|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
1-309 |
0e+00 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 548.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT 80
Cdd:PRK09352 2 MYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VTPDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDG 160
Cdd:PRK09352 82 TTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCVLFGDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 161 AGAVVMGPvSEGRGILSFELGADGTGGKHLY----------KEEYIVMNGREVFKFAVRQMGESCIHVLEKAGLSKNDVD 230
Cdd:PRK09352 162 AGAVVLGA-SEEPGILSTHLGSDGSYGDLLYlpgggsrgpaSPGYLRMEGREVFKFAVRELAKVAREALEAAGLTPEDID 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502276033 231 FLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLTWGAIALRWG 309
Cdd:PRK09352 241 WLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRWP 319
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
1-308 |
3.76e-179 |
|
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: 497.32 E-value: 3.76e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT 80
Cdd:COG0332 1 RNVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VTPDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDG 160
Cdd:COG0332 81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 161 AGAVVMGPVSEGRGILSFELGADGTGGKHLY---------------KEEYIVMNGREVFKFAVRQMGESCIHVLEKAGLS 225
Cdd:COG0332 161 AGAVVLEASEEGPGILGSVLGSDGSGADLLVvpaggsrnppspvdeGDHYLRMDGREVFKFAVRNLPEVIREALEKAGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 226 KNDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLTWGAIA 305
Cdd:COG0332 241 LDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAV 320
|
...
gi 502276033 306 LRW 308
Cdd:COG0332 321 LRW 323
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
2-306 |
1.67e-171 |
|
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: 477.80 E-value: 1.67e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 2 GAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVATV 81
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 82 TPDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDGA 161
Cdd:cd00830 81 TPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 162 GAVVMGPVSEGRGILSFELGADGTGGKHLY---------------KEEYIVMNGREVFKFAVRQMGESCIHVLEKAGLSK 226
Cdd:cd00830 161 GAVVLEATEEDPGILDSVLGSDGSGADLLTipaggsrspfedaegGDPYLVMDGREVFKFAVRLMPESIEEALEKAGLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 227 NDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLTWGAIAL 306
Cdd:cd00830 241 DDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
1-308 |
1.41e-169 |
|
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: 473.02 E-value: 1.41e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT 80
Cdd:TIGR00747 1 MYAGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDETSSTMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VTPDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDG 160
Cdd:TIGR00747 81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVLFGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 161 AGAVVMGPVSEGRGILSFELGADGTGGKHLY----------KEEYIVMNGREVFKFAVRQMGESCIHVLEKAGLSKNDVD 230
Cdd:TIGR00747 161 AGAVVLGESEDPGGIISTHLGADGTQGEALYlpaggrptsgPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDID 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502276033 231 FLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLTWGAIALRW 308
Cdd:TIGR00747 241 WFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-309 |
6.75e-164 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 458.94 E-value: 6.75e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT 80
Cdd:PRK12879 3 SYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VTPDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDG 160
Cdd:PRK12879 83 TTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 161 AGAVVMGPVSEGRGILSFELGADGTGGKHLYKE--------------EYIVMNGREVFKFAVRQMGESCIHVLEKAGLSK 226
Cdd:PRK12879 163 AGAVVLEATENEPGFIDYVLGTDGDGGDILYRTglgttmdrdalsgdGYIVQNGREVFKWAVRTMPKGARQVLEKAGLTK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 227 NDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLTWGAIAL 306
Cdd:PRK12879 243 DDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLV 322
|
...
gi 502276033 307 RWG 309
Cdd:PRK12879 323 KWG 325
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
1-308 |
2.40e-125 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 363.29 E-value: 2.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT 80
Cdd:PLN02326 46 SGSKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VTPDRAFPSvSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDG 160
Cdd:PLN02326 126 SSPDDLFGS-APQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTCILFGDG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 161 AGAVVMGPVSEGR-GILSFELGADGTGGKHL---YKEEY-----------------------IVMNGREVFKFAVRQMGE 213
Cdd:PLN02326 205 AGAVVLQACDDDEdGLLGFDMHSDGNGHKHLhatFKGEDddssggntngvgdfppkkasyscIQMNGKEVFKFAVRCVPQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 214 SCIHVLEKAGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMV 293
Cdd:PLN02326 285 VIESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIATA 364
|
330
....*....|....*
gi 502276033 294 GFGGGLTWGAIALRW 308
Cdd:PLN02326 365 GFGAGLTWGSAIVRW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
1-308 |
1.20e-111 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 326.52 E-value: 1.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT 80
Cdd:CHL00203 1 MGVHILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VTPDRAFPSVScMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDG 160
Cdd:CHL00203 81 STPDDLFGSAS-QLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 161 AGAVVMGPVSEGrGILSFELGADGTGGKHL---YKE----------------EYIVMNGREVFKFAVRQMGESCIHVLEK 221
Cdd:CHL00203 160 AGAAIIGASYEN-SILGFKLCTDGKLNSHLqlmNKPvnnqsfgttklpqgqyQSISMNGKEVYKFAVFQVPAVIIKCLNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 222 AGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLTW 301
Cdd:CHL00203 239 LNISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGAGLTW 318
|
....*..
gi 502276033 302 GAIALRW 308
Cdd:CHL00203 319 GAIVLKW 325
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
5-308 |
9.69e-84 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 255.42 E-value: 9.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 5 IIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVATVTPD 84
Cdd:PRK05963 6 IAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSDAGIERSDIALTLLATSTPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 85 RAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAyRYILVVGAEKLSKIIDWNDRNTAVLFGDGAGAV 164
Cdd:PRK05963 86 HLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQG-KPVLVVAANILSRRINMAERASAVLFADAAGAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 165 VMGPVS-EGRGILSFELGADGTG----------------GKHLYKEEYIVM-NGREVFKFAVRQMGESCIHVLEKAGLSK 226
Cdd:PRK05963 165 VLAPSAkANSGVLGSQLISDGSHydlikipaggsarpfaPERDASEFLMTMqDGRAVFTEAVRMMSGASQNVLASAAMTP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 227 NDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLTWGAIAL 306
Cdd:PRK05963 245 QDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAVVM 324
|
..
gi 502276033 307 RW 308
Cdd:PRK05963 325 RV 326
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3-306 |
4.98e-62 |
|
"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: 199.58 E-value: 4.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 3 AGIIGIGRYLPEKVLTNFDLEKMMdtSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVATVT 82
Cdd:cd00827 2 VGIEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 83 PDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVlFGDGAG 162
Cdd:cd00827 80 PIDKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALEPT-LGDGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 163 AVVMG--PVSEGRGILSFELGADGTGGKHLY-----------KEEYIVMNGREVFKFAVRQMGESCI-HVLEKAG---LS 225
Cdd:cd00827 159 AMLVSrnPGILAAGIVSTHSTSDPGYDFSPYpvmdggypkpcKLAYAIRLTAEPAGRAVFEAAHKLIaKVVRKALdraGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 226 KNDVDFLIPHQANI-RIVEAARQRLELPEEKMSTTI----RKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLT 300
Cdd:cd00827 239 SEDIDYFVPHQPNGkKILEAVAKKLGGPPEKASQTRwillRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFT 318
|
....*.
gi 502276033 301 WGAIAL 306
Cdd:cd00827 319 AEAFVL 324
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
5-308 |
1.85e-61 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 198.14 E-value: 1.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 5 IIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMdTSDMAYFAAKKAIEDAKISPQDIDLILVATVTPD 84
Cdd:PRK07204 7 IKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVDGET-SSYMGAEAAKKAVEDAKLTLDDIDCIICASGTIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 85 RAFPSVSCMLQERLGAVKA--AALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDGAG 162
Cdd:PRK07204 86 QAIPCTASLIQEQLGLQHSgiPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILFGDGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 163 AVVMGPVSEGRGILS-----FELGADGT----GGKHLYKEEYIV---------MNGREVFKFAVRQMGESCIHVLEKAGL 224
Cdd:PRK07204 166 AVVITKGDHSSRILAshmetYSSGAHLSeirgGGTMIHPREYSEerkedflfdMNGRAIFKLSSKYLMKFIDKLLMDAGY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 225 SKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGGLTWGAI 304
Cdd:PRK07204 246 TLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRGNKILLLGTSAGLSIGGI 325
|
....
gi 502276033 305 ALRW 308
Cdd:PRK07204 326 LLEY 329
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
1-310 |
2.58e-48 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 164.41 E-value: 2.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLIlVAT 80
Cdd:PRK06840 3 MNVGIVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVV-IYI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VTPDRAFP--SVSCMLQERLGAVKAAALDISAACAGFIYGMVTA-SQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLF 157
Cdd:PRK06840 82 GSEHKDYPvwSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAkDLLYSDPSIENVLLVGGYRNSDLVDYDNPRTRFMF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 158 --GDGAGAVVMGPVSEGRGILSFELGADGT----------GGKHLYKEEyIVMNGRevFKFAVRQ---MGE--------S 214
Cdd:PRK06840 162 nfAAGGSAALLKKDAGKNRILGSAIITDGSfsedvrvpagGTKQPASPE-TVENRQ--HYLDVIDpesMKErldevsipN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 215 CIHV----LEKAGLSKNDVDFLIP-------HQANIriveaarQRLELPEEKmSTTIRKYGNTSAASIPISIVEELEAGK 283
Cdd:PRK06840 239 FLKVireaLRKSGYTPKDIDYLAIlhmkrsaHIALL-------EGLGLTEEQ-AIYLDEYGHLGQLDQILSLHLALEQGK 310
|
330 340
....*....|....*....|....*..
gi 502276033 284 IKDDDLIIMVGFGGGLTWGAIALRWGR 310
Cdd:PRK06840 311 LKDGDLVVLVSAGTGYTWAATVIRWGP 337
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
3-306 |
1.02e-43 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 152.81 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 3 AGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTR----TGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILV 78
Cdd:PRK12880 8 AKISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYICDENTCVSDLGKHAANTLLQGLNIDKNSLDALIV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 79 ATVTPDRAFPSVSCMLQERLG-AVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGaEKLSKIIDWNDRNTAVLF 157
Cdd:PRK12880 88 VTQSPDFFMPSTACYLHQLLNlSSKTIAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICG-DTLSKFIHPKNMNLAPIF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 158 GDGAGAVVMGPVSEGRGIlsFELGADGTG--------------------GKHLYK-EEY-----IVMNGREVFKFAVRQM 211
Cdd:PRK12880 167 GDGVSATLIEKTDFNEAF--FELGSDGKYfdkliipkgamripkadifnDDSLMQtEEFrqlenLYMDGANIFNMALECE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 212 GESCIHVLEKAGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTTI-RKYGNTSAASIPiSIVEELEAGKikdDDLI 290
Cdd:PRK12880 245 PKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPNFImEKYANLSACSLP-ALLCELDTPK---EFKA 320
|
330
....*....|....*.
gi 502276033 291 IMVGFGGGLTWGAIAL 306
Cdd:PRK12880 321 SLSAFGAGLSWGSAVL 336
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
219-308 |
1.02e-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: 144.57 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 219 LEKAGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGGG 298
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 502276033 299 LTWGAIALRW 308
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
5-308 |
1.17e-40 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 144.25 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 5 IIGIGRYLPEKVLTNFDLEKMMdtSDEWIRTR---------TGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDL 75
Cdd:PRK09258 8 ILSLAYELAPVVVTSSEIEERL--APLYERLRlppgqlealTGIRERRWWPEGTQLSDGAIAAGRKALAEAGIDPSDIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 76 ILVATVTPDRAFPSVSCMLQERLGAVK-AAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDW------ 148
Cdd:PRK09258 86 LINTSVCRDYLEPATACRVHHNLGLPKsCANFDVSNACLGFLNGMLDAANMIELGQIDYALVVSGESAREIVEAtidrll 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 149 NDRNTAVLF---------GDGAGAVVMGPVSEGRGILSFELGADGTGGKH----LYKEEYIVMNGREVFKFAVRQMGESC 215
Cdd:PRK09258 166 APETTREDFaqsfatltlGSGAAAAVLTRGSLHPRGHRLLGGVTRAATEHhelcQGGRDGMRTDAVGLLKEGVELAVDTW 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 216 IHVLEKAGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGF 295
Cdd:PRK09258 246 EAFLAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVALLGI 325
|
330
....*....|...
gi 502276033 296 GGGLTWGAIALRW 308
Cdd:PRK09258 326 GSGLNCSMLEVKW 338
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
106-184 |
2.42e-38 |
|
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: 130.33 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 106 LDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWNDRNTAVLFGDGAGAVVMGPV-SEGRGILSFELGADG 184
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATdEPGARILDSVLGSDG 80
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
54-307 |
1.46e-29 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 115.36 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 54 MAYFAAKKAIEDAKISPQDIDLILVATVTPDRAFPSVSCMLQERLGAvKAAALDISAACAGFIYGMVTASQFIDNGAYRY 133
Cdd:PRK07515 98 MGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGI-EGFAFDMNVACSSATFGIQTAANAIRSGSARR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 134 ILVVGAEKLSKIIDWNDRNTAVLFGDGAGAVVMGPVSEGRGILSFE-LG---------------------ADGTGGKhly 191
Cdd:PRK07515 177 VLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVERADTATSAGGFEiLGtrlftqfsnnirnnfgflnraDPEGIGA--- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 192 KEEYIVMNGREVFKFAVRQMGESCIHVLEKAGLSKNDVDFLIPHQANIRIVEAARQRL---ELPEEKMSTTIRKYGNTSA 268
Cdd:PRK07515 254 RDKLFVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKRFWLHQANINMNQLIGKKVlgrDATPEEAPVILDEYANTSS 333
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 502276033 269 ASipiSIV------EELEAGkikddDLIIMVGFGGGLTWGAIALR 307
Cdd:PRK07515 334 AG---SIIafhkhsDDLAAG-----DLGVICSFGAGYSIGSVIVR 370
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
54-306 |
9.64e-27 |
|
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: 107.34 E-value: 9.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 54 MAYFAAKKAIEDAKISPQD----IDLILVAT---------------------VTPDRAFPSVSCMLQERLGaVKAAALDI 108
Cdd:cd00825 14 LGFEAAERAIADAGLSREYqknpIVGVVVGTgggsprfqvfgadamravgpyVVTKAMFPGASGQIATPLG-IHGPAYDV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 109 SAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIID------------------WNDRNTAVLFGDGAGAVVMGPVS 170
Cdd:cd00825 93 SAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDcefdamgalstpekasrtFDAAADGFVFGDGAGALVVEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 171 EGR--------GILSFELGADGTGGKHLykeeyiVMNGREVfkfaVRQMGEScihvLEKAGLSKNDVDFLIPHQANIRIV 242
Cdd:cd00825 173 HALargahiyaEIVGTAATIDGAGMGAF------APSAEGL----ARAAKEA----LAVAGLTVWDIDYLVAHGTGTPIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 243 EAARQRLELPEEK-----MSTTIRKYGNTSAASIPISIVEELEAGKIKDD-------------------------DLIIM 292
Cdd:cd00825 239 DVKELKLLRSEFGdkspaVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIppsihieeldeaglnivtettprelRTALL 318
|
330
....*....|....
gi 502276033 293 VGFGGGLTWGAIAL 306
Cdd:cd00825 319 NGFGLGGTNATLVL 332
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
7-300 |
3.85e-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: 103.07 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 7 GIGRYLPEKVLTNFDLEK---MMDTSDEW----IRTRTGIEER-RIATDDMDtsDMAYFAAKKAIEDAKISPQDIDLILV 78
Cdd:cd00831 35 PELKEKLKRLCAKTGIETrylVLPGGEETyaprPEMSPSLDERnDIALEEAR--ELAEEAARGALDEAGLRPSDIDHLVV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 79 ATVTpDRAFPSVSCMLQERLG---AVKaaALDISA-ACAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKIIDWND-RNT 153
Cdd:cd00831 113 NTST-GNPTPSLDAMLINRLGlrpDVK--RYNLGGmGCSAGAIALDLAKDLLEANPGARVLVVSTELCSLWYRGPDhRSM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 154 AV---LFGDGAGAVVMG--PVSEGRGILSFEL---------GADGTGGKHLYKEEYIVMNGREVFKFAVRQMGESCIHVL 219
Cdd:cd00831 190 LVgnaLFGDGAAAVLLSndPRDRRRERPLFELvraastllpDSEDAMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 220 EKA--GLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMS---TTIRKYGNTSAASIpISIVEELEA-GKIKDDDLIIMV 293
Cdd:cd00831 270 ARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEasrMVLRRYGNMSSSSV-LYVLAYMEAkGRVKRGDRGLLI 348
|
....*..
gi 502276033 294 GFGGGLT 300
Cdd:cd00831 349 AFGPGFT 355
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
58-306 |
3.66e-24 |
|
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: 98.67 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 58 AAKKAIEDAKISPQDIDLILVATVTPDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAYRYILVV 137
Cdd:cd00327 14 AAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 138 GAEKlskiidwndrntaVLFGDGAGAVVMGPVSEGR--------GILSFELGADGTGGkhlykeeyIVMNGREVFKFAVR 209
Cdd:cd00327 94 GSEE-------------FVFGDGAAAAVVESEEHALrrgahpqaEIVSTAATFDGASM--------VPAVSGEGLARAAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 210 QmgescihVLEKAGLSKNDVDFLIPHQANIRIVEAARQRLELPEEK-----MSTTIRKYGNTSAASIPISIVE---ELEA 281
Cdd:cd00327 153 K-------ALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGvrspaVSATLIMTGHPLGAAGLAILDElllMLEH 225
|
250 260
....*....|....*....|....*....
gi 502276033 282 GKIKDD----DLIIMVGFGGGLTWGAIAL 306
Cdd:cd00327 226 EFIPPTprepRTVLLLGFGLGGTNAAVVL 254
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
1-298 |
1.51e-22 |
|
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: 96.40 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT 80
Cdd:COG3425 1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAGIDPSDIGAVYVGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VT-PDrAFPSVSCMLQERLGAVKAA-ALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEklskiIDWNDRNTAVLFG 158
Cdd:COG3425 81 ESgPD-ASKPIATYVHGALGLPPNCrAFELKFACYAGTAALQAALGWVASGPNKKALVIASD-----IARYGPGSAGEYT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 159 DGAGAVVMgPVSEGRGILSFELGAdGTGGKHLY------KEEYIVMNGR---EVFKFAVRQMGEsciHVLEKAGLSKNDV 229
Cdd:COG3425 155 QGAGAVAM-LVGADPRIAEIEGGS-GSYTTDVMdfwrpnGSDYPLVDGRfsePAYLDHLEEAVK---DYKEKTGLKPDDF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 230 DFLIPHQANIRIVEAARQRL---------ELPEEKMSTTI---RKYGNTSAASIPISIVEELEAGKIKDDDLIIMVGFGG 297
Cdd:COG3425 230 DYFVFHQPFGKMPKKAAKKLgrkagreiqEDFEEQVEPSLiysRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGS 309
|
.
gi 502276033 298 G 298
Cdd:COG3425 310 G 310
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
5-308 |
1.93e-21 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 92.90 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 5 IIGIGRYLPEKVLTNFD----LEKMMDTSDEWIR------TRTGIEERRIATDD------------MDT-----SDMAYF 57
Cdd:COG3424 4 ILSIATAVPPHRYTQEEiaefAAELFGLDERDRRrlrrlfENSGIETRHSVLPLewyleppsfgerNALyieeaLELAEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 58 AAKKAIEDAKISPQDIDLILVATVTPdRAFPSVSCMLQERLGavkaaaLDISAA--------CAGFIYGMVTASQFIDng 129
Cdd:COG3424 84 AARRALDKAGLDPEDIDHLVTVSCTG-FAAPGLDARLINRLG------LRPDVRrlpvggmgCAAGAAGLRRAADFLR-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 130 AY--RYILVVGAE--KLSKIIDWNDRNTAV---LFGDGAGAVVMgpVSEGRGILSFELGADGTggkHLYKEEYIVM---- 198
Cdd:COG3424 155 ADpdAVVLVVCVElcSLTFQRDDDSKDNLVanaLFGDGAAAVVV--SGDPRPGPGPRILAFRS---YLIPDTEDVMgwdv 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 199 --NG------REVFKFAVRQMGESCIHVLEKAGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTT---IRKYGNTS 267
Cdd:COG3424 230 gdTGfrmvlsPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSrevLREYGNMS 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502276033 268 AASIpISIVEE-LEAGKIKDDDLIIMVGFGGGLTWGAIALRW 308
Cdd:COG3424 310 SATV-LFVLERlLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
1-298 |
1.03e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 79.18 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 1 MGAGIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT 80
Cdd:PRK04262 1 MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAGIDPKEIGAVYVGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 81 VTPDRAFPSVSCMLQERLGAVK-AAALDISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKlskiidwndRNTAVlfGD 159
Cdd:PRK04262 81 ESHPYAVKPTATIVAEALGATPdLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADT---------AQGAP--GD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 160 --------GAGAVVMG---PVSEGRGILSFElgadgTGGKHLYKEE---YIVMNGR-----EVFKF---AVRQMgescih 217
Cdd:PRK04262 150 aleytaaaGGAAFIIGkeeVIAEIEATYSYT-----TDTPDFWRREgepYPRHGGRftgepAYFKHiisAAKGL------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 218 vLEKAGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTTI--RKYGNTSAASIPISIVEELEagKIKDDDLIIMVGF 295
Cdd:PRK04262 219 -MEKLGLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGLAAVLD--VAKPGDRILVVSF 295
|
...
gi 502276033 296 GGG 298
Cdd:PRK04262 296 GSG 298
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
47-150 |
1.91e-13 |
|
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: 69.98 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 47 DDMDTSDMAYFAAKKAIEDAKISPQDIDLILVATVTPDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFI 126
Cdd:cd00829 12 SDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPATRVEAAGASGSAAVRAAAAAI 91
|
90 100
....*....|....*....|....
gi 502276033 127 DNGAYRYILVVGAEKLSKIIDWND 150
Cdd:cd00829 92 ASGLADVVLVVGAEKMSDVPTGDE 115
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
5-292 |
6.87e-13 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 68.40 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 5 IIGIGRYLPEKVLTNFDLEK---MMDTSDEWIRTR----TGIEERRIATDD-----MDTSDMAYFAAKKAIEDAKISPQD 72
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEMEAylgLINGKPSRARRIilrnNGIKTRHYALDPegrptHSNAQMAAEAIRDLLDDAGFSLGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 73 IDLILVATVTPDRAFPSVSCMLQerlGAVKAAALDISAA---CAGFIYGMVTASQFIDNGAYRYILVVGAEKLSKI---- 145
Cdd:PRK06816 85 IELLACGTSQPDQLMPGHASMVH---GELGAPPIEVVSSagvCAAGMMALKYAYLSVKAGESRNAVATASELASRWfras 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 146 --------IDWNDRNTAVLF---------GDGAGAVVM--GPVSEGRG-------ILSF------------ELGADGT-- 185
Cdd:PRK06816 162 rfeaeeekLAELEENPEIAFekdflrwmlSDGAGAVLLenKPRPDGLSlridwidLRSYagelpvcmyagaEKNEDGSlk 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 186 GGKHLYKEE---YIVMNGREVFK----FAVRQMGESCIHVLEKAGLSKNDVDFLIPHQANIRIVEA-----ARQRLELPE 253
Cdd:PRK06816 242 GWSDYPPEEaeaASALSLKQDVRllneNIVVYTIKPLLELVDKRNLDPDDIDYFLPHYSSEYFREKivellAKAGFMIPE 321
|
330 340 350
....*....|....*....|....*....|....*....
gi 502276033 254 EKMSTTIRKYGNTSAASIPISIVEELEAGKIKDDDLIIM 292
Cdd:PRK06816 322 EKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
112-307 |
9.12e-10 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 58.94 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 112 CAGFIYGMVTASQFIDNGAYRYILVVGAEklSKIIDWNDRNT--------AVLFGDGAGAVVMG----PVSEG------R 173
Cdd:PLN03169 168 CSGGVAGLRVAKDIAENNPGSRVLLTTSE--TTILGFRPPSPdrpydlvgAALFGDGAAAVIIGadpiPVSESpffelhT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 174 GILSFELGADGTGGKHLYKEEYIVMNGREVFKFAVRQMGESCIHVLEKAGLSKNDVD--FLIPHQANIRIVEAARQRLEL 251
Cdd:PLN03169 246 AIQQFLPGTEKTIDGRLTEEGINFKLGRELPQKIEDNIEGFCKKLMKKAGLVEKDYNdlFWAVHPGGPAILNRLEKKLKL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502276033 252 PEEKMSTT---IRKYGNTSAASIPI---SIVEELEAGKIKDDDLIIMVGFGGGLTWGAIALR 307
Cdd:PLN03169 326 APEKLECSrraLMDYGNVSSNTIVYvleYMREELKKKGEEDEEWGLILAFGPGITFEGILAR 387
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
47-162 |
2.11e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 48.69 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 47 DDMDTSDMAYFAAKKAIEDAKISPQDIDLILVATVtpdrAFPSVSCM----LQERLGAVKAAALDISAACAGFIYGMVTA 122
Cdd:PRK12578 17 DDVSVQELAWESIKEALNDAGVSQTDIELVVVGST----AYRGIELYpapiVAEYSGLTGKVPLRVEAMCATGLAASLTA 92
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 502276033 123 SQFIDNGAYRYILVVGAEKLSKIidwnDRNTAVLFGDGAG 162
Cdd:PRK12578 93 YTAVASGLVDMAIAVGVDKMTEV----DTSTSLAIGGRGG 128
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
36-143 |
2.40e-06 |
|
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: 48.07 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 36 RTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLIlvatvtpdrafpSVSCMLQERLGAV--KAAALD------ 107
Cdd:pfam00108 8 RTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEV------------IVGNVLQAGEGQNpaRQAALKagipds 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 502276033 108 -----ISAACAGFIYGMVTASQFIDNGAYRYILVVGAEKLS 143
Cdd:pfam00108 76 apavtINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMS 116
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
47-143 |
4.28e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 47.63 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 47 DDMDTSDMAYFAAKKAIEDAKISPQDIDLILVAT----VTPDrAFPSvSCMLQ--ERLGAVKAAALDisAACAGFIYGMV 120
Cdd:PRK07516 18 DAETLESLIVRVAREALAHAGIAAGDVDGIFLGHfnagFSPQ-DFPA-SLVLQadPALRFKPATRVE--NACATGSAAVY 93
|
90 100
....*....|....*....|...
gi 502276033 121 TASQFIDNGAYRYILVVGAEKLS 143
Cdd:PRK07516 94 AALDAIEAGRARIVLVVGAEKMT 116
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
54-307 |
8.85e-06 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 46.96 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 54 MAYFAAKKAIEDAKISPQDIDLILVATvTPDRAFPSVSCMLQERLG---AVKAAALdISAACAGFIYGMVTASQFIDNGA 130
Cdd:PLN03168 104 LAAEAAQKAIKEWGGRKSDITHIVFAT-TSGVNMPGADHALAKLLGlkpTVKRVMM-YQTGCFGGASVLRVAKDLAENNK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 131 YRYILVVGAEKLSKIIDWNDRN------TAVLFGDGAGAVVMG--PVSEGRGILsFELG---------ADGTGGKHLYKE 193
Cdd:PLN03168 182 GARVLAVASEVTAVTYRAPSENhldglvGSALFGDGAGVYVVGsdPKPEVEKAL-FEVHwagetilpeSDGAIDGHLTEA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 194 EYIVMNGREVFKFAVRQMGESCIHVLEKAGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTT---IRKYGNTSAAS 270
Cdd:PLN03168 261 GLIFHLMKDVPGLISKNIEKFLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKLTKDKMQGSrdiLSEFGNMSSAS 340
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 502276033 271 IpISIVEELEAGKIK--------DDDLIIMVGFGGGLTWGAIALR 307
Cdd:PLN03168 341 V-LFVLDQIRQRSVKmgastlgeGSEFGFFIGFGPGLTLEVLVLR 384
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
156-306 |
1.30e-04 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 43.12 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 156 LFGDGAGAVVMGP-------------VSEGRGILSfelGADGTGGKHLYKEEYIVMNGREVFKFAVRQMGESCIHVLEKA 222
Cdd:PLN03172 214 LFGDGAAAVIIGAdpdtkierplfeiVSAAQTILP---DSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 223 GLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTT---IRKYGNTSAASIpISIVEE-----LEAGKIKDDDLI---I 291
Cdd:PLN03172 291 GINDWNSIFWIAHPGGPAILDQVEIKLDLKEEKLRATrhvLSDYGNMSSACV-LFILDEmrkksIEEGKGSTGEGLewgV 369
|
170
....*....|....*
gi 502276033 292 MVGFGGGLTWGAIAL 306
Cdd:PLN03172 370 LFGFGPGLTVETVVL 384
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
53-143 |
1.50e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 42.96 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 53 DMAYFAAKKAIEDAKISPQDIDLILVATVTPDRaFPSvscmlQERLGAVKA--------AALDISAACAGFIYGMVTASQ 124
Cdd:PRK06064 24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGL-FVS-----QEHIAALIAdyaglapiPATRVEAACASGGAALRQAYL 97
|
90
....*....|....*....
gi 502276033 125 FIDNGAYRYILVVGAEKLS 143
Cdd:PRK06064 98 AVASGEADVVLAAGVEKMT 116
|
|
| HMG-CoA-S_euk |
TIGR01833 |
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ... |
4-249 |
3.75e-04 |
|
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA synthase is the first step of isopentenyl pyrophosphate (IPP) biosynthesis via the mevalonate pathway. This pathway is found mainly in eukaryotes, but also in archaea and some bacteria. This model is specific for eukaryotes.
Pssm-ID: 273826 [Multi-domain] Cd Length: 457 Bit Score: 41.68 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 4 GIIGIGRYLPEKVLTNFDLEKmMDTSDEWIRTrTGIEERRIA--TDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVATV 81
Cdd:TIGR01833 6 GILALEIYFPSQYVDQAELEK-YDGVSAGKYT-IGLGQTKMGfcTDREDINSLCLTVVSKLMERYNIDYDQIGRLEVGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 82 T---PDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAY--RYILVVGAEkLSKIIDWNDRNTAvl 156
Cdd:TIGR01833 84 TiidKSKSVKTVLMQLFEESGNTDVEGIDTTNACYGGTAALFNAINWIESSSWdgRYALVVAGD-IAVYAKGNARPTG-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 157 fgdGAGAVVM--GPvsegRGILSFELGADGTGGKHLYK-------EEYIVMNGREVFKFAVRQMgESCIHVLEK------ 221
Cdd:TIGR01833 161 ---GAGAVAMliGP----NAPIVFERGLRGSHMQHAYDfykpdlaSEYPVVDGKLSIQCYLSAL-DRCYKSYCKkiekqw 232
|
250 260 270
....*....|....*....|....*....|....
gi 502276033 222 ------AGLSKNDVDFLIPHQANIRIVEAARQRL 249
Cdd:TIGR01833 233 gksgsdRKFTLDDFDYMIFHSPYCKLVQKSLARL 266
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
156-306 |
4.47e-04 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 41.60 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 156 LFGDGAGAVVMGP-------------VSEGRGILSfelGADGTGGKHLYKEEYIVMNGREVFKFAVRQMGESCIHVLEKA 222
Cdd:PLN03173 214 LFGDGAAAIIIGSdpvlgvekplfelVSAAQTILP---DSDGAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 223 GLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTT---IRKYGNTSAASIpISIVEELEAGKIKDD--------DLII 291
Cdd:PLN03173 291 GISDWNSLFWIAHPGGPAILDQVEAKLALKPEKLRATrhvLSEYGNMSSACV-LFILDEMRKKSAEDGlkstgeglEWGV 369
|
170
....*....|....*
gi 502276033 292 MVGFGGGLTWGAIAL 306
Cdd:PLN03173 370 LFGFGPGLTVETVVL 384
|
|
| HMG_CoA_synt_N |
pfam01154 |
Hydroxymethylglutaryl-coenzyme A synthase N terminal; |
4-168 |
2.18e-03 |
|
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
Pssm-ID: 307348 [Multi-domain] Cd Length: 173 Bit Score: 38.37 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 4 GIIGIGRYLPEKVLTNFDLEKMMDTSDEWIRTRTGIEERRIATDDMDTSDMAYFAAKKAIEDAKISPQDIDLILVATVT- 82
Cdd:pfam01154 5 GILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMERYNLPWDKIGRLEVGTETi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 83 --PDRAFPSVSCMLQERLGAVKAAALDISAACAGFIYGMVTASQFIDNGAY--RYILVVGAEklskIIDWNDRNTAVLFG 158
Cdd:pfam01154 85 idKSKSVKSVLMQLFQESGNTDIEGIDTTNACYGGTAALFNAANWIESSSWdgRYALVVCGD----IAIYPSGNARPTGG 160
|
170
....*....|
gi 502276033 159 DGAGAVVMGP 168
Cdd:pfam01154 161 AGAVAMLIGP 170
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
156-306 |
3.06e-03 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 38.93 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 156 LFGDGAGAVVMGP-------------VSEGRGILSFELGA-DGtggkHLYKEEYIVMNGREVFKFAVRQMGESCIHVLEK 221
Cdd:PLN03170 218 LFGDGAAAVIVGAdpderverplfqlVSASQTILPDSEGAiDG----HLREVGLTFHLLKDVPGLISKNIERSLEEAFKP 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 222 AGLSKNDVDFLIPHQANIRIVEAARQRLELPEEKMSTT---IRKYGNTSAASIpISIVEELEAGKIKDD--------DLI 290
Cdd:PLN03170 294 LGITDYNSIFWVAHPGGPAILDQVEAKVGLEKERMRATrhvLSEYGNMSSACV-LFILDEMRKRSAEDGqattgegfDWG 372
|
170
....*....|....*.
gi 502276033 291 IMVGFGGGLTWGAIAL 306
Cdd:PLN03170 373 VLFGFGPGLTVETVVL 388
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
58-143 |
9.85e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 37.40 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502276033 58 AAKKAIEDAKISPQDIDLILVATvTPDrAFPSVsCM----LQERLGAVKAAALDI-SAACAGFIYGMVTASQfIDNGAYR 132
Cdd:PRK08313 31 AIDRALADAGLTWDDIDAVVVGK-APD-FFEGV-MMpelfLADALGATGKPLIRVhTAGSVGGSTAVVAASL-VQSGVYR 106
|
90
....*....|.
gi 502276033 133 YILVVGAEKLS 143
Cdd:PRK08313 107 RVLAVAWEKQS 117
|
|
| |
