|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-457 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 980.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGADPLAGYLNPRALVNLAVESGCDALHPG 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPLAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 81 YGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKATS 160
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 161 GGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIEI 240
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLEL 319
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 320 SVKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEALD 399
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALD 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600629 400 RGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESHPELTQYSIKRNPSHL 457
Cdd:PRK07178 401 RGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPEEL 458
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-442 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 768.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGADPLA-GYLNPRALVNLAVESGCDALHP 79
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAeSYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 80 GYGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKAT 159
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 160 SggggrgirrCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIE 239
Cdd:COG4770 161 AggggkgmrvVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLE 318
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 319 LSVKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEAL 398
Cdd:COG4770 321 LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15600629 399 DRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESH 442
Cdd:COG4770 401 ARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERE 444
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-442 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 708.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGADPLA-GYLNPRALVNLAVESGCDALHP 79
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKkSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 80 GYGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKAT 159
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 160 SGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIE 239
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLE 318
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYeKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 319 LSVKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEAL 398
Cdd:PRK08591 321 LSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15600629 399 DRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESH 442
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-453 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 690.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGAD--PLAGYLNPRALVNLAVESGCDALH 78
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGkhPVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 79 PGYGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKA 158
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 159 TSGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLI 238
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGL 317
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 318 ELS------VKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDT-AIYTGYTIPPYYDSMCLKLIVW 390
Cdd:PRK12999 324 TLHdleigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTAW 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600629 391 ALTWEEALDRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESHPELTQYSIKRN 453
Cdd:PRK12999 404 GRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRD 466
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-453 |
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: 690.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGAD--PLAGYLNPRALVNLAVESGCDALH 78
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGkgPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 79 PGYGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKA 158
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 159 TSGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLI 238
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGL 317
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 318 ELSVK------QDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTD--TAiYTGYTIPPYYDSMCLKLIV 389
Cdd:COG1038 323 SLDDPeigipsQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDggNA-YTGAVITPYYDSLLVKVTA 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600629 390 WALTWEEALDRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESHPELTQYSIKRN 453
Cdd:COG1038 402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRD 465
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-447 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 655.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIG-ADPLAGYLNPRALVNLAVESGCDALHP 79
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGpAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 80 GYGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKAT 159
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 160 SGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIE 239
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLEL 319
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 320 SVKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEALD 399
Cdd:PRK08654 321 SFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15600629 400 RGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESHPELTQ 447
Cdd:PRK08654 401 RMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILE 448
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-442 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 608.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGADPLA-GYLNPRALVNLAVESGCDALHP 79
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQeSYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 80 GYGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKAT 159
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 160 SGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIE 239
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLADGE-VYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLE 318
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 319 LSVKQDDIVHRGYALQFRINAEDPKnNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEAL 398
Cdd:PRK06111 321 LSFTQDDIKRSGHAIEVRIYAEDPK-TFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15600629 399 DRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESH 442
Cdd:PRK06111 400 SRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQ 443
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-445 |
0e+00 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 598.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGADPLA-GYLNPRALVNLAVESGCDALHP 79
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAkSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 80 GYGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKAT 159
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 160 SGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIE 239
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLE 318
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLdKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 319 LSVKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEAL 398
Cdd:TIGR00514 321 LSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15600629 399 DRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESHPEL 445
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-440 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 583.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIG-ADPLAGYLNPRALVNLAVESGCDALHP 79
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGpASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 80 GYGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKAT 159
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 160 SGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIE 239
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLE 318
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 319 LSVKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEAL 398
Cdd:PRK05586 321 LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15600629 399 DRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVE 440
Cdd:PRK05586 401 QKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIE 442
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-442 |
0e+00 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 551.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGADPLAGYLNPRALVNLAVESGCDALHPG 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIKGYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 81 YGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALRE-AERIGYPVMLKAT 159
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESMEEIKIfARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 160 SGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIE 239
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLAD-GEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLE 318
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDyNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 319 LSVKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEAL 398
Cdd:PRK08463 321 LDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15600629 399 DRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESH 442
Cdd:PRK08463 401 NKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETH 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: 530.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 2 IKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIG-ADPLAGYLNPRALVNLAVESGCDALHPG 80
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGpSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 81 YGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKATS 160
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 161 GGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSfGNTVHLFERDCSIQRRNQKLIEI 240
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDG-ERVVHLFERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLAD--GEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLE 318
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 319 LSVKQDDIVHRGYALQFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEAL 398
Cdd:PRK12833 324 LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15600629 399 DRGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVES 441
Cdd:PRK12833 404 ARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEA 446
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-442 |
1.48e-176 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 502.35 E-value: 1.48e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 2 IKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIGADPLA-GYLNPRALVNLAVESGCDALHPG 80
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSeSYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 81 YGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKATS 160
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 161 GGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIEI 240
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLEL 319
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 320 SvKQDDIVHRGYALQFRINAEDPKnNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEALD 399
Cdd:PRK08462 324 P-SQESIKLKGHAIECRITAEDPK-KFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15600629 400 RGLRALDDMRVQGVKTTAPYYQEILRNPEFRSGQFNTSFVESH 442
Cdd:PRK08462 402 KMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
114-320 |
3.02e-79 |
|
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: 245.29 E-value: 3.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 114 DKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIGYPVMLKATSGGGGRGIRRCNSREELEQAFPRVISEATKAFGS 193
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 194 AEVFLEKCIVNPKHIEAQILADSFGNTVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTV 273
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600629 274 EFLL--ADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLELS 320
Cdd:pfam02786 161 EFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
69-318 |
1.17e-60 |
|
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: 198.94 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 69 AVESGCDALHPGYGF---LSENAEL----AEICAERGIkfIGPSAQVIRRMGDKTEARRSMIAAGVPcTPGTEGnVADLA 141
Cdd:COG0439 4 AIIAAAAELARETGIdavLSESEFAvetaAELAEELGL--PGPSPEAIRAMRDKVLMREALAAAGVP-VPGFAL-VDSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 142 EALREAERIGYPVMLKATSGGGGRGIRRCNSREELEQAFPRVISEATKAFGSAEVFLEKCIVNPkHIEAQILADSfGNTV 221
Cdd:COG0439 80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGR-EYSVEGLVRD-GEVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 222 HlferdCSIQRRNQK------LIEIAPSPqLTPEQRAYIGDLAVRAAKAVGYEN-AGTVEFLL-ADGEVYFMEMNTRVQV 293
Cdd:COG0439 158 V-----CSITRKHQKppyfveLGHEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLtPDGEPYLIEINARLGG 231
|
250 260
....*....|....*....|....*..
gi 15600629 294 EH--TITEEITGIDVVREQIRIASGLE 318
Cdd:COG0439 232 EHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-440 |
6.88e-60 |
|
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: 191.55 E-value: 6.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 334 QFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEALDRGLRALDDMRVQGV 413
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*..
gi 15600629 414 KTTAPYYQEILRNPEFRSGQFNTSFVE 440
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLE 107
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-108 |
1.24e-59 |
|
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: 190.78 E-value: 1.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 2 IKKILIANRGEIAVRIVRACAEMGIRSVAVYSEADRHALHVKRADEAHSIG-ADPLAGYLNPRALVNLAVESGCDALHPG 80
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGpGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 15600629 81 YGFLSENAELAEICAERGIKFIGPSAQV 108
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-440 |
2.64e-58 |
|
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: 187.24 E-value: 2.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 334 QFRINAEDPKNNFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCLKLIVWALTWEEALDRGLRALDDMRVQGV 413
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 15600629 414 KTTAPYYQEILRNPEFRSGQFNTSFVE 440
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
17-291 |
1.46e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 74.96 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 17 IVRACAEMGIRSVAVYSEADRHALHVKRADEAH---SIGADPlAGYLnpRALVNLAVESGCDALHPGY----GFLSENAE 89
Cdd:COG3919 20 VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvvpDPGDDP-EAFV--DALLELAERHGPDVLIPTGdeyvELLSRHRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 90 laEIcaERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPcTPGTEgnVADLAEALRE-AERIGYPVMLKATSGGGGRGIR 168
Cdd:COG3919 97 --EL--EEHYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTV--VLDSADDLDAlAEDLGFPVVVKPADSVGYDELS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 169 R--------CNSREELEQAFPRViseatkAFGSAEVFLEKCIvnPKHIEAQI----LADSFGNTVHLFerdcsIQRR--- 233
Cdd:COG3919 170 FpgkkkvfyVDDREELLALLRRI------AAAGYELIVQEYI--PGDDGEMRgltaYVDRDGEVVATF-----TGRKlrh 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600629 234 ------NQKLIEIAPSPQLTpeqrayigDLAVRAAKAVGYENAGTVEFLL--ADGEVYFMEMNTRV 291
Cdd:COG3919 237 yppaggNSAARESVDDPELE--------EAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRF 294
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
89-291 |
2.31e-14 |
|
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: 75.30 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 89 ELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEgnVADLAEALREAERIGYPVMLKATSGGGGRGIR 168
Cdd:COG0458 89 ELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGT--ATSVEEALAIAEEIGYPVIVRPSYVLGGRGMG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 169 RCNSREELEqafpRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLferdCSIQrrNqklIE--------- 239
Cdd:COG0458 167 IVYNEEELE----EYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEpagvhsgds 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600629 240 --IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLADGEVYFMEMNTRV 291
Cdd:COG0458 234 icVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRA 287
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
75-332 |
8.24e-13 |
|
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: 70.80 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 75 DALHPGYG---FLSENAELAE--ICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGteGNVADLAEALREAER 149
Cdd:TIGR01369 83 DAILPTFGgqtALNLAVELEEsgVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSVEEALAAAKE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 150 IGYPVMLKATSGGGGRGIRRCNSREELEqafpRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGN--TVhlferd 227
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELK----EIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNciTV------ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 228 CSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL--ADGEVYFMEMNTRVQVEHTITE 299
Cdd:TIGR01369 231 CNMENfdpmgvHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALnpDSGRYYVIEVNPRVSRSSALAS 310
|
250 260 270
....*....|....*....|....*....|...
gi 15600629 300 EITGIDVVREQIRIASGLELSVKQDDIVHRGYA 332
Cdd:TIGR01369 311 KATGYPIAKVAAKLAVGYTLDELKNPVTGTTPA 343
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
75-406 |
5.21e-11 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 65.18 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 75 DALHPGYG---FLSENAELAE--ICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVadLAEALREAER 149
Cdd:PLN02735 100 DALLPTMGgqtALNLAVALAEsgILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATT--LDECFEIAED 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 150 IG-YPVMLKATSGGGGRGIRRCNSREELEQafprVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNTVHLferdC 228
Cdd:PLN02735 178 IGeFPLIIRPAFTLGGTGGGIAYNKEEFET----ICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVII----C 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 229 SIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGT-VEFLL--ADGEVYFMEMNTRVQVEHTITE 299
Cdd:PLN02735 250 SIENidpmgvHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSnVQFAVnpVDGEVMIIEMNPRVSRSSALAS 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 300 EITGIDVVREQIRIASGLELSVKQDDIVHRGYAlqfrinaedpknNFLPSFG----KITRYY---APGGPGVRTDTAIYT 372
Cdd:PLN02735 330 KATGFPIAKMAAKLSVGYTLDQIPNDITLKTPA------------SFEPSIDyvvtKIPRFAfekFPGSQPILTTQMKSV 397
|
330 340 350
....*....|....*....|....*....|....
gi 15600629 373 GytippyyDSMCLklivwALTWEEALDRGLRALD 406
Cdd:PLN02735 398 G-------EAMAL-----GRTFQESFQKALRSLE 419
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
90-319 |
4.96e-10 |
|
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: 61.94 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 90 LAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEgnVADLAEALREAERIGYPVMLKATSGGGGRGIRR 169
Cdd:TIGR01369 645 LAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKT--ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEI 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 170 CNSREELEqafpRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADsfGNTVHLferdCSIQRRnqklIEIA-------- 241
Cdd:TIGR01369 723 VYNEEELR----RYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEEVLI----PGIMEH----IEEAgvhsgdst 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 242 ---PSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLADGEVYFMEMNTRVQVEHTITEEITGIDVVREQIRIASGLE 318
Cdd:TIGR01369 789 cvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKK 868
|
.
gi 15600629 319 L 319
Cdd:TIGR01369 869 L 869
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
22-287 |
1.91e-09 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 58.93 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 22 AEMGIRsVAVYSEADrhalhvkrADEAHSIGAD-PLAGYLNPRALVNLAveSGCDALhpgyGFLSEN--AELAEICAERg 98
Cdd:COG0026 11 KRLGYR-VHVLDPDP--------DSPAAQVADEhIVADYDDEEALREFA--ERCDVV----TFEFENvpAEALEALEAE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 99 iKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEgnVADLAEALREAERIGYPVMLKAtsggggrgirrC-------- 170
Cdd:COG0026 75 -VPVRPGPEALEIAQDRLLEKAFLAELGIPVAPFAA--VDSLEDLEAAIAELGLPAVLKT-----------Rrggydgkg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 171 ----NSREELEQAFprviseatKAFGSAEVFLEKCIvnpkHIE---AQILA-DSFGNTVH--LFErdcSIQRRNQkLIE- 239
Cdd:COG0026 141 qvviKSAADLEAAW--------AALGGGPCILEEFV----PFErelSVIVArSPDGEVATypVVE---NVHRNGI-LDEs 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15600629 240 IAPSpQLTPEQRAYIGDLAVRAAKAVGYenAGT--VE-FLLADGEVYFMEM 287
Cdd:COG0026 205 IAPA-RISEALAAEAEEIAKRIAEALDY--VGVlaVEfFVTKDGELLVNEI 252
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
59-289 |
9.89e-09 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 56.65 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 59 YLNPRALVNLAVESGCD----ALHPGYGflsENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTE 134
Cdd:COG1181 39 GIDVEDLPAALKELKPDvvfpALHGRGG---EDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 135 GNVADLAEALREAERIGYPVMLKAT--------SggggrgirRCNSREELEQAfprvISEATKaFGSaEVFLEKCI---- 202
Cdd:COG1181 116 LRRGELADLEAIEEELGLPLFVKPAregssvgvS--------KVKNAEELAAA----LEEAFK-YDD-KVLVEEFIdgre 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 203 -----VNPKHIEA----QILADS-F---------GNTVHlferdcsiqrrnqklieIAPSPqLTPEQRAYIGDLAVRAAK 263
Cdd:COG1181 182 vtvgvLGNGGPRAlppiEIVPENgFydyeakytdGGTEY-----------------ICPAR-LPEELEERIQELALKAFR 243
|
250 260
....*....|....*....|....*..
gi 15600629 264 AVGYENAGTVEFLL-ADGEVYFMEMNT 289
Cdd:COG1181 244 ALGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
75-291 |
1.48e-08 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 57.41 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 75 DALHPGYG---FLSENAELAE--ICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGteGNVADLAEALREAER 149
Cdd:PRK05294 84 DAILPTMGgqtALNLAVELAEsgVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAHSMEEALEVAEE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 150 IGYPVMLKAT-------SggggrgiRRCNSREELEqafpRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGN--T 220
Cdd:PRK05294 162 IGYPVIIRPSftlggtgG-------GIAYNEEELE----EIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNciI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 221 VhlferdCSIQrrNqkL----------IEIAPSPQLTPE--QRAYigDLAVRAAKAVGYENAGT-VEFLL--ADGEVYFM 285
Cdd:PRK05294 231 V------CSIE--N--IdpmgvhtgdsITVAPAQTLTDKeyQMLR--DASIAIIREIGVETGGCnVQFALnpKDGRYIVI 298
|
....*.
gi 15600629 286 EMNTRV 291
Cdd:PRK05294 299 EMNPRV 304
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
21-290 |
1.72e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 56.05 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 21 CAEMGIRSVAVYsEADRHALhVKRADEAHSIgadplagylnpRALVNLAVESGCDALHPGY----GFLSENAELAEicaE 96
Cdd:PRK12767 30 GADISELAPALY-FADKFYV-VPKVTDPNYI-----------DRLLDICKKEKIDLLIPLIdpelPLLAQNRDRFE---E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 97 RGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPcTPGT--EGNVADLAEALREAErIGYPVMLKATSGGGGRGIRRCNSRE 174
Cdd:PRK12767 94 IGVKVLVSSKEVIEICNDKWLTYEFLKENGIP-TPKSylPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVNDKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 175 ELEQAFPRViseatkafgsAEVFLEKCIVNPKhIEAQILADSFGNTVHLFER----------DCSIQRRNQKLIeiapsp 244
Cdd:PRK12767 172 ELEFLLEYV----------PNLIIQEFIEGQE-YTVDVLCDLNGEVISIVPRkrievragetSKGVTVKDPELF------ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15600629 245 qltpeqrayigDLAVRAAKAVGYENAGTVEFLLADGEVYFMEMNTR 290
Cdd:PRK12767 235 -----------KLAERLAEALGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
89-320 |
2.27e-08 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 56.90 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 89 ELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNvaDLAEALREAERIGYPVMLKATSggggrgir 168
Cdd:PRK12815 645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTAT--DEEEAFAFAKRIGYPVLIRPSY-------- 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 169 rcnsreeleqafprVIseatKAFGSAEVF----LEKCIVNPKHIEAQILADSF-------------GNTVHL------FE 225
Cdd:PRK12815 715 --------------VI----GGQGMAVVYdepaLEAYLAENASQLYPILIDQFidgkeyevdaisdGEDVTIpgiiehIE 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 226 RDCSiqrRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLADGEVYFMEMNTRVQveHT--ITEEITG 303
Cdd:PRK12815 777 QAGV---HSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRAS--RTvpFVSKATG 851
|
250
....*....|....*..
gi 15600629 304 IDVVREQIRIASGLELS 320
Cdd:PRK12815 852 VPLAKLATKVLLGKSLA 868
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
75-332 |
1.25e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 54.20 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 75 DALHPGYGflSENA-----ELAE--ICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPcTPGTEgNVADLAEALREA 147
Cdd:PRK12815 84 DALLATLG--GQTAlnlavKLHEdgILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEP-VPESE-IVTSVEEALAFA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 148 ERIGYPVMLKATSGGGGRGIRRCNSREELEQAFPRviSEATKAFgsAEVFLEKCIVNPKHIEAQILADSFGNTVHLferd 227
Cdd:PRK12815 160 EKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQ--GLQASPI--HQCLLEESIAGWKEIEYEVMRDRNGNCITV---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 228 CSIQRrnqklIE-----------IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL--ADGEVYFMEMNTRVQVE 294
Cdd:PRK12815 232 CNMEN-----IDpvgihtgdsivVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALdpKSKQYYLIEVNPRVSRS 306
|
250 260 270
....*....|....*....|....*....|....*...
gi 15600629 295 HTITEEITGIDVVREQIRIASGLELSVKQDDIVHRGYA 332
Cdd:PRK12815 307 SALASKATGYPIAKIAAKLAVGYTLNELKNPVTGLTYA 344
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
20-291 |
1.81e-06 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 49.77 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 20 ACAEMGIRsVAVYSEADrhalhvkrADEAHSIGADPL-AGYLNPRALVNLAveSGCDALhpGYGFlsEN--AELAEICAE 96
Cdd:PRK06019 20 AAAPLGYK-VIVLDPDP--------DSPAAQVADEVIvADYDDVAALRELA--EQCDVI--TYEF--ENvpAEALDALAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 97 RGIKFigPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEgnVADLAEALREAERIGYPVMLKAtsggggrgirrC------ 170
Cdd:PRK06019 85 RVPVP--PGPDALAIAQDRLTEKQFLDKLGIPVAPFAV--VDSAEDLEAALADLGLPAVLKT-----------Rrggydg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 171 ------NSREELEQAFprviseatKAFGSAEVFLEKcIVNPKHiEAQILA--DSFGNTVH--LFErdcSIQrRNQKLIE- 239
Cdd:PRK06019 150 kgqwviRSAEDLEAAW--------ALLGSVPCILEE-FVPFER-EVSVIVarGRDGEVVFypLVE---NVH-RNGILRTs 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15600629 240 IAPsPQLTPEQRAYIGDLAVRAAKAVGYenAGT--VE-FLLADGEVYFMEMNTRV 291
Cdd:PRK06019 216 IAP-ARISAELQAQAEEIASRIAEELDY--VGVlaVEfFVTGDGELLVNEIAPRP 267
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
124-291 |
2.61e-06 |
|
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: 47.63 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 124 AAGVPcTPGTEGnVADLAEALREAERIGYPVMLKA-TSGGGGRGIRRCNSREELEQAFprviseatKAFGSAEVFLEKCI 202
Cdd:pfam02222 2 KLGLP-TPRFMA-AESLEELIEAGQELGYPCVVKArRGGYDGKGQYVVRSEADLPQAW--------EELGDGPVIVEEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 203 vnPKHIEAQILADSFGN-TVHLFERDCSIQRRNQKLIEIAPSPqLTPEQRAYIGDLAVRAAKAVGYENAGTVE-FLLADG 280
Cdd:pfam02222 72 --PFDRELSVLVVRSVDgETAFYPVVETIQEDGICRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDG 148
|
170
....*....|.
gi 15600629 281 EVYFMEMNTRV 291
Cdd:pfam02222 149 DLLINELAPRP 159
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
146-289 |
4.23e-06 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 47.31 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 146 EAERIGYPVMLKATSGGGGRGIRRCNSREELEQAfprvISEATKAfgSAEVFLEKCIvNPKHIEAQILADSFGNTVHLFE 225
Cdd:pfam07478 31 VEEALGYPVFVKPARLGSSVGVSKVESREELQAA----IEEAFQY--DEKVLVEEGI-EGREIECAVLGNEDPEVSPVGE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600629 226 R--DCSIQRRNQKLIE-----IAPSPqLTPEQRAYIGDLAVRAAKAVGYENAGTVE-FLLADGEVYFMEMNT 289
Cdd:pfam07478 104 IvpSGGFYDYEAKYIDdsaqiVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVDfFLTEDGEIVLNEVNT 174
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
98-312 |
6.80e-06 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 47.73 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 98 GIKFIGPSaQVIRRMGDKTEARRSMIAAGVPcTPGTeGNVADLAEALREAERIGYPVMLKATSGGGGRGIRRCNSREELE 177
Cdd:TIGR00768 73 GVPVINSS-DAILNAGDKFLSHQLLAKAGIP-LPRT-GLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 178 QafprvISEATKAF-GSAEVFL-EKCIVNPKH--IEAQILADSFGNTVHlfeRDCSIQRRNQKLIEIAPSP-QLTPEQRa 252
Cdd:TIGR00768 150 S-----LLEHFEQLnGPQNLFLvQEYIKKPGGrdIRVFVVGDEVVAAIY---RITSGHWRSNLARGGKAEPcSLTEEIE- 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 253 yigDLAVRAAKAVGYENAGtVEFLLADGEVYFMEMNTRVQVEHtiTEEITGIDVVREQIR 312
Cdd:TIGR00768 221 ---ELAIKAAKALGLDVAG-VDLLESEDGLLVNEVNANPEFKN--SVKTTGVNIAGKLLD 274
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-309 |
7.26e-06 |
|
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: 47.63 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 16 RIVRACAEMGIRsvAVYSEADRHALHVKRADEAHSigADPLAGYlnpRALVNlavesGCDALHPGYGFLsenaELAEica 95
Cdd:COG0189 18 ALIEAAQRRGHE--VEVIDPDDLTLDLGRAPELYR--GEDLSEF---DAVLP-----RIDPPFYGLALL----RQLE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 96 ERGIKFIgPSAQVIRRMGDKTEARRSMIAAGVPcTPGTEGnVADLAEALREAERIGYPVMLKATSGGGGRGIRRCNSREE 175
Cdd:COG0189 79 AAGVPVV-NDPEAIRRARDKLFTLQLLARAGIP-VPPTLV-TRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 176 LEQAFprvisEATKAFGSAEVFLEKCIVNPKHIEAQILA-DsfGNTVHLFER-----DCsiqRRNQKLIEIAPSPQLTPE 249
Cdd:COG0189 156 LESIL-----EALTELGSEPVLVQEFIPEEDGRDIRVLVvG--GEPVAAIRRipaegEF---RTNLARGGRAEPVELTDE 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 250 QRayigDLAVRAAKAVGYENAGtVEFLLADGEVYFMEMNTRVQVEHtiTEEITGIDVVRE 309
Cdd:COG0189 226 ER----ELALRAAPALGLDFAG-VDLIEDDDGPLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
90-290 |
4.29e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 46.24 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 90 LAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGteGNVADLAEALREAERIGYPVML--------KATSg 161
Cdd:PRK05294 645 LAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVrpsyvlggRAME- 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 162 gggrgirRCNSREELEqafpRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADsfGNTV-------HLfER------D- 227
Cdd:PRK05294 722 -------IVYDEEELE----RYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVliggimeHI-EEagvhsgDs 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600629 228 -CSIqrrnqklieiaPSPQLTPEQ----RAYIGDLAvRAAKAVGYENagtVEFLLADGEVYFMEMNTR 290
Cdd:PRK05294 788 aCSL-----------PPQTLSEEIieeiREYTKKLA-LELNVVGLMN---VQFAVKDDEVYVIEVNPR 840
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
75-316 |
1.09e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 44.84 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 75 DALHpgyGFLSENAELAEIcAERGIKFIGPSAQVIRRMG-------------DKTEARRSMIAAGVPcTPGTE--GNVAD 139
Cdd:PRK02186 59 DRIH---RFVSSLDGVAGI-MSSSEYFIEVASEVARRLGlpaanteairtcrDKKRLARTLRDHGID-VPRTHalALRAV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 140 LAEALREAeriGYPVMLKATSGGGGRGIRRCNSREELEQAFPRVISEATKAfgsaevFLEKCIVNPKHIEAQILADSFGN 219
Cdd:PRK02186 134 ALDALDGL---TYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRA------ALVQAYVEGDEYSVETLTVARGH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 220 TV------HLFERDCsiqrrnqkLIEIA---PSPQLTPeQRAYIGDLAVRAAKAVGYE-NAGTVEFLLADGEVYFMEMNT 289
Cdd:PRK02186 205 QVlgitrkHLGPPPH--------FVEIGhdfPAPLSAP-QRERIVRTVLRALDAVGYAfGPAHTELRVRGDTVVIIEINP 275
|
250 260
....*....|....*....|....*....
gi 15600629 290 RVQ--VEHTITEEITGIDVVREQIRIASG 316
Cdd:PRK02186 276 RLAggMIPVLLEEAFGVDLLDHVIDLHLG 304
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
76-289 |
2.22e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 43.13 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 76 ALHpgyGFLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPcTPGTEGnvadLAEALREAERIGYPVM 155
Cdd:PRK14569 63 ALH---GEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMP-TPMAKF----LTDKLVAEDEISFPVA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 156 LKATSGGGGRGIRRCNSREELEQAFprviSEATKafgSAEVFLEKCIVNpKHIEAQILADSFGNTVHLFERDCSIQRRNQ 235
Cdd:PRK14569 135 VKPSSGGSSIATFKVKSIQELKHAY----EEASK---YGEVMIEQWVTG-KEITVAIVNDEVYSSVWIEPQNEFYDYESK 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600629 236 ---KLIEIAPSpQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLAD-GEVYFMEMNT 289
Cdd:PRK14569 207 ysgKSIYHSPS-GLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDrGNFYIMEINS 263
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
146-289 |
3.30e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 42.50 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 146 EAERIGYPVMLKATSGGGGRGIRRCNSREELEQAfprvISEATKAFGSAEVflekcivnPKHIEAQILADSFGNTVHLFE 225
Cdd:PRK14571 120 KTSPLGYPCVVKPRREGSSIGVFICESDEEFQHA----LKEDLPRYGSVIV--------QEYIPGREMTVSILETEKGFE 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600629 226 RDCSIQRRNQKLIE-------------IAPSPqLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLADGEVYFMEMNT 289
Cdd:PRK14571 188 VLPILELRPKRRFYdyvakytkgetefILPAP-LNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEINT 263
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
104-290 |
3.62e-04 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 43.12 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 104 PSAQVIRRMGDKTEARRSMIAAGVPCTPGTEgnVADLAEALREAERIGYPVMLKATSGGGG-RGIRRCNSREELeqafpr 182
Cdd:PLN02948 111 PKSSTIRIIQDKYAQKVHFSKHGIPLPEFME--IDDLESAEKAGDLFGYPLMLKSRRLAYDgRGNAVAKTEEDL------ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 183 viSEATKAFGSAE--VFLEKCIvnPKHIE-AQILADSFGNTVHLFERDCSIQRRNQKLIEIAPSpQLTPEQRAYIGDLav 259
Cdd:PLN02948 183 --SSAVAALGGFErgLYAEKWA--PFVKElAVMVARSRDGSTRCYPVVETIHKDNICHVVEAPA-NVPWKVAKLATDV-- 255
|
170 180 190
....*....|....*....|....*....|....*
gi 15600629 260 rAAKAVG-YENAGT--VE-FLLADGEVYFMEMNTR 290
Cdd:PLN02948 256 -AEKAVGsLEGAGVfgVElFLLKDGQILLNEVAPR 289
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
83-151 |
1.09e-03 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 41.26 E-value: 1.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600629 83 FLSENAELAEICAERGIKFIGPSAQVIRRMGDKTEARRSMIAAGVPCTPGTEGNVADLAEALREAERIG 151
Cdd:PRK06524 111 FVMFDEETEALARQAGLEVMHPPAELRHRLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAG 179
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
114-202 |
2.01e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.52 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 114 DKTEARRSMIAAGVPCTPGTEgnVADLAEALREAERIGYPVMLK----------ATSGgggrgirrcNSREELEQAFprv 183
Cdd:PRK14016 214 DKELTKRLLAAAGVPVPEGRV--VTSAEDAWEAAEEIGYPVVVKpldgnhgrgvTVNI---------TTREEIEAAY--- 279
|
90
....*....|....*....
gi 15600629 184 isEATKAFGSaEVFLEKCI 202
Cdd:PRK14016 280 --AVASKESS-DVIVERYI 295
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
141-290 |
2.62e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 40.53 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 141 AEALREAERIGYPVMLKATSGGGGRGIRRCNSREELEqafpRVISEATKAFGSAEVFLEKCIVNPKHIEAQILADSFGNT 220
Cdd:PLN02735 727 ADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK----TYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNV 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 221 V-------------HLFERDCSIqrrnqklieiaPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEF-LLADGEVYFME 286
Cdd:PLN02735 803 ViggimehieqagvHSGDSACSL-----------PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIE 871
|
....
gi 15600629 287 MNTR 290
Cdd:PLN02735 872 ANPR 875
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
114-289 |
3.05e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 39.71 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 114 DKTEARRSMIAAGVPcTPgtEGNVADLAEALREA-ERIGYPVMLKATSGGGGRGIRRCNSREELEQAfprvISEATKaFG 192
Cdd:PRK01372 98 DKLRTKLVWQAAGLP-TP--PWIVLTREEDLLAAiDKLGLPLVVKPAREGSSVGVSKVKEEDELQAA----LELAFK-YD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 193 SaEVFLEK---------CIVNPK-----HIEAqilADSF---------GNTVHLFerdcsiqrrnqklieiaPSPqLTPE 249
Cdd:PRK01372 170 D-EVLVEKyikgreltvAVLGGKalpviEIVP---AGEFydyeakylaGGTQYIC-----------------PAG-LPAE 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600629 250 QRAYIGDLAVRAAKAVGYENAGTVEFLL-ADGEVYFMEMNT 289
Cdd:PRK01372 228 IEAELQELALKAYRALGCRGWGRVDFMLdEDGKPYLLEVNT 268
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
141-312 |
4.63e-03 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 38.25 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 141 AEALREAERIGYPVMLKATSGGGGRGIRRCNSREELEQafprvISEATKAFGSAEVFLE-------KCIVnpkhIEAQIL 213
Cdd:pfam08443 30 AEQFIEQIKRQFPVIVKSIYGSQGIGVFLAEDEQKLRQ-----TLSATNEQILVQEFIAeannediRCLV----VGDQVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600629 214 AdsfgnTVHLFERDCSIqRRNQKLIEIAPSPQLTPEQRayigDLAVRAAKAVGYENAGtVEFLLADGEVYFMEMNTRVQV 293
Cdd:pfam08443 101 G-----ALHRQSNEGDF-RSNLHRGGVGEKYQLSQEET----ELAIKAAQAMQLDVAG-VDLLRQKRGLLVCEVNSSPGL 169
|
170
....*....|....*....
gi 15600629 294 EhtITEEITGIDVVREQIR 312
Cdd:pfam08443 170 E--GIEKTLGINIAIKIIA 186
|
|
| |
