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Conserved domains on  [gi|488424171|ref|WP_002493556|]
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MULTISPECIES: acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha [Staphylococcus]

Protein Classification

acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha( domain architecture ID 11469138)

acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha is a biotin-dependent carboxylase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
5-445 0e+00

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


:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 667.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:COG4770    6 LIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:COG4770   86 SENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAGGGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:COG4770  166 KGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFTQ 323
Cdd:COG4770  246 ALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNfYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQ 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 324 KDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKV 403
Cdd:COG4770  326 EDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRR 405

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 488424171 404 ALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:COG4770  406 ALAEFVIEGVKTNIPFLRALLAHPDFRAGD---VDTGFIERE 444
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
5-445 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 667.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:COG4770    6 LIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:COG4770   86 SENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAGGGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:COG4770  166 KGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFTQ 323
Cdd:COG4770  246 ALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNfYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQ 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 324 KDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKV 403
Cdd:COG4770  326 EDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRR 405

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 488424171 404 ALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:COG4770  406 ALAEFVIEGVKTNIPFLRALLAHPDFRAGD---VDTGFIERE 444
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 5-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 632.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:PRK08591   6 LIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGYGFL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:PRK08591  86 SENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:PRK08591 166 RGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFTQ 323
Cdd:PRK08591 246 AITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEfYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKQ 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 324 KDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKV 403
Cdd:PRK08591 326 EDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKR 405

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 488424171 404 ALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:PRK08591 406 ALSEFVIDGIKTTIPLHLRLLNDPNFQAGD---YNIHYLEKK 444
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-445 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: 536.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171    1 MYRCLIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPG 80
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   81 YGFLSESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAAS 160
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  161 GGGGKGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEE 240
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  241 APCAALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGEL 319
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEfYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  320 PFTQKDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAIN 399
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIA 401

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 488424171  400 KLKVALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:TIGR00514 402 RMKRALSEFIIDGIKTTIPFHQRILEDENFQHGG---TNIHYLEKK 444
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 114-311 5.03e-58

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: 189.82  E-value: 5.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  114 DKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGGKGIRIVKEASHLDQALKEAKSEGQKYFND 193
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  194 DRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCAALTEERRTRICGDAVKVAQASRYRSAGTI 273
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 488424171  274 EFLV--TEDAHYFIEMNARIQVEHTVTEMRADRDLLQAQL 311
Cdd:pfam02786 161 EFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAA 200
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 334-443 1.78e-48

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: 161.43  E-value: 1.78e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   334 EARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKVALDEMVIEGF 413
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 488424171   414 TTTADFLYAVLNYPIYAKGDaskVDIKFLE 443
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGD---VDTGFLE 107
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
5-445 0e+00

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 667.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:COG4770    6 LIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:COG4770   86 SENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAGGGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:COG4770  166 KGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFTQ 323
Cdd:COG4770  246 ALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNfYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQ 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 324 KDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKV 403
Cdd:COG4770  326 EDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRR 405

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 488424171 404 ALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:COG4770  406 ALAEFVIEGVKTNIPFLRALLAHPDFRAGD---VDTGFIERE 444
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 5-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 632.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:PRK08591   6 LIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGYGFL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:PRK08591  86 SENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATAGGGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:PRK08591 166 RGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFTQ 323
Cdd:PRK08591 246 AITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEfYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKQ 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 324 KDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKV 403
Cdd:PRK08591 326 EDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKR 405

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 488424171 404 ALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:PRK08591 406 ALSEFVIDGIKTTIPLHLRLLNDPNFQAGD---YNIHYLEKK 444
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 5-445 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 545.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171    5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEAN-PLDSYLNIDRIISAAKVTESNVIHPGYGF 83
Cdd:PRK12999    9 LVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKhPVRAYLDIDEIIRVAKQAGVDAIHPGYGF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   84 LSESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGG 163
Cdd:PRK12999   89 LSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKASAGGG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  164 GKGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPC 243
Cdd:PRK12999  169 GRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  244 AALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTED-AHYFIEMNARIQVEHTVTEMRADRDLLQAQ--------LYLL 314
Cdd:PRK12999  249 PGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADgNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQiliaegatLHDL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  315 THGELpfTQKDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDS-LLYTGYQVSPYYDSLVAKVIVKDSN 393
Cdd:PRK12999  329 EIGIP--SQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTAWGRT 406

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488424171  394 RQTAINKLKVALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:PRK12999  407 FEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGD---YTTSFIDET 455
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 5-445 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: 541.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171    5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEAN-PLDSYLNIDRIISAAKvtESNV--IHPGY 81
Cdd:COG1038     8 LVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKgPVDAYLDIEEIIRVAK--EKGVdaIHPGY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   82 GFLSESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASG 161
Cdd:COG1038    86 GFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKAAAG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  162 GGGKGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEA 241
Cdd:COG1038   166 GGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  242 PCAALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTED-AHYFIEMNARIQVEHTVTEMRADRDLLQAQL-----YLLT 315
Cdd:COG1038   246 PAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDgNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQIliaegYSLD 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  316 HGE--LPfTQKDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDS-LLYTGYQVSPYYDSLVAKVIVKDS 392
Cdd:COG1038   326 DPEigIP-SQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGgNAYTGAVITPYYDSLLVKVTAWGR 404

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488424171  393 NRQTAINKLKVALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:COG1038   405 TFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGE---CTTSFIDET 454
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
5-450 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 541.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:PRK08654   6 LIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYGFL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:PRK08654  86 AENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:PRK08654 166 IGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAHYFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFTQK 324
Cdd:PRK08654 246 IMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQE 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 325 DILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKVA 404
Cdd:PRK08654 326 DITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIARMRRA 405

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 488424171 405 LDEMVIEGFTTTADFLYAVLNYPIYAKGDASKvdiKFLEKHQIIKE 450
Cdd:PRK08654 406 LYEYVIVGVKTNIPFHKAVMENENFVRGNLHT---HFIEEETTILE 448
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 5-446 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 539.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:PRK06111   6 LIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGYGLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:PRK06111  86 SENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAGGGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:PRK06111 166 IGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLyLLTHGE-LPFT 322
Cdd:PRK06111 246 FLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNfYFLEMNTRLQVEHPVTEEITGIDLVEQQL-RIAAGEkLSFT 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 323 QKDILFNGHVIEARINAENPeKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLK 402
Cdd:PRK06111 325 QDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLH 403

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 488424171 403 VALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKHQ 446
Cdd:PRK06111 404 DALEELKVEGIKTNIPLLLQVLEDPVFKAGG---YTTGFLTKQL 444
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
5-444 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 539.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:PRK05586   6 LIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGFGFL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:PRK05586  86 SENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASAGGGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:PRK05586 166 RGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFTQ 323
Cdd:PRK05586 246 VMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNfYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQ 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 324 KDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKV 403
Cdd:PRK05586 326 EDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKR 405

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 488424171 404 ALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEK 444
Cdd:PRK05586 406 ALGEFIIEGVNTNIDFQFIILEDEEFIKGT---YDTSFIEK 443
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-445 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: 536.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171    1 MYRCLIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPG 80
Cdd:TIGR00514   2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   81 YGFLSESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAAS 160
Cdd:TIGR00514  82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  161 GGGGKGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEE 240
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  241 APCAALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGEL 319
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEfYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  320 PFTQKDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAIN 399
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIA 401

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 488424171  400 KLKVALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:TIGR00514 402 RMKRALSEFIIDGIKTTIPFHQRILEDENFQHGG---TNIHYLEKK 444
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 5-443 6.83e-173

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 493.12  E-value: 6.83e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:PRK12833   9 LVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYGFL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:PRK12833  89 SENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGGGG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKnNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:PRK12833 169 RGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSP 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTE--DAHYFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFT 322
Cdd:PRK12833 248 SLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFA 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 323 QKDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLK 402
Cdd:PRK12833 328 QGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALARAA 407

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 488424171 403 VALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLE 443
Cdd:PRK12833 408 RALRELRIDGMKTTAPLHRALLADADVRAGR---FHTNFLE 445
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
1-445 1.41e-164

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 471.15  E-value: 1.41e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   1 MYRCLIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPG 80
Cdd:PRK08462   4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  81 YGFLSESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAAS 160
Cdd:PRK08462  84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 161 GGGGKGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEE 240
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 241 APCAALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAH-YFIEMNARIQVEHTVTEMRADRDLLQaQLYLLTHGEL 319
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDfYFMEMNTRLQVEHTVSEMVSGLDLIE-WMIKIAEGEE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 320 PFTQKDILFNGHVIEARINAENPEKnFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAIN 399
Cdd:PRK08462 323 LPSQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 488424171 400 KLKVALDEMVIEGFTTTADFLYAVLNYPIYAkgdASKVDIKFLEKH 445
Cdd:PRK08462 402 KMKRALKEFKVEGIKTTIPFHLEMMENADFI---NNKYDTKYLEEH 444
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
5-445 2.11e-156

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 451.48  E-value: 2.11e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   5 LIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGeANPLDSYLNIDRIISAAKVTESNVIHPGYGFL 84
Cdd:PRK07178   6 LIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIG-ADPLAGYLNPRRLVNLAVETGCDALHPGYGFL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  85 SESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGG 164
Cdd:PRK07178  85 SENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATSGGGG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 165 KGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCA 244
Cdd:PRK07178 165 RGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSP 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 245 ALTEERRTRICGDAVKVAQASRYRSAGTIEFLV-TEDAHYFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTHGELPFTQ 323
Cdd:PRK07178 245 QLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQ 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 324 KDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKV 403
Cdd:PRK07178 325 EDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALDRGRR 404

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 488424171 404 ALDEMVIEGFTTTADFLYAVLNYPIYAKGDaskVDIKFLEKH 445
Cdd:PRK07178 405 ALDDMRVQGVKTTIPYYQEILRNPEFRSGQ---FNTSFVESH 443
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-445 9.14e-146

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 424.61  E-value: 9.14e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   1 MYRCLIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEaNPLDSYLNIDRIISAAKVTESNVIHPG 80
Cdd:PRK08463   2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGT-DPIKGYLDVKRIVEIAKACGADAIHPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  81 YGFLSESTNFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGS---NDavQSVDEIKLLSKEIGFPVVLK 157
Cdd:PRK08463  81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTeklNS--ESMEEIKIFARKIGYPVILK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 158 AASGGGGKGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKL 237
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 238 IEEAPCAALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTE-DAHYFIEMNARIQVEHTVTEMRADRDLLQAQLYLLTH 316
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDyNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 317 GELPFTQKDILFNGHVIEARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQT 396
Cdd:PRK08463 319 EILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 488424171 397 AINKLKVALDEMVIEGFTTTADFLYAVLNYPIYAKGdasKVDIKFLEKH 445
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRG---YFDTSYIETH 444
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 114-311 5.03e-58

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: 189.82  E-value: 5.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  114 DKITARQTVKQAGVPVIPGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGGKGIRIVKEASHLDQALKEAKSEGQKYFND 193
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  194 DRVYVEAFIPVAKHVEVQIIGDGKNNYVHLGERDCSVQRKNQKLIEEAPCAALTEERRTRICGDAVKVAQASRYRSAGTI 273
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 488424171  274 EFLV--TEDAHYFIEMNARIQVEHTVTEMRADRDLLQAQL 311
Cdd:pfam02786 161 EFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAA 200
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 3-105 4.07e-56

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: 181.15  E-value: 4.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171    3 RCLIANRGEIAVRIIRACRELNIETVAIYAKGDENSLHVSLADQAICIGEANPLDSYLNIDRIISAAKVTESNVIHPGYG 82
Cdd:pfam00289   3 KVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGYG 82

                          90       100
                  ....*....|....*....|...
gi 488424171   83 FLSESTNFAKAVEDNHIHFIGPS 105
Cdd:pfam00289  83 FLSENAEFARACEEAGIIFIGPS 105
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 334-444 9.58e-51

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: 167.28  E-value: 9.58e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  334 EARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKVALDEMVIEGF 413
Cdd:pfam02785   1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 488424171  414 TTTADFLYAVLNYPIYAKGDaskVDIKFLEK 444
Cdd:pfam02785  81 KTNIPFLRAILEHPDFRAGE---VDTGFLEE 108
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 334-443 1.78e-48

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: 161.43  E-value: 1.78e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   334 EARINAENPEKNFLPTPGKVNKLHLPQGFNIRVDSLLYTGYQVSPYYDSLVAKVIVKDSNRQTAINKLKVALDEMVIEGF 413
Cdd:smart00878   1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 488424171   414 TTTADFLYAVLNYPIYAKGDaskVDIKFLE 443
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGD---VDTGFLE 107
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 61-311 2.09e-48

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: 166.59  E-value: 2.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  61 NIDRIISAAKVtesnvIHPGYGF---LSES----TNFAKAVEdnHIHFIGPSKTTMEMMGDKITARQTVKQAGVPViPGS 133
Cdd:COG0439    1 DIDAIIAAAAE-----LARETGIdavLSESefavETAAELAE--ELGLPGPSPEAIRAMRDKVLMREALAAAGVPV-PGF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 134 nDAVQSVDEIKLLSKEIGFPVVLKAASGGGGKGIRIVKEASHLDQALKEAKSEGQKYFNDDRVYVEAFIPvAKHVEVQII 213
Cdd:COG0439   73 -ALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLE-GREYSVEGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 214 GDGKNNYVhlgerdCSVQRKNQK------LIEEAPcAALTEERRTRICGDAVKVAQASRY-RSAGTIEFLVTED-AHYFI 285
Cdd:COG0439  151 VRDGEVVV------CSITRKHQKppyfveLGHEAP-SPLPEELRAEIGELVARALRALGYrRGAFHTEFLLTPDgEPYLI 223

                        250       260
                 ....*....|....*....|....*...
gi 488424171 286 EMNARIQVEH--TVTEMRADRDLLQAQL 311
Cdd:COG0439  224 EINARLGGEHipPLTELATGVDLVREQI 251
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 89-297 3.76e-12

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 68.46  E-value: 3.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   89 NFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGsnDAVQSVDEIKLLSKEIGFPVVLKAASGGGGKGIR 168
Cdd:PRK12815  645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMA 722

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  169 IVKEASHLDQALKEAKSegqkyfNDDRVYVEAFIPvAKHVEVQIIGDGKNNY------------VHLGERDCSVQRKNqk 236
Cdd:PRK12815  723 VVYDEPALEAYLAENAS------QLYPILIDQFID-GKEYEVDAISDGEDVTipgiiehieqagVHSGDSIAVLPPQS-- 793

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488424171  237 lieeapcaaLTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAHYFIEMNARiqVEHTV 297
Cdd:PRK12815  794 ---------LSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPR--ASRTV 843
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 89-290 4.03e-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: 68.49  E-value: 4.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171    89 NFAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPGSndAVQSVDEIKLLSKEIGFPVVLKAASGGGGKGIR 168
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWK--TATSVEEAVEFASEIGYPVLVRPSYVLGGRAME 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   169 IVKEASHLDQALKEAKSEGQKYfnddRVYVEAFIPVAKHVEVQIIGDGKNNY------------VHLGERDCSVqrknqk 236
Cdd:TIGR01369  722 IVYNEEELRRYLEEAVAVSPEH----PVLIDKYLEDAVEVDVDAVSDGEEVLipgimehieeagVHSGDSTCVL------ 791

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 488424171   237 lieeaPCAALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAHYFIEMNAR 290
Cdd:TIGR01369  792 -----PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPR 840
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 114-288 1.44e-08

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: 55.88  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 114 DKITARQTVKQAGVPVIPG---SNDAVQSVDEIKllsKEIGFPVVLKAASGGGGKGIRIVKEASHLDQALKEAKSEgqky 190
Cdd:COG1181   95 DKALTKRVLAAAGLPTPPYvvlRRGELADLEAIE---EELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY---- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 191 fnDDRVYVEAFIPvAKHVEVQIIGDGKNNYVHLGE-------RDCSVQRKNQKLIEEAPcAALTEERRTRICGDAVKVAQ 263
Cdd:COG1181  168 --DDKVLVEEFID-GREVTVGVLGNGGPRALPPIEivpengfYDYEAKYTDGGTEYICP-ARLPEELEERIQELALKAFR 243

                        170       180       190
                 ....*....|....*....|....*....|..
gi 488424171 264 A------SRyrsagtIEFLVTEDAH-YFIEMN 288
Cdd:COG1181  244 AlgcrgyAR------VDFRLDEDGEpYLLEVN 269
ddl PRK01966
D-alanine--D-alanine ligase;
75-214 1.15e-07

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 53.20  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  75 NVIHPGYGflsestnfakavEDNHIH---------FIGP----SKTTMemmgDKITARQTVKQAGVPVIPG-----SNDA 136
Cdd:PRK01966  87 PVLHGPPG------------EDGTIQgllellgipYVGCgvlaSALSM----DKILTKRLLAAAGIPVAPYvvltrGDWE 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488424171 137 VQSVDEIKllsKEIGFPVVLKAASGGGGKGIRIVKEASHLDQALKEAKSEgqkyfnDDRVYVEAFIpVAKHVEVQIIG 214
Cdd:PRK01966 151 EASLAEIE---AKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEY------DRKVLVEQGI-KGREIECAVLG 218
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 91-290 2.69e-07

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: 52.96  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  91 AKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPVIPgsNDAVQSVDEIKLLSKEIGFPVVlkaasggggkgIR-- 168
Cdd:COG0458   91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPK--SGTATSVEEALAIAEEIGYPVI-----------VRps 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 169 ---------IVKEASHLDQALKEAKsegqKYFNDDRVYVEAFIPVAKHVEVQIIGDGKNNY-------------VHLGER 226
Cdd:COG0458  158 yvlggrgmgIVYNEEELEEYLERAL----KVSPDHPVLIDESLLGAKEIEVDVVRDGEDNViivgimehiepagVHSGDS 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488424171 227 DCSvqrknqklieeAPCAALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAHYFIEMNAR 290
Cdd:COG0458  234 ICV-----------APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPR 286
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 114-286 7.02e-07

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: 50.84  E-value: 7.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 114 DKITARQTVKQAGVPVIPGSndAVQSVDEIKLLSKEIGFPVVLKAAsggggkgiR---------IVKEASHLDQALKEak 184
Cdd:COG0026   89 DRLLEKAFLAELGIPVAPFA--AVDSLEDLEAAIAELGLPAVLKTR--------RggydgkgqvVIKSAADLEAAWAA-- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 185 segqkyFNDDRVYVEAFIPVAKhvEVQIIG--DGKNNYVH--LGErdcSVQRKNQkLIE-EAPcAALTEERRTRICGDAV 259
Cdd:COG0026  157 ------LGGGPCILEEFVPFER--ELSVIVarSPDGEVATypVVE---NVHRNGI-LDEsIAP-ARISEALAAEAEEIAK 223

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 488424171 260 KVAQASRYRsaGT--IEFLVTEDA---------------HYFIE 286
Cdd:COG0026  224 RIAEALDYV--GVlaVEFFVTKDGellvneiaprphnsgHWTIE 265
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 122-288 1.62e-06

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


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 48.47  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  122 VKQAGVPVIP----GSNDAVQSVDEIKLLSKE-IGFPVVLKAASGGGGKGIRIVKEASHLDQALKEAKsegqKYfnDDRV 196
Cdd:pfam07478   2 LKAAGLPVVPfvtfTRADWKLNPKEWCAQVEEaLGYPVFVKPARLGSSVGVSKVESREELQAAIEEAF----QY--DEKV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  197 YVEAFIPvAKHVEVQIIGDGKNNYVHLGER--DCSVQRKNQKLIEEA-----PcAALTEERRTRICGDAVKVAQASRYRS 269
Cdd:pfam07478  76 LVEEGIE-GREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvP-ADLEEEQEEQIQELALKAYKALGCRG 153

                         170       180
                  ....*....|....*....|
gi 488424171  270 AGTIEFLVTEDAHYFI-EMN 288
Cdd:pfam07478 154 LARVDFFLTEDGEIVLnEVN 173
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 114-203 1.63e-06

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 49.72  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 114 DKITARQTVKQAGVPVIPGSndAVQSVDEIKLLSKEIGFPVVLKAASGGGGKGIRIVKEASHLDQALKEAKsegqKYfnD 193
Cdd:PRK01372  98 DKLRTKLVWQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAF----KY--D 169

                         90
                 ....*....|
gi 488424171 194 DRVYVEAFIP 203
Cdd:PRK01372 170 DEVLVEKYIK 179
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
98-291 6.31e-06

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 48.00  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  98 HIHFIGPSKTTMEMMGDKITARQTVKQAGVPViPGSnDAVQSVDEIKLLSKEIGFPVVLKAASGGGGKG--------IRI 169
Cdd:COG3919  101 HYRLPYPDADLLDRLLDKERFYELAEELGVPV-PKT-VVLDSADDLDALAEDLGFPVVVKPADSVGYDElsfpgkkkVFY 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 170 VKEASHLDQALKEAKSEGQKYFnddrvyVEAFIPVAKHVEVQIigdgkNNYVHL-GE-RDCSVQRKnqklIEEAP----- 242
Cdd:COG3919  179 VDDREELLALLRRIAAAGYELI------VQEYIPGDDGEMRGL-----TAYVDRdGEvVATFTGRK----LRHYPpaggn 243

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488424171 243 -CAALTEERRtRICGDAVKVAQASRYRSAGTIEFLVTED--AHYFIEMNARI 291
Cdd:COG3919  244 sAARESVDDP-ELEEAARRLLEALGYHGFANVEFKRDPRdgEYKLIEINPRF 294
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 91-280 1.05e-05

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 47.45  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  91 AKAVEDNHIHFIGPSktTMEMMGDKITARQTVKQAGVPVIPGSndAVQSVDEIKLLSKEIGFPVVLKAAsggggkgiR-- 168
Cdd:PRK06019  79 LDALAARVPVPPGPD--ALAIAQDRLTEKQFLDKLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTR--------Rgg 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 169 -------IVKEASHLDQALKEaksegqkyFNDDRVYVEAFIPVAKhvEVQIIG--DGKNNYVH--LGErdcSVQRkNQKL 237
Cdd:PRK06019 147 ydgkgqwVIRSAEDLEAAWAL--------LGSVPCILEEFVPFER--EVSVIVarGRDGEVVFypLVE---NVHR-NGIL 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488424171 238 IE-EAPcAALTEERRTRICGDAVKVAQASRYRsaGT--IEFLVTED 280
Cdd:PRK06019 213 RTsIAP-ARISAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGD 255
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 123-214 1.23e-05

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: 45.32  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  123 KQAGVPViPGSNDAvQSVDEIKLLSKEIGFPVVLKAASGGGG-KGIRIVKEASHLDQALKEAKSEgqkyfnddRVYVEAF 201
Cdd:pfam02222   1 QKLGLPT-PRFMAA-ESLEELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELGDG--------PVIVEEF 70

                          90
                  ....*....|...
gi 488424171  202 IPVAKhvEVQIIG 214
Cdd:pfam02222  71 VPFDR--ELSVLV 81
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 114-219 5.27e-05

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 45.53  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 114 DKITARQTVKQAGVPVIPGsnDAVQSVDEIKLLSKEIGFPVVLKA--ASGGGGKGIRIVKEAsHLDQALKEAKSEGqkyf 191
Cdd:PRK14016 214 DKELTKRLLAAAGVPVPEG--RVVTSAEDAWEAAEEIGYPVVVKPldGNHGRGVTVNITTRE-EIEAAYAVASKES---- 286

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488424171 192 ndDRVYVEAFIP---------------VAKHVEVQIIGDGKNN 219
Cdd:PRK14016 287 --SDVIVERYIPgkdhrllvvggklvaAARREPPHVIGDGKHT 327
PylC COG2232
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ...
 244-311 1.91e-04

Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];


Pssm-ID: 441833 [Multi-domain]  Cd Length: 370  Bit Score: 43.37  E-value: 1.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488424171 244 AALTEERRTRICGDAVKVAQASRYRSAGTIEFLVTEDAHYFIEMNARIQVEHTVTEMRADRDLLQAQL 311
Cdd:COG2232  216 LALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHL 283
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-289 1.99e-04

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: 43.01  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171   1 MYRCLIANRGEIA---VRIIRACRELNIETVAIyakgDENSLHVSLaDQAICIGEANPLDSY-LNIDRIISaakvtesnv 76
Cdd:COG0189    1 MMKIAILTDPPDKdstKALIEAAQRRGHEVEVI----DPDDLTLDL-GRAPELYRGEDLSEFdAVLPRIDP--------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  77 ihPGYGflsesTNFAKAVEDNHIHFIGPSkTTMEMMGDKITARQTVKQAGVPVIPGSndAVQSVDEIKLLSKEIGFPVVL 156
Cdd:COG0189   67 --PFYG-----LALLRQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTL--VTRDPDDLRAFLEELGGPVVL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 157 KAASGGGGKGIRIVKEASHLDQALKEAKSEGQKYFnddrvYVEAFIPVAKHVEVQII----------------GDGKNNy 220
Cdd:COG0189  137 KPLDGSGGRGVFLVEDEDALESILEALTELGSEPV-----LVQEFIPEEDGRDIRVLvvggepvaairripaeGEFRTN- 210

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488424171 221 VHLGERdcsvqrknqklieEAPCAALTEERRTricgdAVKVAQASRYRSAGtIEFLVTEDAHYFIEMNA 289
Cdd:COG0189  211 LARGGR-------------AEPVELTDEEREL-----ALRAAPALGLDFAG-VDLIEDDDGPLVLEVNV 260
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
118-160 4.73e-04

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 42.42  E-value: 4.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488424171 118 ARQTVKQAGVPVIPGSndAVQSVDEIKLLSKEIGFPVVLKAAS 160
Cdd:COG1042  493 AKALLAAYGIPVVPTR--LARSAEEAVAAAEEIGYPVVLKIVS 533
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 62-290 1.22e-03

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 40.64  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171  62 IDRIISAAKVTESNVIHPGY----GFLSEStnfAKAVEDNHIHFIGPSKTTMEMMGDKITARQTVKQAGVPViPGS--ND 135
Cdd:PRK12767  58 IDRLLDICKKEKIDLLIPLIdpelPLLAQN---RDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPT-PKSylPE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 136 AVQSVDEIkLLSKEIGFPVVLKAASGGGGKGIRIVKEASHLDQALKEAKS-------EGQKY----FNDDRVYVEAFIPV 204
Cdd:PRK12767 134 SLEDFKAA-LAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPNliiqefiEGQEYtvdvLCDLNGEVISIVPR 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 205 AKhveVQIIGdgknnyvhlGERDCSVQRKNQKLIEEapcaalteerrtricgdAVKVAQASRYRSAGTIEFLVTEDAHYF 284
Cdd:PRK12767 213 KR---IEVRA---------GETSKGVTVKDPELFKL-----------------AERLAEALGARGPLNIQCFVTDGEPYL 263


                 ....*.
gi 488424171 285 IEMNAR 290
Cdd:PRK12767 264 FEINPR 269
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 114-291 3.54e-03

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 39.83  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 114 DKITARQTVKQAGVPVipGSNDAVQSVDEIKLLSKEIGFPVVLKAASGGGGKGIRIVKEAshlDQALkeAKSEGQKYFND 193
Cdd:PRK02186 107 DKKRLARTLRDHGIDV--PRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASV---AEAA--AHCAALRRAGT 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488424171 194 DRVYVEAFIPvAKHVEVQIIGDGKNNYV------HLGERDCSVQrknqkLIEEAPcAALTEERRTRICGDAVKVAQASRY 267
Cdd:PRK02186 180 RAALVQAYVE-GDEYSVETLTVARGHQVlgitrkHLGPPPHFVE-----IGHDFP-APLSAPQRERIVRTVLRALDAVGY 252

                        170       180
                 ....*....|....*....|....*
gi 488424171 268 R-SAGTIEFLVTEDAHYFIEMNARI 291
Cdd:PRK02186 253 AfGPAHTELRVRGDTVVIIEINPRL 277
 
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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