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Conserved domains on  [gi|2318375451|ref|NP_001399671|]
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acetyl-CoA carboxylase 2 isoform g [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA super family cl44129
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
58-584 5.98e-140

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


The actual alignment was detected with superfamily member COG4770:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 419.81  E-value: 5.98e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 217
Cdd:COG4770    71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSE---IPGSP-IFLMKLA 293
Cdd:COG4770   135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:COG4770   204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 452
Cdd:COG4770   284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 453 SENPDEGFKPSSGTVQELNFRSSknvwgyFSVAATGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRG 526
Cdd:COG4770   341 AEDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG 414

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2318375451 527 dFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDimlgvvcgALNVADAM 584
Cdd:COG4770   415 -VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
Biotinyl_lipoyl_domains super family cl11404
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 694-728 3.28e-03

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


The actual alignment was detected with superfamily member cd06850:

Pssm-ID: 448245 [Multi-domain]  Cd Length: 67  Bit Score: 36.63  E-value: 3.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2318375451 694 VLRSPSAGKLTQYTVEDGGHVEAGSSYA-------EMEVTAE 728
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAvleamkmENEVTAP 42
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
58-584 5.98e-140

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 419.81  E-value: 5.98e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 217
Cdd:COG4770    71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSE---IPGSP-IFLMKLA 293
Cdd:COG4770   135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:COG4770   204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 452
Cdd:COG4770   284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 453 SENPDEGFKPSSGTVQELNFRSSknvwgyFSVAATGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRG 526
Cdd:COG4770   341 AEDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG 414

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2318375451 527 dFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDimlgvvcgALNVADAM 584
Cdd:COG4770   415 -VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 58-564 7.77e-118

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 362.20  E-value: 7.77e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:PRK08591    2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltvewteddlqqg 217
Cdd:PRK08591   71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 293
Cdd:PRK08591  135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:PRK08591  204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 452
Cdd:PRK08591  284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 453 SENPDEGFKPSSGTVQelnfrssknvwGYFsvaATGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 518
Cdd:PRK08591  341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 2318375451 519 LKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 564
Cdd:PRK08591  407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 60-555 2.43e-90

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: 307.14  E-value: 2.43e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451   60 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggpnnNNYANVEL 132
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  133 IVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewted 212
Cdd:TIGR01235   66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  213 dlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIF 288
Cdd:TIGR01235  135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  289 LMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY 368
Cdd:TIGR01235  199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  369 SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLK-------DIRLlygespwgvtpisfetpsnppl 441
Cdd:TIGR01235  279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  442 aRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGG-------LHEFADSQFGHCFSWGENREEAISN 514
Cdd:TIGR01235  337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2318375451  515 MVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:TIGR01235  410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 218-411 2.41e-55

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: 188.67  E-value: 2.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 KRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSP----IFLMKLA 293
Cdd:pfam02786  10 KEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQD-G 372
Cdd:pfam02786  90 KGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsG 169

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2318375451 373 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 411
Cdd:pfam02786 170 EYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 449-555 2.19e-34

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: 126.76  E-value: 2.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  449 ARITSENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAATGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 526
Cdd:smart00878   2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79

                           90       100
                   ....*....|....*....|....*....
gi 2318375451  527 dFRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:smart00878  80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 694-728 3.28e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 36.63  E-value: 3.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2318375451 694 VLRSPSAGKLTQYTVEDGGHVEAGSSYA-------EMEVTAE 728
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAvleamkmENEVTAP 42
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 693-725 3.42e-03

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 36.81  E-value: 3.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2318375451 693 TVLRSPSAGKL-----TQYTVEDGGHVEAGSSYAEMEV 725
Cdd:pfam00364   1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEA 38
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
58-584 5.98e-140

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


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 419.81  E-value: 5.98e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:COG4770     2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 217
Cdd:COG4770    71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSE---IPGSP-IFLMKLA 293
Cdd:COG4770   135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:COG4770   204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 452
Cdd:COG4770   284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 453 SENPDEGFKPSSGTVQELNFRSSknvwgyFSVAATGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRG 526
Cdd:COG4770   341 AEDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG 414

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2318375451 527 dFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDimlgvvcgALNVADAM 584
Cdd:COG4770   415 -VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 58-564 7.77e-118

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 362.20  E-value: 7.77e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:PRK08591    2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltvewteddlqqg 217
Cdd:PRK08591   71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 293
Cdd:PRK08591  135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:PRK08591  204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 452
Cdd:PRK08591  284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 453 SENPDEGFKPSSGTVQelnfrssknvwGYFsvaATGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 518
Cdd:PRK08591  341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 2318375451 519 LKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 564
Cdd:PRK08591  407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 56-555 3.19e-111

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 364.07  E-value: 3.19e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451   56 RVIEKVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEYIkmadhyVPVPGGPNNNnYAN 129
Cdd:PRK12999     3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYL------IGEGKHPVRA-YLD 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  130 VELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGltvew 209
Cdd:PRK12999    67 IDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP----- 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  210 teddlqqgkrisvpedvydkgcVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP 286
Cdd:PRK12999   142 ----------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGND 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  287 -IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVE 365
Cdd:PRK12999   200 eVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVE 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  366 YLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRL-------KDIRLlygespwgvtpisfetpsn 438
Cdd:PRK12999   280 FLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLHDLeigipsqEDIRL------------------- 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  439 pplaRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGGLHeFADSQFGHCF--------SWGENREE 510
Cdd:PRK12999   341 ----RGYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVRLDGGNA-FAGAEITPYYdsllvkltAWGRTFEQ 409

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 2318375451  511 AISNMVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:PRK12999   410 AVARMRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 58-555 1.26e-108

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: 357.08  E-value: 1.26e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451   58 IEKVLIANNG-IAavkcmrsIR--RWAYEMfrnerAIRFVVMVTPED------LKANAEY-IKMADHyvPVpggpnnNNY 127
Cdd:COG1038      4 IKKVLVANRGeIA-------IRvfRAATEL-----GIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------DAY 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  128 ANVELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltv 207
Cdd:COG1038     64 LDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GT---- 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  208 ewteddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---G 284
Cdd:COG1038    138 ---------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafG 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  285 SP-IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGT 363
Cdd:COG1038    197 DDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGT 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  364 VEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-------RLKDIRLlygespwgvtpisfetp 436
Cdd:COG1038    277 VEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDdpeigipSQEDIRL----------------- 339

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  437 snpplaRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSV---AATGglheFA--------DSQFGHCFSWG 505
Cdd:COG1038    340 ------NGYAIQCRITTEDPANNFMPDTGRITA--YRSA----GGFGIrldGGNA----YTgavitpyyDSLLVKVTAWG 403

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2318375451  506 ENREEAISNMVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:COG1038    404 RTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 58-557 3.80e-106

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 331.99  E-value: 3.80e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:PRK06111    2 FQKVLIANRGEIAVRIIRTCQKLG---------IRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTvewteddlqqg 217
Cdd:PRK06111   71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLE----------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydkgcvkDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 293
Cdd:PRK06111  140 ----------------DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYI 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:PRK06111  204 EDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKN 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 452
Cdd:PRK06111  284 FYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIY 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 453 SENPDEgFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTV 532
Cdd:PRK06111  341 AEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNI 418

                         490       500
                  ....*....|....*....|....*.
gi 2318375451 533 EYLINLLETESFQNNDIDTGWL-DYL 557
Cdd:PRK06111  419 PLLLQVLEDPVFKAGGYTTGFLtKQL 444
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
59-555 4.95e-106

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 333.49  E-value: 4.95e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  59 EKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAK 138
Cdd:PRK08654    3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 139 RIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqgk 218
Cdd:PRK08654   72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGT----------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 219 risvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSeIPGS-----PIFLMKLA 293
Cdd:PRK08654  135 ----------EEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQS-IAQSafgdsTVFIEKYL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSqDGS 373
Cdd:PRK08654  204 EKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGN 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 452
Cdd:PRK08654  283 FYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRIN 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 453 SENPDEGFKPSSGTVQelNFRSSknvwGYFSVAATGGLH------EFADSQFGHCFSWGENREEAISNMVVALKELSIRG 526
Cdd:PRK08654  340 AEDPLNDFAPSPGKIK--RYRSP----GGPGVRVDSGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYVIVG 413

                         490       500
                  ....*....|....*....|....*....
gi 2318375451 527 dFRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:PRK08654  414 -VKTNIPFHKAVMENENFVRGNLHTHFIE 441
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
58-554 4.86e-96

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 305.48  E-value: 4.86e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:PRK05586    2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 217
Cdd:PRK05586   71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIFLMKLA 293
Cdd:PRK05586  135 -----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFI 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:PRK05586  204 ENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGN 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 452
Cdd:PRK05586  284 FYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSiKQEDIKI-----------------------NGHSIECRIN 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 453 SENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTV 532
Cdd:PRK05586  341 AEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNI 419

                         490       500
                  ....*....|....*....|..
gi 2318375451 533 EYLINLLETESFQNNDIDTGWL 554
Cdd:PRK05586  420 DFQFIILEDEEFIKGTYDTSFI 441
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 58-564 4.54e-94

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 300.90  E-value: 4.54e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDLKANAeyIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:PRK12833    5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 217
Cdd:PRK12833   74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAED----FPILFRQVQSEIPGSPIFLMKLA 293
Cdd:PRK12833  138 -----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQlaaeLPLAQREAQAAFGDGGVYLERFI 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYgNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY-SQDG 372
Cdd:PRK12833  207 ARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARG 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 373 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARI 451
Cdd:PRK12833  286 EFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRfAQGDIAL-----------------------RGAALECRI 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 452 TSENPDEGFKPSSGTVQELNF------RSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELSIR 525
Cdd:PRK12833  343 NAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRID 416

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 2318375451 526 GdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 564
Cdd:PRK12833  417 G-MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
58-555 5.32e-94

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 300.12  E-value: 5.32e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayEMfrNERAIrfVVMVTPEDlkaNAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:PRK08462    4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 217
Cdd:PRK08462   73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIFLMKLA 293
Cdd:PRK08462  137 -----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFI 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:PRK08462  206 NNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 374 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARITS 453
Cdd:PRK08462  286 FYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITA 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 454 ENPdEGFKPSSGTVQEL------NFRSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 527
Cdd:PRK08462  343 EDP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG- 414

                         490       500
                  ....*....|....*....|....*...
gi 2318375451 528 FRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:PRK08462  415 IKTTIPFHLEMMENADFINNKYDTKYLE 442
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 60-555 2.43e-90

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: 307.14  E-value: 2.43e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451   60 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggpnnNNYANVEL 132
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  133 IVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewted 212
Cdd:TIGR01235   66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  213 dlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIF 288
Cdd:TIGR01235  135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  289 LMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY 368
Cdd:TIGR01235  199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  369 SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLK-------DIRLlygespwgvtpisfetpsnppl 441
Cdd:TIGR01235  279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  442 aRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGG-------LHEFADSQFGHCFSWGENREEAISN 514
Cdd:TIGR01235  337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2318375451  515 MVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:TIGR01235  410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
57-555 3.00e-89

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 288.54  E-value: 3.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  57 VIEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYV-----PVPGgpnnnnYANVE 131
Cdd:PRK07178    1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYsigadPLAG------YLNPR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 132 LIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewte 211
Cdd:PRK07178   64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS---------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 212 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-I 287
Cdd:PRK07178  134 -----------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeV 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 288 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 367
Cdd:PRK07178  197 FLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFL 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 368 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHV 446
Cdd:PRK07178  277 LDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFA 333

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 447 IAARITSENPDEGFKPSSGTVQElnfrssknvwgYFSVAATG---------GLH--EFADSQFGHCFSWGENREEAISNM 515
Cdd:PRK07178  334 LQFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRG 402

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 2318375451 516 VVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:PRK07178  403 RRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 58-578 1.11e-70

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 239.33  E-value: 1.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNnYANVELIVDIA 137
Cdd:PRK08463    2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRIGTDPIKG-YLDVKRIVEIA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsgsgltvewteddlqqg 217
Cdd:PRK08463   70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVP------------------ 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 krisvpedvydkGCVKDVDEGLEA----AERIGFPLMIKASEGGGGKGIRKAESAEDFPILF----RQVQSEIPGSPIFL 289
Cdd:PRK08463  132 ------------GTEKLNSESMEEikifARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFM 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 290 MKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYS 369
Cdd:PRK08463  200 EKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 370 QDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLhrlkdirllygespwgvtpisfETPSNPPLARGHVIAA 449
Cdd:PRK08463  280 DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEIL----------------------DLEQSDIKPRGFAIEA 337

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 450 RITSENPDEGFKPSSGTVQEL------NFRSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELS 523
Cdd:PRK08463  338 RITAENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFV 411

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2318375451 524 IRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA------EKPDIMLGVVCGAL 578
Cdd:PRK08463  412 IDG-IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVIAAIAAAL 471
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 218-411 2.41e-55

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: 188.67  E-value: 2.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 218 KRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSP----IFLMKLA 293
Cdd:pfam02786  10 KEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 294 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQD-G 372
Cdd:pfam02786  90 KGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsG 169

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2318375451 373 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 411
Cdd:pfam02786 170 EYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
 58-176 2.90e-43

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: 151.87  E-value: 2.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  58 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 137
Cdd:pfam00289   1 IKKVLIANRGEIAVRIIRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2318375451 138 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEA 176
Cdd:pfam00289  70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 130-410 1.85e-39

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


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 146.56  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 130 VELIVDIAKRIPVQAVWAGWGHASEnpKLPELLCKNGVAflGPPSEAMWALGDKIASTVVAQTLQVPTlPWSGsgltvew 209
Cdd:COG0439     6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 210 teddlqqgkrisvpedvydkgCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEI----PGS 285
Cdd:COG0439    74 ---------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 286 PIFLMKLAQHaRHLEVQILADQyGNAVSlfgrdCSIQRRHQK---IVE---EAPATIAPlAIFEFMEQCAIRLAKTVGYV 359
Cdd:COG0439   133 EVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPLPE-ELRAEIGELVARALRALGYR 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2318375451 360 -SAGTVEYLYSQDGSFHFLELNPRLQVEH--PCTEMIADVNLPAAQLQIAMGVP 410
Cdd:COG0439   205 rGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 449-555 2.19e-34

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: 126.76  E-value: 2.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  449 ARITSENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAATGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 526
Cdd:smart00878   2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79

                           90       100
                   ....*....|....*....|....*....
gi 2318375451  527 dFRTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:smart00878  80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 449-555 1.80e-30

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: 115.67  E-value: 1.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 449 ARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 528
Cdd:pfam02785   2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80

                          90       100
                  ....*....|....*....|....*..
gi 2318375451 529 RTTVEYLINLLETESFQNNDIDTGWLD 555
Cdd:pfam02785  81 KTNIPFLRAILEHPDFRAGEVDTGFLE 107
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
112-411 5.78e-12

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 68.03  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 112 ADHYVPVPGgPNNNNYANVELIVDIAKRIPVQAVWA---GWGHA-SEN-PKLPEllcknGVAFLGPPSEAMWALGDKIAS 186
Cdd:COG3919    48 VDEVVVVPD-PGDDPEAFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 187 TVVAQTLQVPtlpwsgsgltvewteddlqqgkrisVPEDVYdkgcVKDVDEGLEAAERIGFPLMIKASEG--------GG 258
Cdd:COG3919   122 YELAEELGVP-------------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 259 GKGIRKAESAEDFPILFRQ---------VQSEIPG--SPIFLmklaqharhleVQILADQYGNAVSLFGrdcsiqrrHQK 327
Cdd:COG3919   173 KKKVFYVDDREELLALLRRiaaagyeliVQEYIPGddGEMRG-----------LTAYVDRDGEVVATFT--------GRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 328 IVEeAPATIAPLAIFEF-----MEQCAIRLAKTVGYVSAGTVEYLY-SQDGSFHFLELNPRLQVEHPCTEmIADVNLPAA 401
Cdd:COG3919   234 LRH-YPPAGGNSAARESvddpeLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYL 311

                         330
                  ....*....|
gi 2318375451 402 QLQIAMGVPL 411
Cdd:COG3919   312 LYDDAVGRPL 321
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 206-437 3.53e-08

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: 57.32  E-value: 3.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  206 TVEWTED-DLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASE--GGGGKGIrkAESAEDFPILFRQVQSEI 282
Cdd:TIGR01369  121 AIKKAEDrELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSAS 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  283 PGSPIFLMKLAQHARHLEVQILADQYGNAVSLfgrdCSIQR-----RH--QKIVeeapatIAP---LAIFEF--MEQCAI 350
Cdd:TIGR01369  199 PINQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHtgDSIV------VAPsqtLTDKEYqmLRDASI 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  351 RLAKTVGYVSAGTVEY-LYSQDGSFHFLELNPRLQ---------VEHPctemIADVnlpAAQLqiAMGVPLHRLK-DIRl 419
Cdd:TIGR01369  269 KIIRELGIEGGCNVQFaLNPDSGRYYVIEVNPRVSrssalaskaTGYP----IAKV---AAKL--AVGYTLDELKnPVT- 338

                          250
                   ....*....|....*...
gi 2318375451  420 lygespwGVTPISFEtPS 437
Cdd:TIGR01369  339 -------GTTPASFE-PS 348
PLN02735 PLN02735
carbamoyl-phosphate synthase
 230-382 2.47e-07

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 54.40  E-value: 2.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  230 GCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDfpiLFRQVQSEI---PGSPIFLMKLAQHARHLEVQILAD 306
Cdd:PLN02735   721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  307 QYGNAV-----------SLFGRD--CSIQRrhQKIVEEAPATIaplaifefmEQCAIRLAKTVGYVSAGTVEYLYSQDGS 373
Cdd:PLN02735   798 SEGNVViggimehieqaGVHSGDsaCSLPT--QTIPSSCLATI---------RDWTTKLAKRLNVCGLMNCQYAITPSGE 866


                   ....*....
gi 2318375451  374 FHFLELNPR 382
Cdd:PLN02735   867 VYIIEANPR 875
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 232-411 8.14e-07

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


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 52.69  E-value: 8.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  232 VKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADqyGNA 311
Cdd:TIGR01369  690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451  312 VSLFGrdcsIQrRHqkiVEEA-----------PATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSqDGSFHFLELN 380
Cdd:TIGR01369  768 VLIPG----IM-EH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVN 838

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2318375451  381 PRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 411
Cdd:TIGR01369  839 PRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 232-382 1.03e-05

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: 48.72  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 232 VKDVDEGLEAAERIGFPLMIKASE--GGGGKGIrkAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYG 309
Cdd:COG0458   135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 310 NAVSLfgrdCSIQrrHqkiVEEA------PATIAP-----LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYsQDGSFHFLE 378
Cdd:COG0458   213 NVIIV----GIME--H---IEPAgvhsgdSICVAPpqtlsDKEYQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYVIE 282


                  ....
gi 2318375451 379 LNPR 382
Cdd:COG0458   283 VNPR 286
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 232-382 2.86e-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: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 232 VKDVDEGLEAAERIGFPLMIKASEGG-GGKGIRKAESAEDFPilfrQVQSEIPGSPIFLMKLAQHARHLEVQILADQYGN 310
Cdd:pfam02222  13 AESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDRELSVLVVRSVDGE 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2318375451 311 AVSlfgrdCS-IQRRHQK-IVEE--APATIaPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPR 382
Cdd:pfam02222  89 TAF-----YPvVETIQEDgICRLsvAPARV-PQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPR 158
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 220-382 5.17e-04

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 42.95  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 220 ISVPeDVYDKGCVKDVDEGLEAAErIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQ-----VQSEIPGSPIflmklaq 294
Cdd:PRK12767  124 IPTP-KSYLPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY------- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 295 harhlEVQILADQYGNAVSLFGRdcsiqRR--------HQKIVEEAPAtiaplaIFEFMEqcaiRLAKTVGYVSAGTVEY 366
Cdd:PRK12767  195 -----TVDVLCDLNGEVISIVPR-----KRievragetSKGVTVKDPE------LFKLAE----RLAEALGARGPLNIQC 254

                         170
                  ....*....|....*.
gi 2318375451 367 LYSqDGSFHFLELNPR 382
Cdd:PRK12767  255 FVT-DGEPYLFEINPR 269
carB PRK05294
carbamoyl-phosphate synthase large subunit;
232-271 6.77e-04

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 43.16  E-value: 6.77e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2318375451  232 VKDVDEGLEAAERIGFPLMIKAS--EGGGGKGIrkAESAEDF 271
Cdd:PRK05294   149 AHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 232-396 2.02e-03

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


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 40.69  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 232 VKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEipGSPIFLmklaqharhleVQ--ILADQyg 309
Cdd:COG0189   117 TRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTEL--GSEPVL-----------VQefIPEED-- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 310 navslfGRD-----------CSIQRR----HQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGtVEYLYSQDGsF 374
Cdd:COG0189   182 ------GRDirvlvvggepvAAIRRIpaegEFRTNLARGGRAEPVELTDEERELALRAAPALGLDFAG-VDLIEDDDG-P 253

                         170       180
                  ....*....|....*....|..
gi 2318375451 375 HFLELNPRlqvehPCTEMIADV 396
Cdd:COG0189   254 LVLEVNVT-----PGFRGLERA 270
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 694-728 3.28e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 36.63  E-value: 3.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2318375451 694 VLRSPSAGKLTQYTVEDGGHVEAGSSYA-------EMEVTAE 728
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAvleamkmENEVTAP 42
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 693-725 3.42e-03

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 36.81  E-value: 3.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2318375451 693 TVLRSPSAGKL-----TQYTVEDGGHVEAGSSYAEMEV 725
Cdd:pfam00364   1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEA 38
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 240-384 4.51e-03

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 38.52  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318375451 240 EAAERIGFPLMIKASEGGGGKGIRKAE--SAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQIlADQY-GNAVSLF- 315
Cdd:pfam02655  25 EELLREEKKYVVKPRDGCGGEGVRKVEngREDEAFIENVLVQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFv 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2318375451 316 ---GRDCSIQRRHQKIVEEApatiaplaifefmEQCAIRLAKTVGYVSagtVEYLYSqDGSFHFLELNPRLQ 384
Cdd:pfam02655 104 yagNVTPSRTELKEEIIELA-------------EEVVECLPGLRGYVG---VDLVLK-DNEPYVIEVNPRIT 158
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 232-262 4.54e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 40.52  E-value: 4.54e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2318375451 232 VKDVDEGLEAAERIGFPLMIKASEGGGGKGI 262
Cdd:PRK14016  235 VTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
 
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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