|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
1-316 |
0e+00 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 580.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 1 MYSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVAT 80
Cdd:PRK09352 2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 81 TSSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDA 160
Cdd:PRK09352 82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 161 AGAVVVGASEEPGILSTHIYSDGKYGELLSLEV-PERGGDADKWLHMAGNEVFKVAVTQLSKLVKDTLAANNMDKSELDW 239
Cdd:PRK09352 162 AGAVVLGASEEPGILSTHLGSDGSYGDLLYLPGgGSRGPASPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDIDW 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498123120 240 LVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTWGSALVKF 316
Cdd:PRK09352 242 LVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRW 318
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
1-316 |
2.96e-176 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 489.97 E-value: 2.96e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 1 MYSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVAT 80
Cdd:TIGR00747 1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 81 TSSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDA 160
Cdd:TIGR00747 81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 161 AGAVVVGASEEPG-ILSTHIYSDGKYGELLSLEVPERGGDADK-WLHMAGNEVFKVAVTQLSKLVKDTLAANNMDKSELD 238
Cdd:TIGR00747 161 AGAVVLGESEDPGgIISTHLGADGTQGEALYLPAGGRPTSGPSpFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDID 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498123120 239 WLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTWGSALVKF 316
Cdd:TIGR00747 241 WFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
1-316 |
5.27e-175 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 486.92 E-value: 5.27e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 1 MYSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVAT 80
Cdd:COG0332 1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 81 TSSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDA 160
Cdd:COG0332 81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 161 AGAVVVGASEE-PGILSTHIYSDGKYGELL------SLEVPERGGDADKWLHMAGNEVFKVAVTQLSKLVKDTLAANNMD 233
Cdd:COG0332 161 AGAVVLEASEEgPGILGSVLGSDGSGADLLvvpaggSRNPPSPVDEGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 234 KSELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTWGSAL 313
Cdd:COG0332 241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320
|
...
gi 498123120 314 VKF 316
Cdd:COG0332 321 LRW 323
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
2-314 |
8.41e-161 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 450.84 E-value: 8.41e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 2 YSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVATT 81
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 82 SSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDAA 161
Cdd:cd00830 81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 162 GAVVVGASEE-PGILSTHIYSDGKYGELL------SLEVPERGGDADKWLHMAGNEVFKVAVTQLSKLVKDTLAANNMDK 234
Cdd:cd00830 161 GAVVLEATEEdPGILDSVLGSDGSGADLLtipaggSRSPFEDAEGGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 235 SELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTWGSALV 314
Cdd:cd00830 241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-315 |
2.22e-148 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 419.65 E-value: 2.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 1 MYSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVAT 80
Cdd:PRK12879 3 SYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 81 TSSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDA 160
Cdd:PRK12879 83 TTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 161 AGAVVVGASE-EPGILSTHIYSDGKYGELLSLEVP----ERGGDADKW-LHMAGNEVFKVAVTQLSKLVKDTLAANNMDK 234
Cdd:PRK12879 163 AGAVVLEATEnEPGFIDYVLGTDGDGGDILYRTGLgttmDRDALSGDGyIVQNGREVFKWAVRTMPKGARQVLEKAGLTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 235 SELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTWGSALV 314
Cdd:PRK12879 243 DDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLV 322
|
.
gi 498123120 315 K 315
Cdd:PRK12879 323 K 323
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
3-316 |
3.02e-114 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 335.17 E-value: 3.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 3 SKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVATTS 82
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 83 SSHTFpSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDAAG 162
Cdd:PLN02326 128 PDDLF-GSAPQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDGAG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 163 AVVVGASEEP--GILSTHIYSDGK---------YGELLSLEVPERGGDADK--------WLHMAGNEVFKVAVTQLSKLV 223
Cdd:PLN02326 207 AVVLQACDDDedGLLGFDMHSDGNghkhlhatfKGEDDDSSGGNTNGVGDFppkkasysCIQMNGKEVFKFAVRCVPQVI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 224 KDTLAANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAF 303
Cdd:PLN02326 287 ESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATAGF 366
|
330
....*....|...
gi 498123120 304 GGGFTWGSALVKF 316
Cdd:PLN02326 367 GAGLTWGSAIVRW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
1-316 |
1.96e-95 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 285.30 E-value: 1.96e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 1 MYSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVAT 80
Cdd:CHL00203 1 MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 81 TSSSHTFpSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDA 160
Cdd:CHL00203 81 STPDDLF-GSASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 161 AGAVVVGASEEPGILSTHIYSDGKYGELLSL-------------EVPErgGDADkWLHMAGNEVFKVAVTQLSKLVKDTL 227
Cdd:CHL00203 160 AGAAIIGASYENSILGFKLCTDGKLNSHLQLmnkpvnnqsfgttKLPQ--GQYQ-SISMNGKEVYKFAVFQVPAVIIKCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 228 AANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGF 307
Cdd:CHL00203 237 NALNISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGL 316
|
....*....
gi 498123120 308 TWGSALVKF 316
Cdd:CHL00203 317 TWGAIVLKW 325
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
3-316 |
2.31e-83 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 254.65 E-value: 2.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 3 SKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVATTS 82
Cdd:PRK05963 4 SRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 83 SSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTgMCKNVLVIGADALSKTCDPTDRSTIILFGDAAG 162
Cdd:PRK05963 84 PDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRA-QGKPVLVVAANILSRRINMAERASAVLFADAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 163 AVVVGASEEP--GILSTHIYSDGKYGELLSleVPERG---------GDADKWLHMA-GNEVFKVAVTQLSKLVKDTLAAN 230
Cdd:PRK05963 163 AVVLAPSAKAnsGVLGSQLISDGSHYDLIK--IPAGGsarpfaperDASEFLMTMQdGRAVFTEAVRMMSGASQNVLASA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 231 NMDKSELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTWG 310
Cdd:PRK05963 241 AMTPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGG 320
|
....*.
gi 498123120 311 SALVKF 316
Cdd:PRK05963 321 AVVMRV 326
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-314 |
6.21e-70 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 220.00 E-value: 6.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 5 ILGTGSYLPSQVRTNADLEKMVetSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVATTSSS 84
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 85 HTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIIlFGDAAGAV 164
Cdd:cd00827 82 DKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALEPT-LGDGAAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 165 VVGASEEP---GILSTHIYSDGKYG----ELLSLEVPERGGDADKW---LHMAGNEVFKVAVTQLSKLVKDTLAANNMDk 234
Cdd:cd00827 161 LVSRNPGIlaaGIVSTHSTSDPGYDfspyPVMDGGYPKPCKLAYAIrltAEPAGRAVFEAAHKLIAKVVRKALDRAGLS- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 235 SELDWLVPHQAN-YRIISATAKKLTMSLDQVVIT----LDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTW 309
Cdd:cd00827 240 EDIDYFVPHQPNgKKILEAVAKKLGGPPEKASQTrwilLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTA 319
|
....*
gi 498123120 310 GSALV 314
Cdd:cd00827 320 EAFVL 324
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
2-316 |
3.05e-61 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 198.14 E-value: 3.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 2 YSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRIsAENETVADMAFYAAENAIEMAGIDKEDIDLIIVATT 81
Cdd:PRK07204 4 YISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHF-VDGETSSYMGAEAAKKAVEDAKLTLDDIDCIICASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 82 SSSHTFPSSACQVQGKLGIK--GCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGD 159
Cdd:PRK07204 83 TIQQAIPCTASLIQEQLGLQhsGIPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 160 AAGAVVVGASEEPG-ILSTHI--YSDGKY-------GELLSLEVPERGGDADKWLHMAGNEVFKVAVTQLSKLVKDTLAA 229
Cdd:PRK07204 163 GAAAVVITKGDHSSrILASHMetYSSGAHlseirggGTMIHPREYSEERKEDFLFDMNGRAIFKLSSKYLMKFIDKLLMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 230 NNMDKSELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTW 309
Cdd:PRK07204 243 AGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSI 322
|
....*..
gi 498123120 310 GSALVKF 316
Cdd:PRK07204 323 GGILLEY 329
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
50-314 |
5.78e-48 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 161.46 E-value: 5.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 50 TVADMAFYAAENAIEMAGIDKEDIDLIIVATTSSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTG 129
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 130 MCKNVLVIGADalsktcdptdrstIILFGDAAGAVVVGASEE---------PGILSTHIYSDGKYGEllslevperggda 200
Cdd:cd00327 86 KADIVLAGGSE-------------EFVFGDGAAAAVVESEEHalrrgahpqAEIVSTAATFDGASMV------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 201 dkwlhmagnevFKVAVTQLSKLVKDTLAANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQ-----VVITLDKHGNTS 275
Cdd:cd00327 140 -----------PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGvrspaVSATLIMTGHPL 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 498123120 276 AATVPTALDEAVRDGRIK-------RGQTLLLEAFGGGFTWGSALV 314
Cdd:cd00327 209 GAAGLAILDELLLMLEHEfipptprEPRTVLLLGFGLGGTNAAVVL 254
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
54-314 |
5.46e-47 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 161.26 E-value: 5.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 54 MAFYAAENAIEMAGIDKED----IDLIIVATTSSSH---------------------TFPSSACQVQGKLGIKGcPAFDL 108
Cdd:cd00825 14 LGFEAAERAIADAGLSREYqknpIVGVVVGTGGGSPrfqvfgadamravgpyvvtkaMFPGASGQIATPLGIHG-PAYDV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 109 AAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDP------------------TDRSTIILFGDAAGAVVVGASE 170
Cdd:cd00825 93 SAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCefdamgalstpekasrtfDAAADGFVFGDGAGALVVEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 171 E---------PGILSTHIYSDGkygellslevperggdadkwlhmAGNEVFKVAVTQLSKLVKDTLAANNMDKSELDWLV 241
Cdd:cd00825 173 HalargahiyAEIVGTAATIDG-----------------------AGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 242 PHQANYRIISATAKKLTMSLDQ-----VVITLDKHGNTSAATVPTALDEAVRDGRIK----------------------- 293
Cdd:cd00825 230 AHGTGTPIGDVKELKLLRSEFGdkspaVSATKAMTGNLSSAAVVLAVDEAVLMLEHGfippsihieeldeaglnivtett 309
|
330 340
....*....|....*....|...
gi 498123120 294 --RGQTLLLEAFGGGFTWGSALV 314
Cdd:cd00825 310 prELRTALLNGFGLGGTNATLVL 332
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
3-316 |
1.13e-43 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 153.20 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 3 SKILGTGSYLPSQVRTNADLEKMVETSDEWIVAR----TGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIV 78
Cdd:PRK12880 8 AKISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 79 ATTSSSHTFPSSACQVQGKLGIK-GCPAFDLAAACSGFVYALSVADQHIKTGMCKnVLVIGADALSKTCDPTDRSTIILF 157
Cdd:PRK12880 88 VTQSPDFFMPSTACYLHQLLNLSsKTIAFDLGQACAGYLYGLFVAHSLIQSGLGK-ILLICGDTLSKFIHPKNMNLAPIF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 158 GDAAGAVVVGASEEPGILsTHIYSDGKYGEllSLEVPE---RGGDADKW----------------LHMAGNEVFKVAVTQ 218
Cdd:PRK12880 167 GDGVSATLIEKTDFNEAF-FELGSDGKYFD--KLIIPKgamRIPKADIFnddslmqteefrqlenLYMDGANIFNMALEC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 219 LSKLVKDTLAANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQVV-ITLDKHGNTSAATVPTALDEAVRDGRIKRgqt 297
Cdd:PRK12880 244 EPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPnFIMEKYANLSACSLPALLCELDTPKEFKA--- 320
|
330
....*....|....*....
gi 498123120 298 lLLEAFGGGFTWGSALVKF 316
Cdd:PRK12880 321 -SLSAFGAGLSWGSAVLNF 338
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
5-315 |
2.53e-43 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 152.34 E-value: 2.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 5 ILGTGSYLPSQVRTNADL------------------------EKMVETSDEWIVARTGIKER----------------RI 44
Cdd:PRK07515 5 ISGTGLYTPPESISNEELvasfnayverfnaenaaaiaagevEALQPSSSEFIEKASGIKSRyvmdkegildpdrmrpRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 45 SA----ENETVADMAFYAAENAIEMAGIDKEDIDLIIVATTSSSHTFPSSACQVQGKLGIKGCpAFDLAAACSGFVYALS 120
Cdd:PRK07515 85 PErsndELSIQAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIEGF-AFDMNVACSSATFGIQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 121 VADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDAAGAVVVGASEEPG------ILSTHI---YSDG---KYGEL 188
Cdd:PRK07515 164 TAANAIRSGSARRVLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATsaggfeILGTRLftqFSNNirnNFGFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 189 LSLEvPERGGDADKWLHMAGNEVFKVAVTQLSKLVKDTLAANNMDKSELD--WLvpHQANYRIISATAKKL---TMSLDQ 263
Cdd:PRK07515 244 NRAD-PEGIGARDKLFVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKrfWL--HQANINMNQLIGKKVlgrDATPEE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 498123120 264 VVITLDKHGNTSAATVPTALDEAVRDgrIKRGQTLLLEAFGGGFTWGSALVK 315
Cdd:PRK07515 321 APVILDEYANTSSAGSIIAFHKHSDD--LAAGDLGVICSFGAGYSIGSVIVR 370
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
227-316 |
5.03e-43 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 143.03 E-value: 5.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 227 LAANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGG 306
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 498123120 307 FTWGSALVKF 316
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
106-183 |
5.22e-37 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 127.25 E-value: 5.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 106 FDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILFGDAAGAVVVGASEEPG--ILSTHIYSDG 183
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPGarILDSVLGSDG 80
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
5-315 |
1.86e-31 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 120.11 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 5 ILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIvaTTSSS 84
Cdd:PRK06840 7 IVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVI--YIGSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 85 HT-FP--SSACQVQGKLGIKGCPAFDLAAACSGFVYALSVA-DQHIKTGMCKNVLVIGADALSKTCDPTDRSTIILF--G 158
Cdd:PRK06840 85 HKdYPvwSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAkDLLYSDPSIENVLLVGGYRNSDLVDYDNPRTRFMFnfA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 159 DAAGAVVVGasEEPG---ILSTHIYSDGKYGEllSLEVPERGGDADKWLHMAGNEVFKVAVTQLSKL------------- 222
Cdd:PRK06840 165 AGGSAALLK--KDAGknrILGSAIITDGSFSE--DVRVPAGGTKQPASPETVENRQHYLDVIDPESMkerldevsipnfl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 223 --VKDTLAANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQvVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLL 300
Cdd:PRK06840 241 kvIREALRKSGYTPKDIDYLAILHMKRSAHIALLEGLGLTEEQ-AIYLDEYGHLGQLDQILSLHLALEQGKLKDGDLVVL 319
|
330
....*....|....*
gi 498123120 301 EAFGGGFTWGSALVK 315
Cdd:PRK06840 320 VSAGTGYTWAATVIR 334
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
27-308 |
1.30e-25 |
|
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.
Pssm-ID: 238427 [Multi-domain] Cd Length: 361 Bit Score: 104.61 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 27 ETSDEWIVARTGIKERRISAENETVAdMAFYAAENAIEMAGIDKEDIDLIIVATTSSSHTfPSSACQVQGKLG----IKG 102
Cdd:cd00831 62 ETYAPRPEMSPSLDERNDIALEEARE-LAEEAARGALDEAGLRPSDIDHLVVNTSTGNPT-PSLDAMLINRLGlrpdVKR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 103 CPAFDLAaaCSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPTD-RSTII---LFGDAAGAVVVGASEEPG----- 173
Cdd:cd00831 140 YNLGGMG--CSAGAIALDLAKDLLEANPGARVLVVSTELCSLWYRGPDhRSMLVgnaLFGDGAAAVLLSNDPRDRrrerp 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 174 ---ILST--HIYSDGkyGELLSLEVPERGgdadkwLHMAGN-EVFKVAVTQLSKLVKDTLAANNMDKSELD---WLVpHQ 244
Cdd:cd00831 218 lfeLVRAasTLLPDS--EDAMGWHLGEEG------LTFVLSrDVPRLVEKNLERVLRKLLARLGIGLFKLAfdhWCV-HP 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498123120 245 ANYRIISATAKKLTMSLDQVVI---TLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFT 308
Cdd:cd00831 289 GGRAVLDAVEKALGLSPEDLEAsrmVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
3-316 |
5.80e-22 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 94.44 E-value: 5.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 3 SKILGTGSYLPSQVRTNADLEKMVETSDEW----------IVARTGIKERRIS------AENETVAD-MAFY-------- 57
Cdd:COG3424 2 ARILSIATAVPPHRYTQEEIAEFAAELFGLderdrrrlrrLFENSGIETRHSVlplewyLEPPSFGErNALYieealela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 58 --AAENAIEMAGIDKEDIDLIIVATTSSSHTfPSSACQVQGKLGIK-----------GCpafdlAAACSGfvyaLSVADQ 124
Cdd:COG3424 82 eeAARRALDKAGLDPEDIDHLVTVSCTGFAA-PGLDARLINRLGLRpdvrrlpvggmGC-----AAGAAG----LRRAAD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 125 HIKTGMCKNVLVIGADALSKTCDPTDRS--TII---LFGDAAGAVVVGASEEPGIL------STHIYSDGKygELLSLEV 193
Cdd:COG3424 152 FLRADPDAVVLVVCVELCSLTFQRDDDSkdNLVanaLFGDGAAAVVVSGDPRPGPGprilafRSYLIPDTE--DVMGWDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 194 PERGgdadkwLHMA-GNEVFKVAVTQLSKLVKDTLAANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQVVIT---LD 269
Cdd:COG3424 230 GDTG------FRMVlSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSrevLR 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 498123120 270 KHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTWGSALVKF 316
Cdd:COG3424 304 EYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
2-306 |
2.63e-21 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 92.25 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 2 YSK--ILGTGSYLPSQVRTNADLEKMVETSDE-------WIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKED 72
Cdd:PRK09258 3 YSNvaILSLAYELAPVVVTSSEIEERLAPLYErlrlppgQLEALTGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 73 IDLIIVATTSSSHTFPSSACQVQGKLGI-KGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALSKTCDPT-D 150
Cdd:PRK09258 83 IGLLINTSVCRDYLEPATACRVHHNLGLpKSCANFDVSNACLGFLNGMLDAANMIELGQIDYALVVSGESAREIVEATiD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 151 R---------------STIILFGDAAGAVVVGASEEPGilsTHIYSDGkygelLSLEVPE-----RGGDadkwLHMA--G 208
Cdd:PRK09258 163 RllapettredfaqsfATLTLGSGAAAAVLTRGSLHPR---GHRLLGG-----VTRAATEhhelcQGGR----DGMRtdA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 209 NEVFKVAVtqlsKLVKDT----LAANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQVVITLDKHGNTSAATVPTALD 284
Cdd:PRK09258 231 VGLLKEGV----ELAVDTweafLAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMGPASLPITLA 306
|
330 340
....*....|....*....|..
gi 498123120 285 EAVRDGRIKRGQTLLLEAFGGG 306
Cdd:PRK09258 307 MAAEEGFLKPGDRVALLGIGSG 328
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
5-300 |
3.05e-21 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 92.66 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 5 ILGTGSYLPSQVRTNADLE-------KMVETSDEWIVARTGIKERR--ISAENETV---ADMAFYAAENAIEMAGIDKED 72
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEMEaylglinGKPSRARRIILRNNGIKTRHyaLDPEGRPThsnAQMAAEAIRDLLDDAGFSLGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 73 IDLIIVATTSSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALS--------- 143
Cdd:PRK06816 85 IELLACGTSQPDQLMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVATASELASrwfrasrfe 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 144 ---KTCDPTDRSTIILF---------GDAAGAVVVGASEEPGILSTHIysdgKYGELLSL--EVP---------ERGGDA 200
Cdd:PRK06816 165 aeeEKLAELEENPEIAFekdflrwmlSDGAGAVLLENKPRPDGLSLRI----DWIDLRSYagELPvcmyagaekNEDGSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 201 DKWLHMAGNEVFK---VAVTQLSKLV------------KDTLAANNMDKSELDWLVPHQANYRIISATAKKLTMSldQVV 265
Cdd:PRK06816 241 KGWSDYPPEEAEAasaLSLKQDVRLLnenivvytikplLELVDKRNLDPDDIDYFLPHYSSEYFREKIVELLAKA--GFM 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 498123120 266 ITLDK-------HGNTSAATVPTALDEAVRDGRIKRGQTLLL 300
Cdd:PRK06816 319 IPEEKwftnlatVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
37-306 |
2.87e-18 |
|
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 442651 [Multi-domain] Cd Length: 382 Bit Score: 84.46 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 37 TGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVATTSSshtfP----SSACQVQGKLGI-KGCPAFDLAAA 111
Cdd:COG3425 37 LGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGTESG----PdaskPIATYVHGALGLpPNCRAFELKFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 112 CSGFVYALSVADQHIKTGMCKNVLVIGAD----ALSKTCDPTdrstiilFGDAAGAVVVGasEEPGILS----THIYS-- 181
Cdd:COG3425 113 CYAGTAALQAALGWVASGPNKKALVIASDiaryGPGSAGEYT-------QGAGAVAMLVG--ADPRIAEieggSGSYTtd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 182 ---------------DGKYGELLSLEvperggdadkwlhmagnevfkvavtQLSKLVKDTLAANNMDKSELDWLVPHQAN 246
Cdd:COG3425 184 vmdfwrpngsdyplvDGRFSEPAYLD-------------------------HLEEAVKDYKEKTGLKPDDFDYFVFHQPF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498123120 247 YRIISATAKKLTMS---------LDQVVITLDKH---GNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGG 306
Cdd:COG3425 239 GKMPKKAAKKLGRKagreiqedfEEQVEPSLIYSrriGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSG 310
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
1-306 |
9.97e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 70.71 E-value: 9.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 1 MYSKILGTGSYLPSQVRTNADLEKMVETSDEWIVARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVAT 80
Cdd:PRK04262 1 MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 81 TSSSHTFPSSACQVQGKLGI-KGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGAD-ALSKTCDPTDrstiilFG 158
Cdd:PRK04262 81 ESHPYAVKPTATIVAEALGAtPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADtAQGAPGDALE------YT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 159 DAAGAV--VVGASEEPGILStHIYSdgkygelLSLEVPE---RGGDAdkwLHMAGNEV------FKvavtQLSKLVKDTL 227
Cdd:PRK04262 155 AAAGGAafIIGKEEVIAEIE-ATYS-------YTTDTPDfwrREGEP---YPRHGGRFtgepayFK----HIISAAKGLM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 228 AANNMDKSELDWLVPHQANYRIISATAKKLTMSLDQVVITL--DKHGNTSAATVPTALdEAVRDgRIKRGQTLLLEAFGG 305
Cdd:PRK04262 220 EKLGLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGL-AAVLD-VAKPGDRILVVSFGS 297
|
.
gi 498123120 306 G 306
Cdd:PRK04262 298 G 298
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
48-180 |
1.74e-12 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 67.29 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 48 NETVADMAFYAAENAIEMAGIDKEDIDLIIVATTSSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIK 127
Cdd:cd00829 13 DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPATRVEAAGASGSAAVRAAAAAIA 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 498123120 128 TGMCKNVLVIGADALSktcdptDRSTIILFGDAAGAVVVGASEEPGILSTHIY 180
Cdd:cd00829 93 SGLADVVLVVGAEKMS------DVPTGDEAGGRASDLEWEGPEPPGGLTPPAL 139
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
51-310 |
2.75e-08 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 54.66 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 51 VADMAFYAAENAIEMAGIDKEDIDLIIVATTSSSHtFPSSACQVQGKLGIKgcPAFDLA----AACSGFVYALSVADQHI 126
Cdd:PLN03168 101 VPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVN-MPGADHALAKLLGLK--PTVKRVmmyqTGCFGGASVLRVAKDLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 127 KTGMCKNVLVIGADALSKTCDPTDRSTI------ILFGDAAGAVVVGASEEPGIlSTHIYSDGKYGELLsleVPERGGDA 200
Cdd:PLN03168 178 ENNKGARVLAVASEVTAVTYRAPSENHLdglvgsALFGDGAGVYVVGSDPKPEV-EKALFEVHWAGETI---LPESDGAI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 201 DKWLHMAG--NEVFKVAVTQLSKLVKDTL-----AANNMDKSELDWLVpHQANYRIISATAKKLTMSLDQVVITLD---K 270
Cdd:PLN03168 254 DGHLTEAGliFHLMKDVPGLISKNIEKFLnearkCVGSPDWNEMFWAV-HPGGPAILDQVEAKLKLTKDKMQGSRDilsE 332
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 498123120 271 HGNTSAATVPTALDEaVRDGRIKRGQTLLLEAFGGGFTWG 310
Cdd:PLN03168 333 FGNMSSASVLFVLDQ-IRQRSVKMGASTLGEGSEFGFFIG 371
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
54-163 |
5.32e-08 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 53.56 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 54 MAFYAAENAIEMAGIDKEDIDL----IIVATTS---------------------SSHTFPSS-----ACQVQGKLGIKGc 103
Cdd:COG0304 74 YALAAAREALADAGLDLDEVDPdrtgVIIGSGIggldtleeayrallekgprrvSPFFVPMMmpnmaAGHVSIRFGLKG- 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 104 PAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADAlsktcdPTDRSTIILFgDAAGA 163
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEA------AITPLGLAGF-DALGA 205
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
52-143 |
3.59e-07 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 51.00 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 52 ADMAFYAAENAIEMAGIDKEDIDL----IIVATT---------------------SSSHTFPSS-----ACQVQGKLGIK 101
Cdd:cd00834 72 AQFALAAAEEALADAGLDPEELDPerigVVIGSGigglatieeayrallekgprrVSPFFVPMAlpnmaAGQVAIRLGLR 151
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 498123120 102 GcPAFDLAAACSGFVYALSVADQHIKTGMCKNVLVIGADALS 143
Cdd:cd00834 152 G-PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
50-162 |
1.10e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 46.38 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 50 TVADMAFYAAENAIEMAGIDKEDIDLIIVATTSSSHTFPSSACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTG 129
Cdd:PRK12578 20 SVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLRVEAMCATGLAASLTAYTAVASG 99
|
90 100 110
....*....|....*....|....*....|...
gi 498123120 130 MCKNVLVIGADALSKtcdpTDRSTIILFGDAAG 162
Cdd:PRK12578 100 LVDMAIAVGVDKMTE----VDTSTSLAIGGRGG 128
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
47-158 |
2.67e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 45.32 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 47 ENETVADMAFYAAENAIEMAGIDKEDIDLIIVATTS---SSHTFPSS-ACQVQGKLGIKgcPAFDLAAACSGFVYALSVA 122
Cdd:PRK07516 18 DAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNagfSPQDFPASlVLQADPALRFK--PATRVENACATGSAAVYAA 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 498123120 123 DQHIKTGMCKNVLVIGADALSKTcdPTDRSTIILFG 158
Cdd:PRK07516 96 LDAIEAGRARIVLVVGAEKMTAT--PTAEVGDILLG 129
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
58-144 |
4.14e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 44.75 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 58 AAENAIEMAGIDKEDIDLIIVATT--SSSHTFPSSACQVQgKLGIKGCPAFDLAAACSGFVYALSVADQHIKTGMCKNVL 135
Cdd:PRK06059 30 AARAALADAGLDWRDVQLVVGADTirNGYPGFVAGATFAQ-ALGWNGAPVSSSYAACASGSQALQSARAQILAGLCDVAL 108
|
....*....
gi 498123120 136 VIGADALSK 144
Cdd:PRK06059 109 VVGADTTPK 117
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
35-160 |
2.34e-04 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 41.90 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 35 ARTGIKERRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVATTSSSHTFPSSACQVQGKLGI-KGCPAFDLAAACS 113
Cdd:pfam00108 7 ARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIpDSAPAVTINKVCG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 498123120 114 GFVYALSVADQHIKTGMCKNVLVIGADALSK--TCDPTDRSTIILFGDA 160
Cdd:pfam00108 87 SGLKAVYLAAQSIASGDADVVLAGGVESMSHapYALPTDARSGLKHGDE 135
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
43-315 |
1.17e-03 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 40.07 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 43 RISAENETVADMAFYAAENAIEMAGIDKEDIDLIiVATTSSSHTFPSSACQVQGKLGIKgcP-------AFdlaAACSGF 115
Cdd:PLN03169 98 RLDIANEAVTQMAVEASLACIKEWGRPVSDITHL-VYVSSSEARLPGGDLYLAKQLGLS--PdvqrvmlYF---LGCSGG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 116 VYALSVADQHIKTGMCKNVL-------VIGADALSKTcDPTDRSTIILFGDAAGAVVVGASEEPGILS------------ 176
Cdd:PLN03169 172 VAGLRVAKDIAENNPGSRVLlttsettILGFRPPSPD-RPYDLVGAALFGDGAAAVIIGADPIPVSESpffelhtaiqqf 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 177 ---THIYSDGKYGE-----LLSLEVPER-----GGDADKWLHMAGNEvfkvavtqlsklvkdtlaanNMDKSELDWLVpH 243
Cdd:PLN03169 251 lpgTEKTIDGRLTEeginfKLGRELPQKiedniEGFCKKLMKKAGLV--------------------EKDYNDLFWAV-H 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 244 QANYRIISATAKKLTMSLDQVVIT---LDKHGNTSAATVPTALdEAVRDGRIKRGQT-----LLLeAFGGGFTWGSALVK 315
Cdd:PLN03169 310 PGGPAILNRLEKKLKLAPEKLECSrraLMDYGNVSSNTIVYVL-EYMREELKKKGEEdeewgLIL-AFGPGITFEGILAR 387
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
53-160 |
1.19e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 40.27 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 53 DMAFYAAENAIEMAGIDKEDIDLIIVATTSSShTFPS---SACQVQGKLGIKGCPAFDLAAACSGFVYALSVADQHIKTG 129
Cdd:PRK06064 24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSAG-LFVSqehIAALIADYAGLAPIPATRVEAACASGGAALRQAYLAVASG 102
|
90 100 110
....*....|....*....|....*....|.
gi 498123120 130 MCKNVLVIGADALSKTCDPTDRSTIILFGDA 160
Cdd:PRK06064 103 EADVVLAAGVEKMTDVPTPDATEAIARAGDY 133
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
181-315 |
4.65e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 38.42 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 181 SDGKYGELLSLEVPERGGDAdkwlhmagnevFKVAVTQLSKLVKD---------TLAANNMDKSELDWLVP--------- 242
Cdd:PLN02192 334 SAGKIGVSLSKDLMAVAGDA-----------LKTNITTLGPLVLPmseqllffaTLVGKKLFKMKLKPYIPdfklafehf 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498123120 243 --HQANYRIISATAKKLTMS---LDQVVITLDKHGNTSAATVPTALDEAVRDGRIKRGQTLLLEAFGGGFTWGSALVK 315
Cdd:PLN02192 403 ciHAGGRAVLDELEKNLQLSdwhMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIKKGDRTWQIAFGSGFKCNSAVWK 480
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
42-161 |
6.80e-03 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 37.75 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 42 RRISAENETVADMAFYAAENAIEMAGIDKEDIDLIIVAttssshTFPSSACQVQGKLG---------IKGCPAFDLAAAC 112
Cdd:PRK06289 17 RNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVG------NFFGELFAGQGHLGampatvhpaLWGVPASRHEAAC 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 498123120 113 -SGFVYALSvADQHIKTGMCKNVLVIGADaLSKTCdPTDRSTIILfGDAA 161
Cdd:PRK06289 91 aSGSVATLA-AMADLRAGRYDVALVVGVE-LMKTV-PGDVAAEHL-GAAA 136
|
|
| PRK08304 |
PRK08304 |
stage V sporulation protein AD; Validated |
54-137 |
6.85e-03 |
|
stage V sporulation protein AD; Validated
Pssm-ID: 236230 Cd Length: 337 Bit Score: 37.90 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 54 MAFYAAENAIEMAGIDKEDIDLIIVA-----TTSSSHtfpssacqVQGKLGIkgcPAFDLAAACSGFVYALSVADQHIKT 128
Cdd:PRK08304 59 MMEDAIQQALQKANLKKSDIDYLLAGdllnqIISANF--------AARELGI---PFLGLYGACSTMMESLALGSMLIDG 127
|
....*....
gi 498123120 129 GMCKNVLVI 137
Cdd:PRK08304 128 GFADRVLAA 136
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
62-166 |
9.47e-03 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 37.54 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498123120 62 AIEMAGIDKEDIDL----IIVATTSS-------SHTFPSSACQVQG------------KLGIKGcPAFDLAAACSGFVYA 118
Cdd:cd00833 98 ALEDAGYSPESLAGsrtgVFVGASSSdylellaRDPDEIDAYAATGtsraflanrisyFFDLRG-PSLTVDTACSSSLVA 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498123120 119 LSVADQHIKTGMCKNVLVIGAD---------------ALSKT--CDPTDRS---TIilFGDAAGAVVV 166
Cdd:cd00833 177 LHLACQSLRSGECDLALVGGVNlilspdmfvgfskagMLSPDgrCRPFDADadgYV--RGEGVGVVVL 242
|
|
| |
