|
Name |
Accession |
Description |
Interval |
E-value |
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
39-499 |
0e+00 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 732.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 39 ERIDNKRHAALLGGGQRRIDAQHKR-----------------------------------FPGDSVVTGRGRINGRLVYV 83
Cdd:COG4799 7 AELRARREEALLGGGEKAIERQHARgkltareridllldpgsflelgalaghrmyddddrVPGDGVVTGIGTVDGRPVVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 84 FSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCA 163
Cdd:COG4799 87 VANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQISVIMGPCA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 164 GGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFLPLS 243
Cdd:COG4799 167 AGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPSN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 244 SQDPAPIRECHDPsDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQPNV 323
Cdd:COG4799 247 NLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQPMV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 324 ASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDV 403
Cdd:COG4799 326 LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 404 MSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFK----GHQDVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTRAR 476
Cdd:COG4799 406 MCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRrelaAAEDPEALRAELIAEYeeqANPYYAAARGWIDDVIDPRDTRRV 485
|
490 500
....*....|....*....|...
gi 568961907 477 ICCDLEVLASKKVHRPWRKHANI 499
Cdd:COG4799 486 LARALEAAANKPEERPPKKHGVI 508
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
62-499 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 655.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 62 KRFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADI 141
Cdd:pfam01039 40 KRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 142 FLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHR 221
Cdd:pfam01039 120 FGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIMVEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 222 AFDNDVDALCNLREFFNFLPL---SSQDPAPIRECHDPSDRLVPeLDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSY 298
Cdd:pfam01039 200 TALDDEDALELIRKWLSYLPKpapNNREPVPIVPTKDPPDRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 299 AKNIVVGFARMNGRTVGIVGNQPNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLL 378
Cdd:pfam01039 279 AKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 379 YAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIF--------KGHQDVEAA----QA 446
Cdd:pfam01039 359 YALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAWPTARIAVMGPEGAVEIKFrkekaaaeMRGKDLAATrkqkIA 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568961907 447 EYVEKFANPFPAAVRGFVDDIIQPSSTRARICCDLEVLASKKVHRPWRKHANI 499
Cdd:pfam01039 439 EYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPRFFPWRKHGNI 491
|
|
| mmdA |
TIGR01117 |
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA ... |
39-501 |
0e+00 |
|
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA decarboxylase aplha subunit in archaea and bacteria. Metylmalonyl-CoA decarboxylase Na+ pump is a representative of a class of Na+ transport decarboxylases that couples the energy derived by decarboxylation of carboxylic acid substrates to drive the extrusion of Na+ ion across the membrane. [Energy metabolism, ATP-proton motive force interconversion, Energy metabolism, Fermentation, Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130187 Cd Length: 512 Bit Score: 624.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 39 ERIDNKRHAALLGGGQRRIDAQH--------------------------------------KRFPGDSVVTGRGRINGRL 80
Cdd:TIGR01117 4 EELHEKKEKIKQGGGEKRIEKQHaqgkmtarerlallfdpgsfveidqfvkhrctnfgmdkKELPAEGVVTGYGTIDGRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 81 VYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMG 160
Cdd:TIGR01117 84 VYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKGYGDIFYRNTIASGVVPQISAIMG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 161 PCAGGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFL 240
Cdd:TIGR01117 164 PCAGGAVYSPALTDFIYMVDNTSQMFITGPQVIKTVTGEEVTAEQLGGAMAHNSVSGVAHFIAEDDDDCIMLIRRLLSFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 241 PLSSQDPAPIRECHDPSDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQ 320
Cdd:TIGR01117 244 PSNNMEKAPLVKTGDDPTRETPELYDLLPDNPNKPYDMRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGIIANQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 321 PNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGA 400
Cdd:TIGR01117 324 PKVMAGCLDIDSSDKIARFIRFCDAFNIPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAYGGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 401 YDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFKghQDVEAAQ----------AEYVEKFANPFPAAVRGFVDDIIQP 470
Cdd:TIGR01117 404 YLAMCSKHLGADQVYAWPTAEIAVMGPAGAANIIFR--KDIKEAKdpaatrkqkiAEYREEFANPYKAAARGYVDDVIEP 481
|
490 500 510
....*....|....*....|....*....|.
gi 568961907 471 SSTRARICCDLEVLASKKVHRPWRKHANIPL 501
Cdd:TIGR01117 482 KQTRPKIVNALAMLESKREKLPPKKHGNIPL 512
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
65-474 |
1.12e-71 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 238.17 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 65 PGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAG---YADI 141
Cdd:PLN02820 115 PSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDrdhFGRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 142 FLRNVTASGV-IPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAH 220
Cdd:PLN02820 195 FYNQARMSSAgIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 221 RAFDNDVDALCNLREFFNFLPLSSQDP------APIRECHDPsdrLVP--ELDTVVPLESSKAYNMLDIIHAVIDEREFF 292
Cdd:PLN02820 275 HFAQDELHALAIGRNIVKNLHLAAKQGmentlgSKNPEYKEP---LYDvkELRGIVPADHKQSFDVRSVIARIVDGSEFD 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 293 EIMPSYAKNIVVGFARMNGRTVGIVGNqpnvaSGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIR 372
Cdd:PLN02820 352 EFKKNYGTTLVTGFARIYGQPVGIIGN-----NGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 373 HGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIF---------KGHQ---- 439
Cdd:PLN02820 427 AGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAqierenkkrQGIQwske 506
|
410 420 430
....*....|....*....|....*....|....*...
gi 568961907 440 DVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTR 474
Cdd:PLN02820 507 EEEAFKAKTVEAYereANPYYSTARLWDDGVIDPADTR 544
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
39-499 |
0e+00 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 732.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 39 ERIDNKRHAALLGGGQRRIDAQHKR-----------------------------------FPGDSVVTGRGRINGRLVYV 83
Cdd:COG4799 7 AELRARREEALLGGGEKAIERQHARgkltareridllldpgsflelgalaghrmyddddrVPGDGVVTGIGTVDGRPVVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 84 FSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCA 163
Cdd:COG4799 87 VANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQISVIMGPCA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 164 GGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFLPLS 243
Cdd:COG4799 167 AGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPSN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 244 SQDPAPIRECHDPsDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQPNV 323
Cdd:COG4799 247 NLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQPMV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 324 ASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDV 403
Cdd:COG4799 326 LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 404 MSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFK----GHQDVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTRAR 476
Cdd:COG4799 406 MCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRrelaAAEDPEALRAELIAEYeeqANPYYAAARGWIDDVIDPRDTRRV 485
|
490 500
....*....|....*....|...
gi 568961907 477 ICCDLEVLASKKVHRPWRKHANI 499
Cdd:COG4799 486 LARALEAAANKPEERPPKKHGVI 508
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
62-499 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 655.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 62 KRFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADI 141
Cdd:pfam01039 40 KRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 142 FLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHR 221
Cdd:pfam01039 120 FGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIMVEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 222 AFDNDVDALCNLREFFNFLPL---SSQDPAPIRECHDPSDRLVPeLDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSY 298
Cdd:pfam01039 200 TALDDEDALELIRKWLSYLPKpapNNREPVPIVPTKDPPDRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 299 AKNIVVGFARMNGRTVGIVGNQPNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLL 378
Cdd:pfam01039 279 AKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 379 YAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIF--------KGHQDVEAA----QA 446
Cdd:pfam01039 359 YALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAWPTARIAVMGPEGAVEIKFrkekaaaeMRGKDLAATrkqkIA 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568961907 447 EYVEKFANPFPAAVRGFVDDIIQPSSTRARICCDLEVLASKKVHRPWRKHANI 499
Cdd:pfam01039 439 EYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPRFFPWRKHGNI 491
|
|
| mmdA |
TIGR01117 |
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA ... |
39-501 |
0e+00 |
|
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA decarboxylase aplha subunit in archaea and bacteria. Metylmalonyl-CoA decarboxylase Na+ pump is a representative of a class of Na+ transport decarboxylases that couples the energy derived by decarboxylation of carboxylic acid substrates to drive the extrusion of Na+ ion across the membrane. [Energy metabolism, ATP-proton motive force interconversion, Energy metabolism, Fermentation, Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130187 Cd Length: 512 Bit Score: 624.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 39 ERIDNKRHAALLGGGQRRIDAQH--------------------------------------KRFPGDSVVTGRGRINGRL 80
Cdd:TIGR01117 4 EELHEKKEKIKQGGGEKRIEKQHaqgkmtarerlallfdpgsfveidqfvkhrctnfgmdkKELPAEGVVTGYGTIDGRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 81 VYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMG 160
Cdd:TIGR01117 84 VYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKGYGDIFYRNTIASGVVPQISAIMG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 161 PCAGGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFL 240
Cdd:TIGR01117 164 PCAGGAVYSPALTDFIYMVDNTSQMFITGPQVIKTVTGEEVTAEQLGGAMAHNSVSGVAHFIAEDDDDCIMLIRRLLSFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 241 PLSSQDPAPIRECHDPSDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQ 320
Cdd:TIGR01117 244 PSNNMEKAPLVKTGDDPTRETPELYDLLPDNPNKPYDMRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGIIANQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 321 PNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGA 400
Cdd:TIGR01117 324 PKVMAGCLDIDSSDKIARFIRFCDAFNIPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAYGGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 401 YDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFKghQDVEAAQ----------AEYVEKFANPFPAAVRGFVDDIIQP 470
Cdd:TIGR01117 404 YLAMCSKHLGADQVYAWPTAEIAVMGPAGAANIIFR--KDIKEAKdpaatrkqkiAEYREEFANPYKAAARGYVDDVIEP 481
|
490 500 510
....*....|....*....|....*....|.
gi 568961907 471 SSTRARICCDLEVLASKKVHRPWRKHANIPL 501
Cdd:TIGR01117 482 KQTRPKIVNALAMLESKREKLPPKKHGNIPL 512
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
65-474 |
1.12e-71 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 238.17 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 65 PGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAG---YADI 141
Cdd:PLN02820 115 PSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDrdhFGRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 142 FLRNVTASGV-IPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAH 220
Cdd:PLN02820 195 FYNQARMSSAgIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 221 RAFDNDVDALCNLREFFNFLPLSSQDP------APIRECHDPsdrLVP--ELDTVVPLESSKAYNMLDIIHAVIDEREFF 292
Cdd:PLN02820 275 HFAQDELHALAIGRNIVKNLHLAAKQGmentlgSKNPEYKEP---LYDvkELRGIVPADHKQSFDVRSVIARIVDGSEFD 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 293 EIMPSYAKNIVVGFARMNGRTVGIVGNqpnvaSGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIR 372
Cdd:PLN02820 352 EFKKNYGTTLVTGFARIYGQPVGIIGN-----NGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 373 HGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIF---------KGHQ---- 439
Cdd:PLN02820 427 AGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAqierenkkrQGIQwske 506
|
410 420 430
....*....|....*....|....*....|....*...
gi 568961907 440 DVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTR 474
Cdd:PLN02820 507 EEEAFKAKTVEAYereANPYYSTARLWDDGVIDPADTR 544
|
|
| AccD |
COG0777 |
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
67-135 |
8.62e-13 |
|
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440540 [Multi-domain] Cd Length: 280 Bit Score: 68.55 E-value: 8.62e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961907 67 DSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESL 135
Cdd:COG0777 107 DAVVTGTGTINGIPVVVAVMDFSFMGGSMGSVVGEKITRAIERAIEKKLPLIIFSASGGARMQEGILSL 175
|
|
| PRK07189 |
PRK07189 |
malonate decarboxylase subunit beta; Reviewed |
67-193 |
2.57e-10 |
|
malonate decarboxylase subunit beta; Reviewed
Pssm-ID: 235954 Cd Length: 301 Bit Score: 61.46 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 67 DSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVG-----APVIGLNDSGGARIQEGVESLAGYADI 141
Cdd:PRK07189 56 DGVVVGKGTLDGRPVVVAAQEGRFMGGSVGEVHGAKLAGALELAAEDNrngipTAVLLLFETGGVRLQEANAGLAAIAEI 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568961907 142 FLRNVTASGVIPQISLIMGP--CAGGAVYSPALTDfTFMVKDTSYLFITGPEVV 193
Cdd:PRK07189 136 MRAIVDLRAAVPVIGLIGGRvgCFGGMGIAAALCS-YLIVSEEGRLGLSGPEVI 188
|
|
| PRK05724 |
PRK05724 |
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated |
279-400 |
1.32e-08 |
|
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
Pssm-ID: 235580 [Multi-domain] Cd Length: 319 Bit Score: 56.30 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 279 LDIIHAVIDEreFFEIM--PSYA--KNIVVGFARMNGRTVGIVGNQpnvaSGClDINSSV-------------KGARFVR 341
Cdd:PRK05724 73 LDYIELLFTD--FTELHgdRAFAddKAIVGGLARLNGRPVMVIGHQ----KGR-DTKEKIrrnfgmprpegyrKALRLMK 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961907 342 FCDAFNIPLITFVDVPGFLPG-TAQEYG---GIirhgAKLLYAFAEATVPKI-TVITRKAYGGA 400
Cdd:PRK05724 146 MAEKFGLPIITFIDTPGAYPGiGAEERGqseAI----ARNLREMARLKVPIIcTVIGEGGSGGA 205
|
|
| accD |
CHL00174 |
acetyl-CoA carboxylase beta subunit; Reviewed |
67-141 |
2.60e-07 |
|
acetyl-CoA carboxylase beta subunit; Reviewed
Pssm-ID: 214384 [Multi-domain] Cd Length: 296 Bit Score: 52.21 E-value: 2.60e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961907 67 DSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADI 141
Cdd:CHL00174 121 DAVQTGIGQLNGIPVALGVMDFQFMGGSMGSVVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQMAKI 195
|
|
| AccA |
COG0825 |
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
279-393 |
9.62e-07 |
|
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440587 [Multi-domain] Cd Length: 315 Bit Score: 50.42 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 279 LDIIHAVIDEreFFEIM--PSYA--KNIVVGFARMNGRTVGIVGNQpnvasgcldinssvKGA----------------- 337
Cdd:COG0825 70 LDYIEAIFTD--FIELHgdRAFGddPAIVGGLARFDGRPVMVIGHQ--------------KGRdtkerikrnfgmphpeg 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961907 338 -----RFVRFCDAFNIPLITFVDVPGFLPG-TAQEYG---GIirhgAKLLYAFAEATVPKITVIT 393
Cdd:COG0825 134 yrkalRLMKLAEKFGLPIITFIDTPGAYPGiGAEERGqseAI----ARNLREMARLKVPIISVVI 194
|
|
| PLN03230 |
PLN03230 |
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional |
302-400 |
3.74e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
Pssm-ID: 178769 [Multi-domain] Cd Length: 431 Bit Score: 43.01 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 302 IVVGFARMNGRTVGIVGNQPNVAS--------GCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPG-TAQEYGgiir 372
Cdd:PLN03230 168 IVCGIGSMEGMSFMFIGHQKGRNTkeniyrnfAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPGAYAGiKAEELG---- 243
|
90 100 110
....*....|....*....|....*....|..
gi 568961907 373 HGAKLLYAFAEA---TVPKI-TVITRKAYGGA 400
Cdd:PLN03230 244 QGEAIAFNLREMfglRVPIIaTVIGEGGSGGA 275
|
|
| accA |
CHL00198 |
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional |
302-400 |
5.41e-04 |
|
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
Pssm-ID: 214393 [Multi-domain] Cd Length: 322 Bit Score: 42.11 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 302 IVVGFARMNGRTVGIVGNQ------PNVAS--GCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRH 373
Cdd:CHL00198 101 LVGGIGKINGRTIVFLGHQrgrntkENVLRnfGMPSPGGYRKALRLMKHANKFGLPILTFIDTPGAWAGVKAEKLGQGEA 180
|
90 100
....*....|....*....|....*...
gi 568961907 374 GAKLLYAFAEATVPKI-TVITRKAYGGA 400
Cdd:CHL00198 181 IAVNLREMFSFEVPIIcTIIGEGGSGGA 208
|
|
| PRK12319 |
PRK12319 |
acetyl-CoA carboxylase subunit alpha; Provisional |
302-445 |
6.94e-03 |
|
acetyl-CoA carboxylase subunit alpha; Provisional
Pssm-ID: 183435 [Multi-domain] Cd Length: 256 Bit Score: 38.22 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961907 302 IVVGFARMNGRTVGIVGNQP------NVAS--GCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRH 373
Cdd:PRK12319 45 VVGGIGYLAGQPVTVVGIQKgknlqdNLKRnfGQPHPEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961907 374 GAKLLYAFAEATVPKITVITRKAYGG---AYDVMSSKHLLGDTNYawptaeiAVMGAKGAVEIIFK-GHQDVEAAQ 445
Cdd:PRK12319 125 IARNLMEMSDLKVPIIAIIIGEGGSGgalALAVADQVWMLENTMY-------AVLSPEGFASILWKdGSRATEAAE 193
|
|
|