NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16131144|ref|NP_417722|]
View 

biotin carboxylase [Escherichia coli str. K-12 substr. MG1655]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


:

Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 909.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  320 PLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPaKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16131144  399 IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGLQEK 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 909.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  320 PLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPaKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16131144  399 IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGLQEK 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
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: 814.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144     1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGpLGDDMDKNRAIAKRIGYPVIIKA 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDG-LVEDEEENVRIAKRIGYPVIIKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   320 PLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPiKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 16131144   399 IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGLQE 448
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMGE 449
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: 776.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:COG4770   1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:COG4770  81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPV-QDAEEALAIAEEIGYPVLIKA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 161 SgggggrgmrvvrgdA--------------ELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLA 226
Cdd:COG4770 160 S--------------AggggkgmrvvrseeELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLG 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 227 ERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITG 305
Cdd:COG4770 226 ERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTG 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 306 VDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSM 384
Cdd:COG4770 306 IDLVEEQIRIAAGEPLPFTQEDIKLRGHAIECRINAEDPaRGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSM 385

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 385 IGKLICYGENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKL 444
Cdd:COG4770 386 IAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIEREL 445
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 115-322 2.38e-99

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: 296.14  E-value: 2.38e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   115 DKVSAIAAMKKAGVPCVPGSDGPlGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFS 194
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGP-VETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   195 NDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGT 274
Cdd:pfam02786  80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 16131144   275 FEFLFE--NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQPLS 322
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-441 2.18e-59

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: 189.55  E-value: 2.18e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGI 414
Cdd:smart00878   1 ECRINAEDPaNGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*..
gi 16131144    415 KTNVDLQIRIMNDENFQHGGTNIHYLE 441
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
 
Name Accession Description Interval E-value
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 909.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08591   1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:PRK08591  81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPV-DDEEEALAIAKEIGYPVIIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEkNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  320 PLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPaKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16131144  399 IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGLQEK 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEE 450
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: 814.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144     1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:TIGR00514   1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGpLGDDMDKNRAIAKRIGYPVIIKA 160
Cdd:TIGR00514  81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDG-LVEDEEENVRIAKRIGYPVIIKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDkNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   320 PLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPiKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 16131144   399 IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGLQE 448
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMGE 449
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: 776.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:COG4770   1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:COG4770  81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPV-QDAEEALAIAEEIGYPVLIKA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 161 SgggggrgmrvvrgdA--------------ELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLA 226
Cdd:COG4770 160 S--------------AggggkgmrvvrseeELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLG 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 227 ERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITG 305
Cdd:COG4770 226 ERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTG 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 306 VDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSM 384
Cdd:COG4770 306 IDLVEEQIRIAAGEPLPFTQEDIKLRGHAIECRINAEDPaRGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSM 385

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 385 IGKLICYGENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKL 444
Cdd:COG4770 386 IAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIEREL 445
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-444 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 689.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK06111   1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:PRK06111  81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNL-EDAEEAIAIARQIGYPVMLKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK06111 160 SAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGE-FYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK06111 240 EEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  320 PLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAI 399
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDPKTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 16131144  400 ARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKL 444
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQL 444
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1-449 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 664.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08654   1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:PRK08654  81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGI-EDIEEAKEIAEEIGYPVIIKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  321 LSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAI 399
Cdd:PRK08654 320 LSFKQEDITIRGHAIECRINAEDPlNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAI 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 16131144  400 ARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGLQEK 449
Cdd:PRK08654 400 ARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEE 449
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1-445 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 611.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK05586   1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:PRK05586  81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEI-ENEEEALEIAKEIGYPVMVKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  320 PLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPkNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 16131144  399 IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLG 445
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKKLV 446
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 1-433 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 575.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144     1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPS-VKSYLNIPAIISAAEITGAVAIH 79
Cdd:PRK12999    4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHpVRAYLDIDEIIRVAKQAGVDAIH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    80 PGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIK 159
Cdd:PRK12999   84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPI-DDIEEALEFAEEIGYPIMLK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   160 ASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:PRK12999  163 ASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   240 VEEAPAPGITPELRRYIgerCAKA---CVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:PRK12999  243 VEIAPAPGLSEELRERI---CEAAvklARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   316 AAGQPLS------IKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWES-HIYAGYTVPPYYDSMIGK 387
Cdd:PRK12999  320 AEGATLHdleigiPSQEDIRLRGYAIQCRITTEDPaNNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVK 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 16131144   388 LICYGENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHG 433
Cdd:PRK12999  400 LTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAG 445
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 1-433 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: 557.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPS-VKSYLNIPAIISAAEITGAVAIH 79
Cdd:COG1038    3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGpVDAYLDIEEIIRVAKEKGVDAIH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   80 PGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIK 159
Cdd:COG1038   83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPV-DDLEEALAFAEEIGYPVMLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  160 ASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:COG1038  162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  240 VEEAPAPGITPELRRYIGE---RCAKAcvdIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:COG1038  242 VEIAPAPNLDEELREAICEaavKLAKA---VGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILI 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  316 AAGQPLS------IKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRW-ESHIYAGYTVPPYYDSMIGK 387
Cdd:COG1038  319 AEGYSLDdpeigiPSQEDIRLNGYAIQCRITTEDPaNNFMPDTGRITAYRSAGGFGIRLdGGNAYTGAVITPYYDSLLVK 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 16131144  388 LICYGENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHG 433
Cdd:COG1038  399 VTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAG 444
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 2-441 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 555.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    2 LDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:PRK12833   5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   82 YGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKAS 161
Cdd:PRK12833  85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVV-ASLDAALEVAARIGYPLMIKAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  162 GGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQgNAIYLAERDCSMQRRHQKVVE 241
Cdd:PRK12833 164 AGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  242 EAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK12833 243 EAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  320 PLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK12833 323 PLRFAQGDIALRGAALECRINAEDPlRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAA 402

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 16131144  399 IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLE 441
Cdd:PRK12833 403 LARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
2-443 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 555.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    2 LDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:PRK08462   4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   82 YGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKAS 161
Cdd:PRK08462  84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGAL-KSYEEAKKIAKEIGYPVILKAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  162 GGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVVE 241
Cdd:PRK08462 163 AGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  242 EAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDsNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  321 LSiKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIA 400
Cdd:PRK08462 323 LP-SQESIKLKGHAIECRITAEDPKKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 16131144  401 RMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKK 443
Cdd:PRK08462 402 KMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-441 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 548.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPsVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK07178   1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADP-LAGYLNPRRLVNLAVETGCDALHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLGDdMDKNRAIAKRIGYPVIIKA 160
Cdd:PRK07178  80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLAD-LDEALAEAERIGYPVMLKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE-NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDaDGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  320 PLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA 398
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPkNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 16131144  399 IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLE 441
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVE 441
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-445 2.14e-172

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 492.02  E-value: 2.14e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    1 MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPsVKSYLNIPAIISAAEITGAVAIHP 80
Cdd:PRK08463   1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDP-IKGYLDVKRIVEIAKACGADAIHP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDgPLGDD-MDKNRAIAKRIGYPVIIK 159
Cdd:PRK08463  80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLNSEsMEEIKIFARKIGYPVILK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  160 ASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKV 239
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  240 VEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAG 318
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  319 QPLSIKQEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDV 397
Cdd:PRK08463 319 EILDLEQSDIKPRGFAIEARITAENVwKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDL 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 16131144  398 AIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLG 445
Cdd:PRK08463 399 AVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQ 446
urea_carbox TIGR02712
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ...
 3-442 3.61e-164

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: 493.78  E-value: 3.61e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144      3 DKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPGY 82
Cdd:TIGR02712    2 DTVLIANRGEIAVRIIRTLRRMGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144     83 GFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSdgPLGDDMDKNRAIAKRIGYPVIIKASG 162
Cdd:TIGR02712   82 GFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLPGT--GLLSSLDEALEAAKEIGYPVMLKSTA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    163 GGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVVEE 242
Cdd:TIGR02712  160 GGGGIGMQKCDSAAELAEAFETVKRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    243 APAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP 320
Cdd:TIGR02712  240 TPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdeARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGEL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    321 LSIKQ--EEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGgfGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDV 397
Cdd:TIGR02712  320 PDFASlnISLTPRGAAIEARVYAENPaKNFQPSPGLLTDVQFPD--DVRVDTWVETGTEVSPEYDPMLAKIIVHGSDRED 397

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 16131144    398 AIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEK 442
Cdd:TIGR02712  398 AILKLHQALAETRVYGIETNLDYLRSILSSETFRSAQVSTRTLNS 442
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 4-433 1.47e-159

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


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 480.48  E-value: 1.47e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144      4 KIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPS---VKSYLNIPAIISAAEITGAVAIHP 80
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDlgpIEAYLSIDEIIRVAKLNGVDAIHP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144     81 GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLgDDMDKNRAIAKRIGYPVIIKA 160
Cdd:TIGR01235   81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPP-ETMEEVLDFAAAIGYPVIIKA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    161 SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV 240
Cdd:TIGR01235  160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    241 EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQ 319
Cdd:TIGR01235  240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVdNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    320 PLSIK------QEEVHVRGHAVECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWES-HIYAGYTVPPYYDSMIGKLICY 391
Cdd:TIGR01235  320 SLPTPqlgvpnQEDIRTNGYAIQCRVTTEDPaNNFQPDTGRIEAYRSAGGFGIRLDGgNSYAGAIITPYYDSLLVKVSAW 399

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 16131144    392 GENRDVAIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHG 433
Cdd:TIGR01235  400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDG 441
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 115-322 2.38e-99

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: 296.14  E-value: 2.38e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   115 DKVSAIAAMKKAGVPCVPGSDGPlGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFS 194
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGP-VETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   195 NDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGT 274
Cdd:pfam02786  80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 16131144   275 FEFLFE--NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQPLS 322
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 62-320 7.33e-69

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: 219.74  E-value: 7.33e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  62 NIPAIISA-AEITGAVAIHpgyGFLSENAN----FAEQVERSGFIfiGPKAETIRLMGDKVSAIAAMKKAGVPcVPGSDg 136
Cdd:COG0439   1 DIDAIIAAaAELARETGID---AVLSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGFA- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 137 pLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYMEKYLENpRHVEIQVLA 216
Cdd:COG0439  74 -LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 217 DgQGNAIYlaerdCSMQRRHQK---VVE---EAPAPgITPELRRYIGERCAKACVDIGY-RGAGTFEFLF-ENGEFYFIE 288
Cdd:COG0439 152 R-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLIE 224

                       250       260       270
                ....*....|....*....|....*....|....
gi 16131144 289 MNTRIQVEH--PVTEMITGVDLIKEQLRIAAGQP 320
Cdd:COG0439 225 INARLGGEHipPLTELATGVDLVREQIRLALGEP 258
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 2-109 2.88e-60

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: 191.93  E-value: 2.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144     2 LDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPG 81
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80

                          90       100
                  ....*....|....*....|....*...
gi 16131144    82 YGFLSENANFAEQVERSGFIFIGPKAET 109
Cdd:pfam00289  81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-441 2.18e-59

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: 189.55  E-value: 2.18e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGI 414
Cdd:smart00878   1 ECRINAEDPaNGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80

                           90       100
                   ....*....|....*....|....*..
gi 16131144    415 KTNVDLQIRIMNDENFQHGGTNIHYLE 441
Cdd:smart00878  81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 336-442 3.86e-56

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: 181.15  E-value: 3.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   336 ECRINAEDP-NTFLPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGI 414
Cdd:pfam02785   1 EARIYAEDPdNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80

                          90       100
                  ....*....|....*....|....*...
gi 16131144   415 KTNVDLQIRIMNDENFQHGGTNIHYLEK 442
Cdd:pfam02785  81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 90-321 1.06e-12

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


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 70.41  E-value: 1.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144     90 NFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSdgpLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGM 169
Cdd:TIGR01369  644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWK---TATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    170 RVVRGDAELAQSISmtraEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIY-LAErdcsmqrrHqkvVEEA----- 243
Cdd:TIGR01369  721 EIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPgIME--------H---IEEAgvhsg 785

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    244 ------PAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAA 317
Cdd:TIGR01369  786 dstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865


                   ....
gi 16131144    318 GQPL 321
Cdd:TIGR01369  866 GKKL 869
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 90-322 6.90e-11

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 64.61  E-value: 6.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    90 NFAEQVERSGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSdgpLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGM 169
Cdd:PRK12815  645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGL---TATDEEEAFAFAKRIGYPVLIRPSYVIGGQGM 721

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   170 RVVRGDAELAQSIsmtraeAKAAFSNDMVYMEKYLENpRHVEIQVLADgqGNAIYLA---ErdcsmqrrHqkvVEEA--- 243
Cdd:PRK12815  722 AVVYDEPALEAYL------AENASQLYPILIDQFIDG-KEYEVDAISD--GEDVTIPgiiE--------H---IEQAgvh 781

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   244 --------PAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRI 315
Cdd:PRK12815  782 sgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKV 861


                  ....*..
gi 16131144   316 AAGQPLS 322
Cdd:PRK12815  862 LLGKSLA 868
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
84-335 7.70e-08

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 54.16  E-value: 7.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  84 FLSENANFAEQversGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPC----VPGSDGPLgddmdknRAIAKRIGYPVIIK 159
Cdd:COG3919  90 LLSRHRDELEE----HYRLPYPDADLLDRLLDKERFYELAEELGVPVpktvVLDSADDL-------DALAEDLGFPVVVK 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 160 ASG-GGGGRGMRVVRGDAELAQSismtRAEAKAAF------SNDMVYMEkYLENPRHVE--IQVLADGQGNAIYLaerdC 230
Cdd:COG3919 159 PADsVGYDELSFPGKKKVFYVDD----REELLALLrriaaaGYELIVQE-YIPGDDGEMrgLTAYVDRDGEVVAT----F 229

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 231 SMQRRHQK--------VVEEAPAPGITPELRRYIGErcakacvdIGYRGAGTFEFLF--ENGEFYFIEMNTRI--QVEHP 298
Cdd:COG3919 230 TGRKLRHYppaggnsaARESVDDPELEEAARRLLEA--------LGYHGFANVEFKRdpRDGEYKLIEINPRFwrSLYLA 301

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 16131144 299 VtemITGVDLIKEQLRIAAGQPL-SIKQEEVHVRGHAV 335
Cdd:COG3919 302 T---AAGVNFPYLLYDDAVGRPLePVPAYREGVLWRVL 336
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 90-292 3.77e-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: 52.19  E-value: 3.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  90 NFAEQVERSGFI----FIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSdgpLGDDMDKNRAIAKRIGYPVIIKASGGGG 165
Cdd:COG0458  85 NLAVELEEAGILegvkILGTSPDAIDLAEDRELFKELLDKLGIPQPKSG---TATSVEEALAIAEEIGYPVIVRPSYVLG 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 166 GRGMRVVRGDAELAQSIsmtrAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLaerdCSMQrrHqkvVEEA-- 243
Cdd:COG0458 162 GRGMGIVYNEEELEEYL----ERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgv 228

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131144 244 ---------PAPGITPE----LRRYiGERCAKAcvdIGYRGAGTFEFLFENGEFYFIEMNTR 292
Cdd:COG0458 229 hsgdsicvaPPQTLSDKeyqrLRDA-TLKIARA---LGVVGLCNIQFAVDDGRVYVIEVNPR 286
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 5-321 3.21e-05

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: 46.53  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144      5 IVIANRGEIALRILRACK---ELGIKTVAVHSSAdrdlkhvlladETVCIGPAPSVKSYL------NIPAIISAAEITGa 75
Cdd:TIGR01369   17 IVIGQAAEFDYSGSQACKalkEEGYRVILVNSNP-----------ATIMTDPEMADKVYIepltpeAVEKIIEKERPDA- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144     76 vaIHPGYGflSENA-NFAEQVERSGFI------FIGPKAETIRLMGDKVSAIAAMKKAGVPcVPGSDgpLGDDMDKNRAI 148
Cdd:TIGR01369   85 --ILPTFG--GQTAlNLAVELEESGVLekygveVLGTPVEAIKKAEDRELFREAMKEIGEP-VPESE--IAHSVEEALAA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    149 AKRIGYPVIIKASGGGggrgmrvvrgdAELAQSISMTRAE----AKAAFSNDM---VYMEKYLENPRHVEIQVLADGQGN 221
Cdd:TIGR01369  158 AKEIGYPVIVRPAFTL-----------GGTGGGIAYNREElkeiAERALSASPinqVLVEKSLAGWKEIEYEVMRDSNDN 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144    222 AIYLaerdCSMQR-----RHQK---VVeeAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLF--ENGEFYFIEMNT 291
Cdd:TIGR01369  227 CITV----CNMENfdpmgVHTGdsiVV--APSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNP 300

                          330       340       350
                   ....*....|....*....|....*....|
gi 16131144    292 RIQVEHPVTEMITGVDLIKEQLRIAAGQPL 321
Cdd:TIGR01369  301 RVSRSSALASKATGYPIAKVAAKLAVGYTL 330
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 16-290 7.42e-05

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: 44.55  E-value: 7.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  16 RILRACKELGIktvavhssadrDLKHVLLADETVCIGPAPSVKSYLNIP---AIISAAeitgavaIHPGYGFlsenaNFA 92
Cdd:COG0189  18 ALIEAAQRRGH-----------EVEVIDPDDLTLDLGRAPELYRGEDLSefdAVLPRI-------DPPFYGL-----ALL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  93 EQVERSGFIFIGPkAETIRLMGDKVSAIAAMKKAGVPCvpgsdgP---LGDDMDKNRAIAKRIGYPVIIKAsgggggrgm 169
Cdd:COG0189  75 RQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPV------PptlVTRDPDDLRAFLEELGGPVVLKP--------- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 170 rvvrgdAELAQSISMTRAEAKAAF----------SNDMVYMEKYLENPRHVEIQVLA-DGQgnaiYLAerdcSMQRRHQK 238
Cdd:COG0189 139 ------LDGSGGRGVFLVEDEDALesilealtelGSEPVLVQEFIPEEDGRDIRVLVvGGE----PVA----AIRRIPAE 204

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131144 239 -----------VVEEAPapgITPELRRyIGERCAKAcVDIGYrgAGtFEFLFENGEFYFIEMN 290
Cdd:COG0189 205 gefrtnlarggRAEPVE---LTDEERE-LALRAAPA-LGLDF--AG-VDLIEDDDGPLVLEVN 259
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 123-291 9.69e-05

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: 43.46  E-value: 9.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   123 MKKAGVPCVP----GSDGPLGDDMDKNRAIAKRIGYPVIIKAsgggggrgmrvvrgdAELAQSISMTRAEA--------K 190
Cdd:pfam07478   2 LKAAGLPVVPfvtfTRADWKLNPKEWCAQVEEALGYPVFVKP---------------ARLGSSVGVSKVESreelqaaiE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   191 AAFSND-MVYMEKYLENpRHVEIQVLADGQGNAIYLAER--DCSMQRRHQKVVEEA-----PApGITPELRRYIGERCAK 262
Cdd:pfam07478  67 EAFQYDeKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALK 144

                         170       180       190
                  ....*....|....*....|....*....|
gi 16131144   263 ACVDIGYRGAGTFE-FLFENGEFYFIEMNT 291
Cdd:pfam07478 145 AYKALGCRGLARVDfFLTEDGEIVLNEVNT 174
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 115-291 5.14e-04

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: 42.02  E-value: 5.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 115 DKVSAIAAMKKAGVPCVPGSDGPLGDDMDKnRAIAKRIGYPVIIKASgggggrgmrvvRGDAELAQSISMTRAEAKAAFS 194
Cdd:COG1181  95 DKALTKRVLAAAGLPTPPYVVLRRGELADL-EAIEEELGLPLFVKPA-----------REGSSVGVSKVKNAEELAAALE 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144 195 NDMVY-----MEKYLEnPRHVEIQVLADGQGNA-----I------------YLAErdcsmqrrhqKVVEEAPAPgITPEL 252
Cdd:COG1181 163 EAFKYddkvlVEEFID-GREVTVGVLGNGGPRAlppieIvpengfydyeakYTDG----------GTEYICPAR-LPEEL 230

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 16131144 253 RRYIGERCAKACVDIGYRGAGTFEFLF-ENGEFYFIEMNT 291
Cdd:COG1181 231 EERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
PRK14571 PRK14571
D-alanyl-alanine synthetase A; Provisional
 244-291 5.80e-04

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 184751 [Multi-domain]  Cd Length: 299  Bit Score: 41.73  E-value: 5.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 16131144  244 PAPgITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNT 291
Cdd:PRK14571 217 PAP-LNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEINT 263
carB PRK05294
carbamoyl-phosphate synthase large subunit;
110-161 3.84e-03

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 39.70  E-value: 3.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131144   110 IRLMGDKVSAI----------AAMKKAGVPcVPGSDgpLGDDMDKNRAIAKRIGYPVIIKAS 161
Cdd:PRK05294  113 VELIGAKLEAIdkaedrelfkEAMKKIGLP-VPRSG--IAHSMEEALEVAEEIGYPVIIRPS 171
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 77-292 5.52e-03

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 38.71  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144   77 AIHPGY----GFLSENAN-FAEQversGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCvPGSDGPLGDDMDKNRAIAKR 151
Cdd:PRK12767  72 LLIPLIdpelPLLAQNRDrFEEI----GVKVLVSSKEVIEICNDKWLTYEFLKENGIPT-PKSYLPESLEDFKAALAKGE 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131144  152 IGYPVIIK-----ASGggggrgmrvvrgDAELAQSISMtrAEAKAAFSNDMVYMEkYLENPRhVEIQVLADGQGNAIyla 226
Cdd:PRK12767 147 LQFPLFVKprdgsASI------------GVFKVNDKEE--LEFLLEYVPNLIIQE-FIEGQE-YTVDVLCDLNGEVI--- 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131144  227 erdCSMQRRHQKVVEEAPAPGIT---PELRRYIgERCAKAcvdIGYRGAGTFEFLFENGEFYFIEMNTR 292
Cdd:PRK12767 208 ---SIVPRKRIEVRAGETSKGVTvkdPELFKLA-ERLAEA---LGARGPLNIQCFVTDGEPYLFEINPR 269
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH