO:0016874
PubMed:  18725455|21592965

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


:

Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 884.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEYkTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEK-NGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 884.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEYkTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEK-NGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-445 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 843.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:COG4770  161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEyKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:COG4770  241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVD-ADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:COG4770  320 PLPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:COG4770  400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERE 444
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-446 0e+00

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: 750.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEYKtKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN-GEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 446515525  401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEHE 446
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKL 445
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 116-323 3.13e-84

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: 257.23  E-value: 3.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  116 KDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKATAGGGGKGIRVARHEEELIKGIQITQQEASTAFGNP 195
Cdd:pfam02786   2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  196 GVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLEESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVE 275
Cdd:pfam02786  82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446515525  276 FIYEYKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGEKLS 323
Cdd:pfam02786 162 FALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 337-443 1.52e-68

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 213.04  E-value: 1.52e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   337 ECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEAIAKMKRALSEFVIEGV 416
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*..
gi 446515525   417 HTTIPFHLQLLDHPDFVKGEFNTKFLE 443
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 884.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEYkTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEK-NGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-445 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 843.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:COG4770    1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:COG4770   81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:COG4770  161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEyKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:COG4770  241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVD-ADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:COG4770  320 PLPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:COG4770  400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERE 444
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-446 0e+00

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: 750.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEYKtKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN-GEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 446515525  401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEHE 446
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKL 445
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1-446 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 699.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:PRK08654   1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:PRK08654  81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEykTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGE 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:PRK08654 319 ELSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEHE 446
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEET 444
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1-444 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 692.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:PRK05586   1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:PRK05586  81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEyKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEE 444
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 664.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:PRK06111   1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:PRK06111  81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEyKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPaKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEA 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:PRK06111 399 ISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQ 443
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 1-449 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 627.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISK-ESYLNLTNIISVAKLTGCDAIH 79
Cdd:PRK12999    4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   80 PGYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKA 159
Cdd:PRK12999   84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  160 TAGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLL 239
Cdd:PRK12999  164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  240 EESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEYKTKtFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASG 319
Cdd:PRK12999  244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGN-FYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  320 EKLS------LQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDS-AVYPGYSIPPFYDSMVAKLIV 392
Cdd:PRK12999  323 ATLHdleigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTA 402

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446515525  393 HGKTREEAIAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH-ELVT 449
Cdd:PRK12999  403 WGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETpELFD 460
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1-447 0e+00

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: 613.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVG----PTiskESYLNLTNIISVAKLTGCD 76
Cdd:COG1038     3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGegkgPV---DAYLDIEEIIRVAKEKGVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   77 AIHPGYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVI 156
Cdd:COG1038    80 AIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  157 IKATAGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQ 236
Cdd:COG1038   160 LKAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  237 KLLEESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEyKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILV 316
Cdd:COG1038   240 KVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVD-DDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  317 ASGEKLS------LQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSA-VYPGYSIPPFYDSMVAK 389
Cdd:COG1038   319 AEGYSLDdpeigiPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGnAYTGAVITPYYDSLLVK 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446515525  390 LIVHGKTREEAIAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH-EL 447
Cdd:COG1038   399 VTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETpEL 457
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 606.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTiSKESYLNLTNIISVAKLTGCDAIHP 80
Cdd:PRK07178   1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD-PLAGYLNPRRLVNLAVETGCDALHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKAT 160
Cdd:PRK07178  80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 161 AGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLE 240
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 241 ESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEyKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGE 320
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 321 KLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEA 400
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 446515525 401 IAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESH 443
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 2-443 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 579.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   2 IKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHPG 81
Cdd:PRK12833   5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  82 YGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKATA 161
Cdd:PRK12833  85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 162 GGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHgNAIHLGERDCTIQRRLQKLLEE 241
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 242 SPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEYKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGEK 321
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 322 LSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEAI 401
Cdd:PRK12833 324 LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 446515525 402 AKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLE 443
Cdd:PRK12833 404 ARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
2-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 573.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   2 IKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHPG 81
Cdd:PRK08462   4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  82 YGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKATA 161
Cdd:PRK08462  84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 162 GGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLEE 241
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 242 SPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEyKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGEK 321
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 322 LsLQQEEVQFNGWAIECRINAENPaKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEAI 401
Cdd:PRK08462 323 L-PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAI 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 446515525 402 AKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:PRK08462 401 AKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-445 0e+00

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 523.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   1 MIKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKeSYLNLTNIISVAKLTGCDAIHP 80
Cdd:PRK08463   1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  81 GYGFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSQGIIKNTEEAI-ELANQIGYPVIIKA 159
Cdd:PRK08463  80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIkIFARKIGYPVILKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 160 TAGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLL 239
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 240 EESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEyKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASG 319
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 320 EKLSLQQEEVQFNGWAIECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREE 399
Cdd:PRK08463 319 EILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 446515525 400 AIAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLEEH 445
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETH 444
urea_carbox TIGR02712
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ...
 3-443 4.94e-177

urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 274264 [Multi-domain]  Cd Length: 1201  Bit Score: 527.29  E-value: 4.94e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525     3 KKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHPGY 82
Cdd:TIGR02712    2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    83 GFLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGSqGIIKNTEEAIELANQIGYPVIIKATAG 162
Cdd:TIGR02712   82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT-GLLSSLDEALEAAKEIGYPVMLKSTAG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   163 GGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLEES 242
Cdd:TIGR02712  161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   243 PSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIYEYKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGEKL 322
Cdd:TIGR02712  241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   323 SLQQ--EEVQFNGWAIECRINAENPAKKFMPSPGK-VEMYLPPggfGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREE 399
Cdd:TIGR02712  321 DFASlnISLTPRGAAIEARVYAENPAKNFQPSPGLlTDVQFPD---DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 446515525   400 AIAKMKRALSEFVIEGVHTTIPFHLQLLDHPDFVKGEFNTKFLE 443
Cdd:TIGR02712  398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLN 441
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 116-323 3.13e-84

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: 257.23  E-value: 3.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  116 KDVARDTMKEAGVPIVPGSQGIIKNTEEAIELANQIGYPVIIKATAGGGGKGIRVARHEEELIKGIQITQQEASTAFGNP 195
Cdd:pfam02786   2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  196 GVYLEKYVEDFRHVEIQIMADTHGNAIHLGERDCTIQRRLQKLLEESPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVE 275
Cdd:pfam02786  82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446515525  276 FIYEYKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQILVASGEKLS 323
Cdd:pfam02786 162 FALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 337-443 1.52e-68

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 213.04  E-value: 1.52e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   337 ECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEAIAKMKRALSEFVIEGV 416
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*..
gi 446515525   417 HTTIPFHLQLLDHPDFVKGEFNTKFLE 443
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 337-444 2.28e-67

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 426981 [Multi-domain]  Cd Length: 108  Bit Score: 210.43  E-value: 2.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  337 ECRINAENPAKKFMPSPGKVEMYLPPGGFGIRVDSAVYPGYSIPPFYDSMVAKLIVHGKTREEAIAKMKRALSEFVIEGV 416
Cdd:pfam02785   1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80

                          90       100
                  ....*....|....*....|....*...
gi 446515525  417 HTTIPFHLQLLDHPDFVKGEFNTKFLEE 444
Cdd:pfam02785  81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 2-109 2.47e-67

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: 210.04  E-value: 2.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    2 IKKVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCVGPTISKESYLNLTNIISVAKLTGCDAIHPG 81
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 446515525   82 YGFLAENADFAELCRECNLIFIGPSPEA 109
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 69-321 2.57e-57

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: 189.70  E-value: 2.57e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  69 VAKLTGCDAIhpgygfLAENAD----FAELCRECNLIfiGPSPEAISKMGTKDVARDTMKEAGVPiVPGSQgIIKNTEEA 144
Cdd:COG0439   12 LARETGIDAV------LSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGFA-LVDSPEEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 145 IELANQIGYPVIIKATAGGGGKGIRVARHEEELIKGIQITQQEASTAFGNPGVYLEKYVEDfRHVEIQIMADtHGNAIHl 224
Cdd:COG0439   82 LAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR-DGEVVV- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 225 gerdCTIQRRLQK------LLEESPSPaLDEEIRKQMGEAAVKAAVAVDY-TGAGTVEFIYEyKTKTFYFMEMNTRIQVE 297
Cdd:COG0439  159 ----CSITRKHQKppyfveLGHEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLT-PDGEPYLIEINARLGGE 232

                        250       260
                 ....*....|....*....|....*.
gi 446515525 298 H--PVTEMVTGMDLIKEQILVASGEK 321
Cdd:COG0439  233 HipPLTELATGVDLVREQIRLALGEP 258
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 14-322 1.43e-12

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: 70.03  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    14 AVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYcvgptISKESYLNLTNIISVAKLTGCdAIHPGyGFLAENAdfAE 93
Cdd:TIGR01369  577 CVHAVLALRELGYETIMINYNPETVSTDYDTSDRLY-----FEPLTFEDVMNIIELEKPEGV-IVQFG-GQTPLNL--AK 647

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    94 LCRECNLIFIGPSPEAIskmgtkDVARD------TMKEAGVPIVPGsqGIIKNTEEAIELANQIGYPVIIKATAGGGGKG 167
Cdd:TIGR01369  648 ALEEAGVPILGTSPESI------DRAEDrekfseLLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRA 719

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   168 IRVARHEEELIKGIqitqQEASTAFGNPGVYLEKYVEDFRHVEIQIMADtHGNA-------------IHLGERDCTIqrr 234
Cdd:TIGR01369  720 MEIVYNEEELRRYL----EEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVlipgimehieeagVHSGDSTCVL--- 791

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   235 lqklleesPSPALDEEIRKQMGEAAVKAAVAVDYTGAGTVEFIyeYKTKTFYFMEMNTRIQVEHPVTEMVTGMDLIKEQI 314
Cdd:TIGR01369  792 --------PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFA--VKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAV 861


                   ....*...
gi 446515525   315 LVASGEKL 322
Cdd:TIGR01369  862 RVMLGKKL 869
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 2-222 9.73e-12

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: 67.33  E-value: 9.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525     2 IKKVLIANRGEIAV-----------RIIRACKEMDIETVAIYS-----EADKEslhvqIADEAYCVGPTISkesylNLTN 65
Cdd:TIGR01369    6 IKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSnpatiMTDPE-----MADKVYIEPLTPE-----AVEK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    66 IISVAKLtgcDAIHPGYG-----FLAENADFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPiVPGSQgIIKN 140
Cdd:TIGR01369   76 IIEKERP---DAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEP-VPESE-IAHS 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   141 TEEAIELANQIGYPVIIKATAGGGGKGIRVARHEEELIKgiqITQQeASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGN 220
Cdd:TIGR01369  151 VEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKE---IAER-ALSASPINQVLVEKSLAGWKEIEYEVMRDSNDN 226


                   ..
gi 446515525   221 AI 222
Cdd:TIGR01369  227 CI 228
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
4-294 1.76e-11

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 65.33  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   4 KVLIANRGEIAVRIIRACKEMDIETVAIYSEADKESLHVQIADEA-YCVGPTISKESYLNltNIISVAKLTGCDAIHPGY 82
Cdd:COG3919    7 RVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVvVVPDPGDDPEAFVD--ALLELAERHGPDVLIPTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  83 ----GFLAENADfaELCRecNLIFIGPSPEAISKMGTKDVARDTMKEAGVPiVPGSQgIIKNTEEAIELANQIGYPVIIK 158
Cdd:COG3919   85 deyvELLSRHRD--ELEE--HYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTV-VLDSADDLDALAEDLGFPVVVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 159 AT--------AGGGGKGIRVARHEEELIKGIqitqqEASTAFGNPGVyLEKYVEDFRHVEIQIMA--DTHGNAIHLgerd 228
Cdd:COG3919  159 PAdsvgydelSFPGKKKVFYVDDREELLALL-----RRIAAAGYELI-VQEYIPGDDGEMRGLTAyvDRDGEVVAT---- 228

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515525 229 CTIQRRLQK--------LLEESPSPALDEEIRKQMGEAavkaavavDYTGAGTVEFIYEYKTKTFYFMEMNTRI 294
Cdd:COG3919  229 FTGRKLRHYppaggnsaARESVDDPELEEAARRLLEAL--------GYHGFANVEFKRDPRDGEYKLIEINPRF 294
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 103-222 6.19e-10

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: 61.05  E-value: 6.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 103 IGPSPEAIskmgtkDVA------RDTMKEAGVPIVPGsqGIIKNTEEAIELANQIGYPVIIKA------TAGgggkgiRV 170
Cdd:COG0458  102 LGTSPDAI------DLAedrelfKELLDKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPsyvlggRGM------GI 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446515525 171 ARHEEELIKGIqitqQEASTAFGNPGVYLEKYVEDFRHVEIQIMADTHGNAI 222
Cdd:COG0458  168 VYNEEELEEYL----ERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVI 215
carB PRK05294
carbamoyl-phosphate synthase large subunit;
97-222 7.46e-09

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 58.18  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   97 ECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPiVPGSqGIIKNTEEAIELANQIGYPVIikataggggkgIR------- 169
Cdd:PRK05294  110 KYGVELIGAKLEAIDKAEDRELFKEAMKKIGLP-VPRS-GIAHSMEEALEVAEEIGYPVI-----------IRpsftlgg 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446515525  170 ----VARHEEELI----KGIQ---ITQqeastafgnpgVYLEKYVEDFRHVEIQIMADTHGNAI 222
Cdd:PRK05294  177 tgggIAYNEEELEeiveRGLDlspVTE-----------VLIEESLLGWKEYEYEVMRDKNDNCI 229
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 103-222 4.22e-07

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 52.66  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  103 IGPSPEAISKMGTKDVARDTMKEAGVPIvpGSQGIIKNTEEAIELANQIGYPVIIKATAGGGGKGIRVARHEEELIKgiQ 182
Cdd:PRK12815  116 LGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQ--L 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446515525  183 ITQQEASTAFGNpgVYLEKYVEDFRHVEIQIMADTHGNAI 222
Cdd:PRK12815  192 FKQGLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCI 229
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 108-207 2.98e-05

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 46.30  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 108 EAIS--KMGTKDVardtMKEAGVPiVPgSQGIIKNTEEAIELANQIGYPVIIKAtaggggkgiRVARHEeeliKGIQI-- 183
Cdd:PRK14016 209 VDIAcdKELTKRL----LAAAGVP-VP-EGRVVTSAEDAWEAAEEIGYPVVVKP---------LDGNHG----RGVTVni 269

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446515525 184 -TQQEASTAFGN-----PGVYLEKYVE--DFR 207
Cdd:PRK14016 270 tTREEIEAAYAVaskesSDVIVERYIPgkDHR 301
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 3-157 3.17e-05

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 46.50  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525    3 KKVLIANRGEI-----------AVRIIRACKEMDIETVAIYSEADKESLHVQIADEAYCvgptiskESyLNLTNIISVAK 71
Cdd:PRK12815  556 KKVLILGSGPIrigqgiefdysSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYF-------EP-LTLEDVLNVAE 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   72 LTGCDAIHPGYGFLAENAdFAELCRECNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPGsqGIIKNTEEAIELANQI 151
Cdd:PRK12815  628 AENIKGVIVQFGGQTAIN-LAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRI 704


                  ....*.
gi 446515525  152 GYPVII 157
Cdd:PRK12815  705 GYPVLI 710
PLN02735 PLN02735
carbamoyl-phosphate synthase
 104-231 9.62e-05

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 45.15  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  104 GPSPEAISKMGTKDVARDTMKEAGVPIVPGsqGIIKNTEEAIELANQIGYPVIIKATAGGGGKGIRVARHEEELIKGIQI 183
Cdd:PLN02735  691 GTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLET 768

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446515525  184 TQQEastafgNPG--VYLEKYVEDFRHVEIQIMADTHGN-------------AIHLGERDCTI 231
Cdd:PLN02735  769 AVEV------DPErpVLVDKYLSDATEIDVDALADSEGNvviggimehieqaGVHSGDSACSL 825
carB PRK05294
carbamoyl-phosphate synthase large subunit;
103-157 2.25e-04

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 43.93  E-value: 2.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515525  103 IGPSPEAIskmgtkDVARD------TMKEAGVPIVPGsqGIIKNTEEAIELANQIGYPVII 157
Cdd:PRK05294  657 LGTSPDAI------DLAEDrerfskLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLV 709
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 74-276 3.93e-04

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: 42.37  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  74 GCDAIhpGYGFlaENADF---AELCRECNLIfigPSPEAISkmgtkdVARD--TMK----EAGVPIVPGSqgIIKNTEEA 144
Cdd:COG0026   52 RCDVV--TFEF--ENVPAealEALEAEVPVR---PGPEALE------IAQDrlLEKaflaELGIPVAPFA--AVDSLEDL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 145 IELANQIGYPVIIKATaggggkgiR---------VARHEEELikgiqitqQEASTAFGNPGVYLEKYVeDFRHvEIQIMA 215
Cdd:COG0026  117 EAAIAELGLPAVLKTR--------RggydgkgqvVIKSAADL--------EAAWAALGGGPCILEEFV-PFER-ELSVIV 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446515525 216 --DTHGNAIH--LGErdcTIQRrlQKLLEESPSPA-LDEEIRKQMGEAAVKAAVAVDYTGAGTVEF 276
Cdd:COG0026  179 arSPDGEVATypVVE---NVHR--NGILDESIAPArISEALAAEAEEIAKRIAEALDYVGVLAVEF 239
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
119-159 1.62e-03

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 40.88  E-value: 1.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446515525 119 ARDTMKEAGVPIVPGsqGIIKNTEEAIELANQIGYPVIIKA 159
Cdd:COG1042  493 AKALLAAYGIPVVPT--RLARSAEEAVAAAEEIGYPVVLKI 531
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 20-215 2.56e-03

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 39.75  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  20 ACKEMDIEtVAIYSEaDKESLHVQIADEAYCvgptiskESYLNLTNIISVAKltGCDAIhpGYGFlaENADFAELCRECN 99
Cdd:PRK06019  20 AAAPLGYK-VIVLDP-DPDSPAAQVADEVIV-------ADYDDVAALRELAE--QCDVI--TYEF--ENVPAEALDALAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525 100 LIFIGPSPEAISkmgtkdVARD--TMK----EAGVPIVPGSqgIIKNTEEAIELANQIGYPVIIKATaggggkgiR---- 169
Cdd:PRK06019  85 RVPVPPGPDALA------IAQDrlTEKqfldKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTR--------Rggyd 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446515525 170 -----VARHEEELikgiqitqQEASTAFGNPGVYLEKYVeDFRHvEIQIMA 215
Cdd:PRK06019 149 gkgqwVIRSAEDL--------EAAWALLGSVPCILEEFV-PFER-EVSVIV 189
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 124-215 3.17e-03

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: 38.39  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  124 KEAGVPiVPGSQgIIKNTEEAIELANQIGYPVIIKA-TAGGGGKGIRVARHEEELikgiqitqQEASTAFGNPGVYLEKY 202
Cdd:pfam02222   1 QKLGLP-TPRFM-AAESLEELIEAGQELGYPCVVKArRGGYDGKGQYVVRSEADL--------PQAWEELGDGPVIVEEF 70

                          90
                  ....*....|...
gi 446515525  203 VeDFRhVEIQIMA 215
Cdd:pfam02222  71 V-PFD-RELSVLV 81
PLN02735 PLN02735
carbamoyl-phosphate synthase
 76-222 4.59e-03

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 39.38  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525   76 DAIHPGYG---------FLAENADFAELcrecNLIFIGPSPEAISKMGTKDVARDTMKEAGVPIVPgsQGIIKNTEEAIE 146
Cdd:PLN02735  100 DALLPTMGgqtalnlavALAESGILEKY----GVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTLDECFE 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446515525  147 LANQIG-YPVIIKATAGGGGKGIRVARHEEELiKGIQITQQEASTafgNPGVYLEKYVEDFRHVEIQIMADTHGNAI 222
Cdd:PLN02735  174 IAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEF-ETICKAGLAASI---TSQVLVEKSLLGWKEYELEVMRDLADNVV 246
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 45-177 5.74e-03

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 38.71  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446515525  45 ADEAYcVGPTISKESYLNltNIISVAKLTGCDAIHPGY----GFLAENAD-FAELcrecNLIFIGPSPEAISKMGTKDVA 119
Cdd:PRK12767  43 ADKFY-VVPKVTDPNYID--RLLDICKKEKIDLLIPLIdpelPLLAQNRDrFEEI----GVKVLVSSKEVIEICNDKWLT 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446515525 120 RDTMKEAGVPiVPGSqgIIKNTEEAIELA---NQIGYPVIIKATAGGGGKGIRVARHEEEL 177
Cdd:PRK12767 116 YEFLKENGIP-TPKS--YLPESLEDFKAAlakGELQFPLFVKPRDGSASIGVFKVNDKEEL 173
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 127-158 6.79e-03

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


Pssm-ID: 463918 [Multi-domain]  Cd Length: 221  Bit Score: 37.84  E-value: 6.79e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446515525  127 GVPIVPgsQGIIKNTEEAIELANQIGYPVIIK 158
Cdd:pfam13549  23 GIPVVP--TRLARSPEEAVAAAEEIGYPVVLK 52
 
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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