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Conserved domains on  [gi|579671149|gb|EUX15571|]
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acetyl-CoA carboxylase, biotin carboxylase subunit [Staphylococcus aureus M0321]

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
 1-451 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


:

Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 889.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:PRK08591   2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:PRK08591  82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNdNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKN-GEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 579671149 401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQNSIMNDEG 451
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-451 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 889.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:PRK08591   2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:PRK08591  82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNdNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKN-GEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 579671149 401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQNSIMNDEG 451
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-444 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 825.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:COG4770    2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:COG4770   82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:COG4770  162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNkFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:COG4770  242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN-FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:COG4770  321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 579671149 401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQN 444
Cdd:COG4770  401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERE 444
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-448 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: 696.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNdNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN-GEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 579671149  401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQNSIMN 448
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMG 448
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 115-322 1.26e-91

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: 276.11  E-value: 1.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  115 KDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNG 194
Cdd:pfam02786   2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  195 GLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEAPSPILDDETRREMGNAAVRAAKAVNYENAGTIE 274
Cdd:pfam02786  82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 579671149  275 FIYDLNDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDVLP 322
Cdd:pfam02786 162 FALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-442 1.26e-56

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: 182.61  E-value: 1.26e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   336 EFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIMAGIRALSEFVVLGI 415
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*..
gi 579671149   416 DTTIPFHIKLLNNDIFRSGKFNTNFLE 442
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-451 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 889.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:PRK08591   2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:PRK08591  82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNdNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKN-GEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 579671149 401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQNSIMNDEG 451
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-444 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 825.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:COG4770    2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:COG4770   82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:COG4770  162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNkFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:COG4770  242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN-FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:COG4770  321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 579671149 401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQN 444
Cdd:COG4770  401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERE 444
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-448 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: 696.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNdNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN-GEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 579671149  401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQNSIMN 448
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMG 448
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
2-444 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 684.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   2 KKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPGY 81
Cdd:PRK08654   3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  82 GFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAG 161
Cdd:PRK08654  83 GFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 162 GGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEA 241
Cdd:PRK08654 163 GGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 242 PSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDlnDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDVL 321
Cdd:PRK08654 243 PSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 322 PYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIM 401
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIA 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 579671149 402 AGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQN 444
Cdd:PRK08654 401 RMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEE 443
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
2-444 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 668.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   2 KKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPGY 81
Cdd:PRK05586   3 KKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  82 GFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAG 161
Cdd:PRK05586  83 GFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 162 GGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEA 241
Cdd:PRK05586 163 GGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 242 PSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNkFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDVL 321
Cdd:PRK05586 243 PSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGN-FYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 322 PYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIM 401
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQ 401

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 579671149 402 AGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQN 444
Cdd:PRK05586 402 KMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 2-443 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 655.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   2 KKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPGY 81
Cdd:PRK06111   3 QKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  82 GFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAG 161
Cdd:PRK06111  83 GLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 162 GGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEA 241
Cdd:PRK06111 163 GGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 242 PSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDlNDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDVL 321
Cdd:PRK06111 243 PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 322 PYKQEDIKLTGHAIEFRINAENPyKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIM 401
Cdd:PRK06111 322 SFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAIS 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 579671149 402 AGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQ 443
Cdd:PRK06111 401 RLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 1-444 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 609.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSK-DSYLNIPNILSIATSTGCDGVHP 79
Cdd:PRK12999    5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVDAIHP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   80 GYGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKAT 159
Cdd:PRK12999   85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKAS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  160 AGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVE 239
Cdd:PRK12999  165 AGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  240 EAPSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDlNDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMG- 318
Cdd:PRK12999  245 IAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVD-ADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGa 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  319 -----DVLPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIES-ACYTNYTIPPYYDSMVAKLIIH 392
Cdd:PRK12999  324 tlhdlEIGIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTAW 403

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 579671149  393 EPTRDEAIMAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQN 444
Cdd:PRK12999  404 GRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDET 455
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-442 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 609.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTlSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:PRK07178   2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD-PLAGYLNPRRLVNLAVETGCDALHPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:PRK07178  81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDlNDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:PRK07178 320 LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEAL 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 579671149 401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLE 442
Cdd:PRK07178 400 DRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE 441
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
1-444 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 599.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:PRK08462   4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:PRK08462  84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE 240
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNkFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD-FYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 321 LPyKQEDIKLTGHAIEFRINAENPyKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:PRK08462 323 LP-SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAI 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 579671149 401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQN 444
Cdd:PRK08462 401 AKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1-444 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: 598.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSK-DSYLNIPNILSIATSTGCDGVHP 79
Cdd:COG1038     4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDAIHP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   80 GYGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKAT 159
Cdd:COG1038    84 GYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  160 AGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVE 239
Cdd:COG1038   164 AGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  240 EAPSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDlNDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGD 319
Cdd:COG1038   244 IAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVD-DDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  320 VLP------YKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRI-ESACYTNYTIPPYYDSMVAKLIIH 392
Cdd:COG1038   323 SLDdpeigiPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLdGGNAYTGAVITPYYDSLLVKVTAW 402

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 579671149  393 EPTRDEAIMAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQN 444
Cdd:COG1038   403 GRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDET 454
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 1-443 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 578.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPG 80
Cdd:PRK12833   5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATA 160
Cdd:PRK12833  85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 161 GGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYgNVIHLGERDCTIQRRMQKLVEE 240
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 241 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDV 320
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 321 LPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAI 400
Cdd:PRK12833 324 LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 579671149 401 MAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQ 443
Cdd:PRK12833 404 ARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEA 446
urea_carbox TIGR02712
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ...
 2-443 0e+00

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: 543.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149     2 KKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPGY 81
Cdd:TIGR02712    2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    82 GFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSdGLMKDVSEAKKIAKKIGYPVIIKATAG 161
Cdd:TIGR02712   82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT-GLLSSLDEALEAAKEIGYPVMLKSTAG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   162 GGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEA 241
Cdd:TIGR02712  161 GGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEET 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   242 PSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDVL 321
Cdd:TIGR02712  241 PAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   322 PYKQEDIKLT--GHAIEFRINAENPYKNFMPSPGKIEQYLAPGgyGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEA 399
Cdd:TIGR02712  321 DFASLNISLTprGAAIEARVYAENPAKNFQPSPGLLTDVQFPD--DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDREDA 398

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 579671149   400 IMAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQ 443
Cdd:TIGR02712  399 ILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNS 442
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-444 0e+00

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 521.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKdSYLNIPNILSIATSTGCDGVHPG 80
Cdd:PRK08463   2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  81 YGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGSDGLMKD-VSEAKKIAKKIGYPVIIKAT 159
Cdd:PRK08463  81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSEsMEEIKIFARKIGYPVILKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 160 AGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVE 239
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 240 EAPSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNdNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGD 319
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDY-NRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 320 VLPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEA 399
Cdd:PRK08463 320 ILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 579671149 400 IMAGIRALSEFVVLGIDTTIPFHIKLLNNDIFRSGKFNTNFLEQN 444
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETH 444
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 115-322 1.26e-91

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: 276.11  E-value: 1.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  115 KDVAKAEMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNG 194
Cdd:pfam02786   2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  195 GLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEEAPSPILDDETRREMGNAAVRAAKAVNYENAGTIE 274
Cdd:pfam02786  82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 579671149  275 FIYDLNDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDVLP 322
Cdd:pfam02786 162 FALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 61-319 1.53e-66

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: 213.97  E-value: 1.53e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  61 NIPNILS----IATSTGCDGVhpgygfLAENAD----FAELCEAcqLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVvPG 132
Cdd:COG0439    1 DIDAIIAaaaeLARETGIDAV------LSESEFavetAAELAEE--LGLPGPSPEAIRAMRDKVLMREALAAAGVPV-PG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 133 SDGLmKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGFRMTEQEAQTAFGNGGLYMEKFIENfRHIEIQI 212
Cdd:COG0439   72 FALV-DSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 213 VGDsYGNVIHlgerdCTIQRRMQK---LVE---EAPSPiLDDETRREMGNAAVRAAKAVNYEN-AGTIEFIYDlNDNKFY 285
Cdd:COG0439  150 LVR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLT-PDGEPY 221

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 579671149 286 FMEMNTRIQVEH--PVTEMVTGIDLVKLQLQVAMGD 319
Cdd:COG0439  222 LIEINARLGGEHipPLTELATGVDLVREQIRLALGE 257
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 2-105 8.28e-61

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: 193.47  E-value: 8.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    2 KKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYLNIPNILSIATSTGCDGVHPGY 81
Cdd:pfam00289   2 KKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGY 81

                          90       100
                  ....*....|....*....|....
gi 579671149   82 GFLAENADFAELCEACQLKFIGPS 105
Cdd:pfam00289  82 GFLSENAEFARACEEAGIIFIGPS 105
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-442 1.26e-56

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: 182.61  E-value: 1.26e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   336 EFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIMAGIRALSEFVVLGI 415
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*..
gi 579671149   416 DTTIPFHIKLLNNDIFRSGKFNTNFLE 442
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-443 3.11e-55

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: 178.84  E-value: 3.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  336 EFRINAENPYKNFMPSPGKIEQYLAPGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIMAGIRALSEFVVLGI 415
Cdd:pfam02785   1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80

                          90       100
                  ....*....|....*....|....*...
gi 579671149  416 DTTIPFHIKLLNNDIFRSGKFNTNFLEQ 443
Cdd:pfam02785  81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 13-318 5.10e-14

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: 74.65  E-value: 5.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    13 AVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCvgptlskdSYLNIPNILSIATSTGCDG--VHPGyGFLAENAdf 90
Cdd:TIGR01369  577 CVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYF--------EPLTFEDVMNIIELEKPEGviVQFG-GQTPLNL-- 645

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    91 AELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGsdGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVA 170
Cdd:TIGR01369  646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   171 RDEKELETGFRmteqEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSyGNVIHLGerdctiqrrMQKLVEEA--------- 241
Cdd:TIGR01369  724 YNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDG-EEVLIPG---------IMEHIEEAgvhsgdstc 789

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579671149   242 --PSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDlnDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMG 318
Cdd:TIGR01369  790 vlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK--DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLG 866
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 75-328 8.07e-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: 67.72  E-value: 8.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149    75 DGVHPGYG-----FLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGsdGLMKDVSEAKKIAKK 149
Cdd:TIGR01369   83 DAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSVEEALAAAKE 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   150 IGYPVIIKATAGGGGKGIRVARDEKEL----ETGFRMTEQeaqtafgnGGLYMEKFIENFRHIEIQIVGDSYGNVI---- 221
Cdd:TIGR01369  161 IGYPVIVRPAFTLGGTGGGIAYNREELkeiaERALSASPI--------NQVLVEKSLAGWKEIEYEVMRDSNDNCItvcn 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   222 ---------HLGERDCTiqrrmqklveeAPSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTR 292
Cdd:TIGR01369  233 menfdpmgvHTGDSIVV-----------APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPR 301

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 579671149   293 IQVEHPVTEMVTGIDLVKLQLQVAMGDVLPYKQEDI 328
Cdd:TIGR01369  302 VSRSSALASKATGYPIAKVAAKLAVGYTLDELKNPV 337
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 92-331 9.22e-12

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: 66.83  E-value: 9.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  92 ELCEACQL---KFIGPSYQSIQKmgikdvakAE--------MIKANVPVVPGsdGLMKDVSEAKKIAKKIGYPVIIKA-- 158
Cdd:COG0458   89 ELEEAGILegvKILGTSPDAIDL--------AEdrelfkelLDKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPsy 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 159 ----TAGgggkgiRVARDEKELETGFRmteqEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNV-------------I 221
Cdd:COG0458  159 vlggRGM------GIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNViivgimehiepagV 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 222 HLGERDCTiqrrmqklveeAPSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIydLNDNKFYFMEMNTRiqvehpVTE 301
Cdd:COG0458  229 HSGDSICV-----------APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFA--VDDGRVYVIEVNPR------ASR 289

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 579671149 302 MV------TGIDLVKLQLQVAMGdvlpYKQEDIKLT 331
Cdd:COG0458  290 SSpfaskaTGYPIAKIAAKLALG----YTLDELGND 321
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
1-322 1.06e-10

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 63.02  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEA-YCVGPTLSKDSYLNipNILSIATSTGCD---G 76
Cdd:COG3919    5 RFRVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVvVVPDPGDDPEAFVD--ALLELAERHGPDvliP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  77 VHPGYG-FLAENADfaELCEAcqLKFIGPSYQSIQKMGIKD--VAKAEmiKANVPVvPGSDgLMKDVSEAKKIAKKIGYP 153
Cdd:COG3919   83 TGDEYVeLLSRHRD--ELEEH--YRLPYPDADLLDRLLDKErfYELAE--ELGVPV-PKTV-VLDSADDLDALAEDLGFP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 154 VIIKAT--------AGGGGKGIRVARDEKELETGFRmteqeAQTAFGNGGLYMEkFIENFRHIEIQIVG--DSYGNVIHL 223
Cdd:COG3919  155 VVVKPAdsvgydelSFPGKKKVFYVDDREELLALLR-----RIAAAGYELIVQE-YIPGDDGEMRGLTAyvDRDGEVVAT 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 224 gerdCTIQRRMQKLVEEAPSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPvteMV 303
Cdd:COG3919  229 ----FTGRKLRHYPPAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFWRSLY---LA 301

                        330       340
                 ....*....|....*....|.
gi 579671149 304 T--GIDLVKLQLQVAMGDVLP 322
Cdd:COG3919  302 TaaGVNFPYLLYDDAVGRPLE 322
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 115-291 9.91e-09

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: 56.27  E-value: 9.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 115 KDVAKAEMIKANVPVVPG---SDGlmkDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGFRmteqeaqTAF 191
Cdd:COG1181   96 KALTKRVLAAAGLPTPPYvvlRRG---ELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALE-------EAF 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 192 GNGGLYM-EKFIENfRHIEIQIVGDSYGNVIHLGE-------RDCTIQRRMQKLVEEAPSPiLDDETRREMGNAAVRAAK 263
Cdd:COG1181  166 KYDDKVLvEEFIDG-REVTVGVLGNGGPRALPPIEivpengfYDYEAKYTDGGTEYICPAR-LPEELEERIQELALKAFR 243

                        170       180
                 ....*....|....*....|....*...
gi 579671149 264 AVNYENAGTIEFIYDlNDNKFYFMEMNT 291
Cdd:COG1181  244 ALGCRGYARVDFRLD-EDGEPYLLEVNT 270
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 60-318 1.36e-08

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 57.29  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   60 LNIPNILSIATSTGCDGVHPGYGFLAENAdFAELCEACQLKFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGsdGLMKD 139
Cdd:PRK12815  617 LTLEDVLNVAEAENIKGVIVQFGGQTAIN-LAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATD 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  140 VSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGFrmteqeAQTAFGNGGLYMEKFIENfRHIEIQIVGDSygn 219
Cdd:PRK12815  694 EEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYL------AENASQLYPILIDQFIDG-KEYEVDAISDG--- 763

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  220 vihlgeRDCTIQRRMQKlVEEA-----------PSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIydLNDNKFYFME 288
Cdd:PRK12815  764 ------EDVTIPGIIEH-IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFV--LANDEIYVLE 834

                         250       260       270
                  ....*....|....*....|....*....|
gi 579671149  289 MNTRIQVEHPVTEMVTGIDLVKLQLQVAMG 318
Cdd:PRK12815  835 VNPRASRTVPFVSKATGVPLAKLATKVLLG 864
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 100-293 6.87e-08

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 54.98  E-value: 6.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  100 KFIGPSYQSIQKMGIKDVAKAEMIKANVPVvpGSDGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELEtg 179
Cdd:PRK12815  114 ELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELE-- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  180 fRMTEQEAQTAFGNGGLyMEKFIENFRHIEIQIVGDSYGNV-------------IHLGErdcTIqrrmqkLVeeAPSPIL 246
Cdd:PRK12815  190 -QLFKQGLQASPIHQCL-LEESIAGWKEIEYEVMRDRNGNCitvcnmenidpvgIHTGD---SI------VV--APSQTL 256

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 579671149  247 DDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRI 293
Cdd:PRK12815  257 TDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRV 303
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 115-291 3.67e-05

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 45.49  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 115 KDVAKAEMIKANVPVVPGSdgLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGFRmteqeaqTAFGNG 194
Cdd:PRK01372  99 KLRTKLVWQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALE-------LAFKYD 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 195 GLYM-EKFI------------ENFRHIEIQIVGDSY--------GNVIHLgerdCtiqrrmqklveeaPSPiLDDETRRE 253
Cdd:PRK01372 170 DEVLvEKYIkgreltvavlggKALPVIEIVPAGEFYdyeakylaGGTQYI----C-------------PAG-LPAEIEAE 231

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 579671149 254 MGNAAVRAAKAVNYENAGTIEFIYDlNDNKFYFMEMNT 291
Cdd:PRK01372 232 LQELALKAYRALGCRGWGRVDFMLD-EDGKPYLLEVNT 268
carB PRK05294
carbamoyl-phosphate synthase large subunit;
100-292 4.00e-05

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 46.24  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  100 KFIGPSYQSIQKMGIKDVAKAEMIKANVPVVPGsdGLMKDVSEAKKIAKKIGYPVIikataggggkgIR----------- 168
Cdd:PRK05294  114 ELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEEIGYPVI-----------IRpsftlggtggg 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  169 VARDEKELET----GFRMTEqeaqtafgNGGLYMEKFIENFRHIEIQIVGDSYGNVI-------------HLGERDCTiq 231
Cdd:PRK05294  181 IAYNEEELEEiverGLDLSP--------VTEVLIEESLLGWKEYEYEVMRDKNDNCIivcsienidpmgvHTGDSITV-- 250

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579671149  232 rrmqklveeAPSPILDDETRREMGNAAVRAAKAVNYENAGT-IEFIYDLNDNKFYFMEMNTR 292
Cdd:PRK05294  251 ---------APAQTLTDKEYQMLRDASIAIIREIGVETGGCnVQFALNPKDGRYIVIEMNPR 303
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 105-308 5.27e-04

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 41.56  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  105 SYQSIQKMGIKDVAKAEMIKANVPVvPGSdGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGFRMTE 184
Cdd:TIGR00768  79 SSDAILNAGDKFLSHQLLAKAGIPL-PRT-GLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFE 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  185 QEAQTAfgnGGLYMEKFIE--NFRHIEIQIVGDSygnVIhlgerdCTIQR----RMQKLVEE--APSPI-LDDETRremg 255
Cdd:TIGR00768 157 QLNGPQ---NLFLVQEYIKkpGGRDIRVFVVGDE---VV------AAIYRitsgHWRSNLARggKAEPCsLTEEIE---- 220

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 579671149  256 NAAVRAAKAVNYENAGtIEFIYDlnDNKFYFMEMNTRIQVEHpvTEMVTGIDL 308
Cdd:TIGR00768 221 ELAIKAAKALGLDVAG-VDLLES--EDGLLVNEVNANPEFKN--SVKTTGVNI 268
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-311 1.17e-03

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: 40.69  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149   1 MKKVLIANRGEIA---VRIIRACRDLGIQTVAIysegDKDALHTQIADeaycvGPTLSKDSYLNIPNILSIATSTgcdgv 77
Cdd:COG0189    1 MMKIAILTDPPDKdstKALIEAAQRRGHEVEVI----DPDDLTLDLGR-----APELYRGEDLSEFDAVLPRIDP----- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  78 hPGYGFlaenaDFAELCEACQLKFIgPSYQSIQKMGIKDVAKAEMIKANVPVVPgsDGLMKDVSEAKKIAKKIGYPVIIK 157
Cdd:COG0189   67 -PFYGL-----ALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPP--TLVTRDPDDLRAFLEELGGPVVLK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 158 ATAGGGGKGIRVARDEKELETGFrmteqEAQTAFGNGGLYMEKFIENFRHIEIQI--VGdsyGNVIHlgerdcTIQRRMQ 235
Cdd:COG0189  138 PLDGSGGRGVFLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVlvVG---GEPVA------AIRRIPA 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149 236 K-----------LVEEAPspiLDDETRRemgnAAVRAAKAVNYENAGtIEFIYDlnDNKFYFMEMNTRIQVEHpvTEMVT 304
Cdd:COG0189  204 EgefrtnlarggRAEPVE---LTDEERE----LALRAAPALGLDFAG-VDLIED--DDGPLVLEVNVTPGFRG--LERAT 271


                 ....*..
gi 579671149 305 GIDLVKL 311
Cdd:COG0189  272 GVDIAEA 278
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 124-214 2.11e-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: 38.77  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  124 KANVPVVPGSDglMKDVSEAKKIAKKIGYPVIIKA-TAGGGGKGIRVARDEKELetgfrmteQEAQTAFGNGGLYMEKFI 202
Cdd:pfam02222   2 KLGLPTPRFMA--AESLEELIEAGQELGYPCVVKArRGGYDGKGQYVVRSEADL--------PQAWEELGDGPVIVEEFV 71

                          90
                  ....*....|..
gi 579671149  203 eNFRHiEIQIVG 214
Cdd:pfam02222  72 -PFDR-ELSVLV 81
carB PRK05294
carbamoyl-phosphate synthase large subunit;
140-321 3.94e-03

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 39.70  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  140 VSEAKKIAKKIGYPVII--------KAtaggggkgIRVARDEKELETGFRmteqEAQTAFGNGGLYMEKFIENFRHIEIQ 211
Cdd:PRK05294  693 VEEALEVAEEIGYPVLVrpsyvlggRA--------MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGAIEVDVD 760

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579671149  212 IVGDsyGNVIHLGerdcTIqrrMQKlVEEA-----------PSPILDDETRREMGNAAVRAAKAVNYE---NagtIEFIY 277
Cdd:PRK05294  761 AICD--GEDVLIG----GI---MEH-IEEAgvhsgdsacslPPQTLSEEIIEEIREYTKKLALELNVVglmN---VQFAV 827

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 579671149  278 DlnDNKFYFMEMNTRIQVEHPVTEMVTGIDLVKLQLQVAMGDVL 321
Cdd:PRK05294  828 K--DDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKL 869
 
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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