|
Name |
Accession |
Description |
Interval |
E-value |
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
3-335 |
5.86e-159 |
|
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: 447.25 E-value: 5.86e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 3 HSKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERRHIIRGEdTTTSMGVKAAKIAIERSGVAKEDIDFVVFAT 82
Cdd:COG0332 2 NVRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDE-TTSDLAVEAARKALEAAGIDPEDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 83 LSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTTRGrgVSVIFG 162
Cdd:COG0332 81 VTPDYLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRS--TCVLFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 163 DGAGAAVLSREEDlSKGILSTHLHSEGEHAEelALQAPGMGARWVTDIIADNDPndesyYPYMNGQFVFKNAVVRFAEVI 242
Cdd:COG0332 159 DGAGAVVLEASEE-GPGILGSVLGSDGSGAD--LLVVPAGGSRNPPSPVDEGDH-----YLRMDGREVFKFAVRNLPEVI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 243 NEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVLAAF 322
Cdd:COG0332 231 REALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGF 310
|
330
....*....|...
gi 2236732263 323 GSGFTWASAIIKW 335
Cdd:COG0332 311 GAGLTWGAAVLRW 323
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
1-335 |
4.59e-155 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 437.20 E-value: 4.59e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 1 MYHSKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERRhiIRGEDTTTS-MGVKAAKIAIERSGVAKEDIDFVV 79
Cdd:PRK09352 1 MMYAKILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERR--IAAPDETTSdLATEAAKKALEAAGIDPEDIDLII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 80 FATLSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTTRGrgVSV 159
Cdd:PRK09352 79 VATTTPDYAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRS--TCV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 160 IFGDGAGAAVLSREEDlsKGILSTHLHSEGEHAEELALQAPGMGARWVTDIIadndpndesyypYMNGQFVFKNAVVRFA 239
Cdd:PRK09352 157 LFGDGAGAVVLGASEE--PGILSTHLGSDGSYGDLLYLPGGGSRGPASPGYL------------RMEGREVFKFAVRELA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 240 EVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVL 319
Cdd:PRK09352 223 KVAREALEAAGLTPEDIDWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLL 302
|
330
....*....|....*.
gi 2236732263 320 AAFGSGFTWASAIIKW 335
Cdd:PRK09352 303 EGFGGGLTWGAALVRW 318
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
3-333 |
1.94e-142 |
|
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: 405.39 E-value: 1.94e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 3 HSKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERrHIIRGEDTTTSMGVKAAKIAIERSGVAKEDIDFVVFAT 82
Cdd:cd00830 1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRER-RIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIVAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 83 LSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTtrGRGVSVIFG 162
Cdd:cd00830 80 STPDYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWT--DRSTAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 163 DGAGAAVLSREEDlSKGILSTHLHSEGEHAEelALQAPGMGARWVTDIIADNDPndesyYPYMNGQFVFKNAVVRFAEVI 242
Cdd:cd00830 158 DGAGAVVLEATEE-DPGILDSVLGSDGSGAD--LLTIPAGGSRSPFEDAEGGDP-----YLVMDGREVFKFAVRLMPESI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 243 NEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVLAAF 322
Cdd:cd00830 230 EEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGF 309
|
330
....*....|.
gi 2236732263 323 GSGFTWASAII 333
Cdd:cd00830 310 GAGLTWGAALL 320
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-335 |
6.32e-127 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 366.11 E-value: 6.32e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 1 MYHSKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERRhiIRGEDTTTS-MGVKAAKIAIERSGVAKEDIDFVV 79
Cdd:PRK12879 2 MSYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERR--IAHVEEYTSdLAIKAAERALARAGLDAEDIDLII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 80 FATLSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTTRGrgVSV 159
Cdd:PRK12879 80 VATTTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVTDYTDRT--TCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 160 IFGDGAGAAVLSREEDlSKGILSTHLHSEGEHAEELALQAPGmgarwvTDIiaDNDPNDESYYPYMNGQFVFKNAVVRFA 239
Cdd:PRK12879 158 LFGDGAGAVVLEATEN-EPGFIDYVLGTDGDGGDILYRTGLG------TTM--DRDALSGDGYIVQNGREVFKWAVRTMP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 240 EVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVL 319
Cdd:PRK12879 229 KGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLL 308
|
330
....*....|....*.
gi 2236732263 320 AAFGSGFTWASAIIKW 335
Cdd:PRK12879 309 YGFGAGLTWAALLVKW 324
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
4-335 |
4.86e-124 |
|
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: 358.62 E-value: 4.86e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 4 SKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERRhiIRGEDTTTS-MGVKAAKIAIERSGVAKEDIDFVVFAT 82
Cdd:TIGR00747 3 AGILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERR--IAADDETSStMGFEAAKRAIENAGISKDDIDLIIVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 83 LSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTTRGrgVSVIFG 162
Cdd:TIGR00747 81 TTPDHAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRG--TCVLFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 163 DGAGAAVLSREEDLsKGILSTHLHSEGEHAEELALQAPGMGarwvtdiiadndPNDESYYPYMNGQFVFKNAVVRFAEVI 242
Cdd:TIGR00747 159 DGAGAVVLGESEDP-GGIISTHLGADGTQGEALYLPAGGRP------------TSGPSPFITMEGNEVFKHAVRKMGDVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 243 NEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVLAAF 322
Cdd:TIGR00747 226 EETLEANGLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAF 305
|
330
....*....|...
gi 2236732263 323 GSGFTWASAIIKW 335
Cdd:TIGR00747 306 GGGLTWGAALVRF 318
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
4-335 |
2.85e-102 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 305.51 E-value: 2.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 4 SKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIqERRHIIRGEDTTTSMGVKAAKIAIERSGVAKEDIDFVVFATL 83
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGI-RNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 84 SPDYYFpGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTTRGrgVSVIFGD 163
Cdd:PLN02326 127 SPDDLF-GSAPQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRG--TCILFGD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 164 GAGAAVLSREEDLSKGILSTHLHSEGEHAEELALQ---APGMGARWVTDIIADNDPNDESYYP-YMNGQFVFKNAVVRFA 239
Cdd:PLN02326 204 GAGAVVLQACDDDEDGLLGFDMHSDGNGHKHLHATfkgEDDDSSGGNTNGVGDFPPKKASYSCiQMNGKEVFKFAVRCVP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 240 EVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVL 319
Cdd:PLN02326 284 QVIESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKVKKGDVIAT 363
|
330
....*....|....*.
gi 2236732263 320 AAFGSGFTWASAIIKW 335
Cdd:PLN02326 364 AGFGAGLTWGSAIVRW 379
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
6-335 |
5.77e-73 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 228.68 E-value: 5.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 6 IAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERrHIIRGEDTTTSMGVKAAKIAIERSGVAKEDIDFVVFATLSP 85
Cdd:CHL00203 5 ILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKR-HLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATSTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 86 DYYFpGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTTRGrgVSVIFGDGA 165
Cdd:CHL00203 84 DDLF-GSASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRK--TCILFGDGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 166 GAAVLsrEEDLSKGILSTHLHSEGEHAEELAL-QAPGMGARWVTDIIadndPNDESYYPYMNGQFVFKNAVVRFAEVINE 244
Cdd:CHL00203 161 GAAII--GASYENSILGFKLCTDGKLNSHLQLmNKPVNNQSFGTTKL----PQGQYQSISMNGKEVYKFAVFQVPAVIIK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 245 GLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVLAAFGS 324
Cdd:CHL00203 235 CLNALNISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVLSGFGA 314
|
330
....*....|.
gi 2236732263 325 GFTWASAIIKW 335
Cdd:CHL00203 315 GLTWGAIVLKW 325
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
4-335 |
2.06e-68 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 216.90 E-value: 2.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 4 SKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERRHIIRGEdTTTSMGVKAAKIAIERSGVAKEDIDFVVFATL 83
Cdd:PRK05963 4 SRIAGFGHAVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDE-TLSDLAASAGDMALSDAGIERSDIALTLLATS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 84 SPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTgMYKNILVIGSEVHSTGLDMTTRGRgvSVIFGD 163
Cdd:PRK05963 83 TPDHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRA-QGKPVLVVAANILSRRINMAERAS--AVLFAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 164 GAGAAVLSREEDLSKGILSTHLHSEGEHAEELALQAPGMGARWVTDIIADndpndESYYPYMNGQFVFKNAVVRFAEVIN 243
Cdd:PRK05963 160 AAGAVVLAPSAKANSGVLGSQLISDGSHYDLIKIPAGGSARPFAPERDAS-----EFLMTMQDGRAVFTEAVRMMSGASQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 244 EGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVLAAFG 323
Cdd:PRK05963 235 NVLASAAMTPQDIDRFFPHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAG 314
|
330
....*....|..
gi 2236732263 324 SGFTWASAIIKW 335
Cdd:PRK05963 315 AGMTGGAVVMRV 326
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
6-333 |
4.11e-64 |
|
"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: 205.74 E-value: 4.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 6 IAGLGYYVPSNVVTNDDLSKIMdtNDEWIQERTGIQERRHIIRGEDTTTsMGVKAAKIAIERSGVAKEDIDFVVFATLSP 85
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEDVPT-MAVEAARRALERAGIDPDDIGLLIVATESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 86 DYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTTRGRgvsVIFGDGA 165
Cdd:cd00827 81 IDKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALE---PTLGDGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 166 GAAVLSREEDLSK-GILSTHLHSEGeHAEELALQAPGMGARWVTDIIADNDPNDEsyypyMNGQFVFKNAVVRFAEVINE 244
Cdd:cd00827 158 AAMLVSRNPGILAaGIVSTHSTSDP-GYDFSPYPVMDGGYPKPCKLAYAIRLTAE-----PAGRAVFEAAHKLIAKVVRK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 245 GLEANGLQvSDIDMLIPHQAN-LRISQFIQNKFKLTDDQV----HNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVL 319
Cdd:cd00827 232 ALDRAGLS-EDIDYFVPHQPNgKKILEAVAKKLGGPPEKAsqtrWILLRRVGNMYAASILLGLASLLESGKLKAGDRVLL 310
|
330
....*....|....
gi 2236732263 320 AAFGSGFTWASAII 333
Cdd:cd00827 311 FSYGSGFTAEAFVL 324
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
1-335 |
2.62e-58 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 191.20 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 1 MYHSKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERrHIIRGEdTTTSMGVKAAKIAIERSGVAKEDIDFVVF 80
Cdd:PRK07204 2 KRYISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTR-HFVDGE-TSSYMGAEAAKKAVEDAKLTLDDIDCIIC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 81 ATLSPDYYFPGPGVLVQRDLGLRTVG--ALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGL---DMTTrgr 155
Cdd:PRK07204 80 ASGTIQQAIPCTASLIQEQLGLQHSGipCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLnwgQNES--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 156 gvSVIFGDGAGAAVLSREEDLSKgILSTHL--HSEGEHAEELalQAPGMgarwvtdIIADNDPNDESYYPY---MNGQFV 230
Cdd:PRK07204 157 --CILFGDGAAAVVITKGDHSSR-ILASHMetYSSGAHLSEI--RGGGT-------MIHPREYSEERKEDFlfdMNGRAI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 231 FKNAVVRFAEVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGK 310
Cdd:PRK07204 225 FKLSSKYLMKFIDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKK 304
|
330 340
....*....|....*....|....*
gi 2236732263 311 IKSGDTVVLAAFGSGFTWASAIIKW 335
Cdd:PRK07204 305 VQRGNKILLLGTSAGLSIGGILLEY 329
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
246-335 |
2.44e-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: 144.18 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 246 LEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVLAAFGSG 325
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
|
90
....*....|
gi 2236732263 326 FTWASAIIKW 335
Cdd:pfam08541 81 LTWGAALLRW 90
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
3-335 |
1.66e-39 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 142.07 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 3 HSKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERrHIIRGEDTTTSMGVKAAKIAIERSGVAKEDIDFVVFAT 82
Cdd:PRK06840 4 NVGIVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEK-PVPGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVIYIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 83 lSP--DYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVA-DQYIKTGMYKNILVIGSEVHSTGLDMTTRGRGVSV 159
Cdd:PRK06840 83 -SEhkDYPVWSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAkDLLYSDPSIENVLLVGGYRNSDLVDYDNPRTRFMF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 160 IFGDGAGAAVLSREEDLSKgILSTHLHSEGEHAEELALqaPGMGARWVtdiiADNDPNDESYYPYMNGQFV-FKN----- 233
Cdd:PRK06840 162 NFAAGGSAALLKKDAGKNR-ILGSAIITDGSFSEDVRV--PAGGTKQP----ASPETVENRQHYLDVIDPEsMKErldev 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 234 AVVRFAEVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQvHNNIQKYGNTTAASIPIALTEAWEQGKIKS 313
Cdd:PRK06840 235 SIPNFLKVIREALRKSGYTPKDIDYLAILHMKRSAHIALLEGLGLTEEQ-AIYLDEYGHLGQLDQILSLHLALEQGKLKD 313
|
330 340
....*....|....*....|..
gi 2236732263 314 GDTVVLAAFGSGFTWASAIIKW 335
Cdd:PRK06840 314 GDLVVLVSAGTGYTWAATVIRW 335
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
4-335 |
4.31e-36 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 133.55 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 4 SKIAGLGYYVPSNVVTNDDLSKIMDTNDEWIQER----TGIQERrhIIRGEDTTTS-MGVKAAKIAIERSGVAKEDIDFV 78
Cdd:PRK12880 8 AKISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTR--YICDENTCVSdLGKHAANTLLQGLNIDKNSLDAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 79 VFATLSPDYYFPGPGVLVQRDLGL--RTVgALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTgldMTTRGRG 156
Cdd:PRK12880 86 IVVTQSPDFFMPSTACYLHQLLNLssKTI-AFDLGQACAGYLYGLFVAHSLIQSGLGKILLICGDTLSKF---IHPKNMN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 157 VSVIFGDGAGAAVLSREEdlsKGILSTHLHSEGEHAEELALQAPGMGarwvtdIIADNDPNDESYYP----------YMN 226
Cdd:PRK12880 162 LAPIFGDGVSATLIEKTD---FNEAFFELGSDGKYFDKLIIPKGAMR------IPKADIFNDDSLMQteefrqlenlYMD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 227 GQFVFKNAVVRFAEVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNI-QKYGNTTAASIPIALTEA 305
Cdd:PRK12880 233 GANIFNMALECEPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEELKLNDDKVPNFImEKYANLSACSLPALLCEL 312
|
330 340 350
....*....|....*....|....*....|
gi 2236732263 306 WEQGKIKSgdtvVLAAFGSGFTWASAIIKW 335
Cdd:PRK12880 313 DTPKEFKA----SLSAFGAGLSWGSAVLNF 338
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
6-334 |
7.34e-34 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 127.69 E-value: 7.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 6 IAGLGYYVPSNVVTNDDLSKIMDT------------------------NDEWIQERTGIqERRHII-------------- 47
Cdd:PRK07515 5 ISGTGLYTPPESISNEELVASFNAyverfnaenaaaiaagevealqpsSSEFIEKASGI-KSRYVMdkegildpdrmrpr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 48 ---RGED---TTTSMGVKAAKIAIERSGVAKEDIDFVVFATLSPDYYFPGPGVLVQRDLGLRtvG-ALDVRNQCSGFVYA 120
Cdd:PRK07515 84 ipeRSNDelsIQAEMGVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIE--GfAFDMNVACSSATFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 121 ISVADQYIKTGMYKNILVIGSEVHSTGLDMttRGRGVSVIFGDGAGAAVLSREEDLSKG----ILSTHLHSEgehaeela 196
Cdd:PRK07515 162 IQTAANAIRSGSARRVLVVNPEICSGHLNF--RDRDSHFIFGDVATAVIVERADTATSAggfeILGTRLFTQ-------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 197 lqapgmgarWVTDI---------IADNDPNDESYYPYMNGQFVFKNAVVRFAEVINEGLEANGLQVSDIDMLIPHQANLR 267
Cdd:PRK07515 232 ---------FSNNIrnnfgflnrADPEGIGARDKLFVQEGRKVFKEVCPMVAEHIVEHLAENGLTPADVKRFWLHQANIN 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 268 ISQFIQNKF---KLTDDQVHNNIQKYGNTTAASIPIALTEAweQGKIKSGDTVVLAAFGSGFTWASAIIK 334
Cdd:PRK07515 303 MNQLIGKKVlgrDATPEEAPVILDEYANTSSAGSIIAFHKH--SDDLAAGDLGVICSFGAGYSIGSVIVR 370
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
52-333 |
1.06e-31 |
|
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: 119.47 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 52 TTTSMGVKAAKIAIERSGVAKEDIDFVVFATLSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTG 131
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 132 MYKNILVIGSEVhstgldmttrgrgvsVIFGDGAGAAVLSREEDLSK-------GILSTHLHSEGEHAEELalqapgmga 204
Cdd:cd00327 86 KADIVLAGGSEE---------------FVFGDGAAAAVVESEEHALRrgahpqaEIVSTAATFDGASMVPA--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 205 rwvtdiiadndpndesyyPYMNGQfvfknavvrfAEVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVH 284
Cdd:cd00327 142 ------------------VSGEGL----------ARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVR 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2236732263 285 NN-----IQKYGNTTAASIPIALTEAWEQGKIKSG-------DTVVLAAFGSGFTWASAII 333
Cdd:cd00327 194 SPavsatLIMTGHPLGAAGLAILDELLLMLEHEFIpptprepRTVLLLGFGLGGTNAAVVL 254
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
108-189 |
8.22e-30 |
|
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: 108.76 E-value: 8.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 108 LDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTtrGRGVSVIFGDGAGAAVLSREEDLSKGILSTHLHS 187
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWT--DRSTAVLFGDGAGAVVLEATDEPGARILDSVLGS 78
|
..
gi 2236732263 188 EG 189
Cdd:pfam08545 79 DG 80
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-335 |
3.62e-27 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 108.81 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 1 MYHSK--IAGLGYYVPSNVVTNDDL-SKIMDTNDEW------IQERTGIQERRhiIRGEDTTTSMG-VKAAKIAIERSGV 70
Cdd:PRK09258 1 MKYSNvaILSLAYELAPVVVTSSEIeERLAPLYERLrlppgqLEALTGIRERR--WWPEGTQLSDGaIAAGRKALAEAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 71 AKEDIDFVVFATLSPDYYFPGPGVLVQRDLGL-RTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSE-----VH 144
Cdd:PRK09258 79 DPSDIGLLINTSVCRDYLEPATACRVHHNLGLpKSCANFDVSNACLGFLNGMLDAANMIELGQIDYALVVSGEsareiVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 145 STGLDMTTRGRGV--------SVIFGDGAGAAVLSREEDLSKG--ILSTHLHSEGEHAEELALQAPGMgarwVTDIIAdn 214
Cdd:PRK09258 159 ATIDRLLAPETTRedfaqsfaTLTLGSGAAAAVLTRGSLHPRGhrLLGGVTRAATEHHELCQGGRDGM----RTDAVG-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 215 dpndesyypymngqfVFKNAVVRFAEVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNIQKYGNTT 294
Cdd:PRK09258 233 ---------------LLKEGVELAVDTWEAFLAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMG 297
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2236732263 295 AASIPIALTEAWEQGKIKSGDTVVLAAFGSGFTWASAIIKW 335
Cdd:PRK09258 298 PASLPITLAMAAEEGFLKPGDRVALLGIGSGLNCSMLEVKW 338
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
4-335 |
4.98e-26 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 105.99 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 4 SKIAGLGYYVPSNVVTNDD----LSKIMDTNDEW------IQERTGIqERRHII-----RGEDTTTS------------M 56
Cdd:COG3424 2 ARILSIATAVPPHRYTQEEiaefAAELFGLDERDrrrlrrLFENSGI-ETRHSVlplewYLEPPSFGernalyieealeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 57 GVKAAKIAIERSGVAKEDIDFVVFATlSPDYYFPGPGVLVQRDLGLRTvgalDVRNQ------CSGFVYAISVADQYIKT 130
Cdd:COG3424 81 AEEAARRALDKAGLDPEDIDHLVTVS-CTGFAAPGLDARLINRLGLRP----DVRRLpvggmgCAAGAAGLRRAADFLRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 131 GMYKNILVIGSEVHSTGLDMTTRGRG---VSVIFGDGAGAAVLSREEDLSKGI----LSTHLHSEGEHAeelalqapgMG 203
Cdd:COG3424 156 DPDAVVLVVCVELCSLTFQRDDDSKDnlvANALFGDGAAAVVVSGDPRPGPGPrilaFRSYLIPDTEDV---------MG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 204 arW-VTDiiadndpndesyypymNG-QFVFKNAV---VR--FAEVINEGLEANGLQVSDIDMLIPHQANLRISQFIQNKF 276
Cdd:COG3424 227 --WdVGD----------------TGfRMVLSPEVpdlIAehLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEAL 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2236732263 277 KLTDDQV---HNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVLAAFGSGFTWASAIIKW 335
Cdd:COG3424 289 GLPPEALahsREVLREYGNMSSATVLFVLERLLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
6-325 |
2.79e-25 |
|
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: 104.49 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 6 IAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERRHIIRGEDTTTsMGVKAAKIAIERSGVAKEDIDFVVFATLS- 84
Cdd:COG3425 5 IDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVT-MAANAARRALDRAGIDPSDIGAVYVGTESg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 85 PDYYFPGpGVLVQRDLGL-RTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEV----HSTGLDMTtrgrgvsv 159
Cdd:COG3425 84 PDASKPI-ATYVHGALGLpPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIarygPGSAGEYT-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 160 iFGDGAGAAVLSREEDLskgilsthlhsegehaeeLALqAPGMGArWVTDIiadND---PNDESyYPYMNGQFV----FK 232
Cdd:COG3425 155 -QGAGAVAMLVGADPRI------------------AEI-EGGSGS-YTTDV---MDfwrPNGSD-YPLVDGRFSepayLD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 233 navvRFAEVINEGLEANGLQVSDIDMLIPHQAN------------LRISQFIQNKFKltdDQVHNNI---QKYGNTTAAS 297
Cdd:COG3425 210 ----HLEEAVKDYKEKTGLKPDDFDYFVFHQPFgkmpkkaakklgRKAGREIQEDFE---EQVEPSLiysRRIGNTYTGS 282
|
330 340
....*....|....*....|....*...
gi 2236732263 298 IPIALTEAWEQGKIKSGDTVVLAAFGSG 325
Cdd:COG3425 283 LYLGLASLLDNAKDLPGDRIGLFSYGSG 310
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
54-333 |
9.07e-23 |
|
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: 96.94 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 54 TSMGVKAAKIAIERSGVAKED----IDFVVFATLSPDY---------------------YFPGPGVLVQRDLGLRtVGAL 108
Cdd:cd00825 12 SILGFEAAERAIADAGLSREYqknpIVGVVVGTGGGSPrfqvfgadamravgpyvvtkaMFPGASGQIATPLGIH-GPAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 109 DVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEV---------HSTGLDMTTRG-------RGVSVIFGDGAGAAVLSR 172
Cdd:cd00825 91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEElaapmdcefDAMGALSTPEKasrtfdaAADGFVFGDGAGALVVEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 173 EEDLSK-------GILSTHLHSEGEHAEELALQAPGMgarwvtdiiadndpndesyypymngqfvfknavvrfAEVINEG 245
Cdd:cd00825 171 LEHALArgahiyaEIVGTAATIDGAGMGAFAPSAEGL------------------------------------ARAAKEA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 246 LEANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNN-----IQKYGNTTAASIPIALTEAWEQGKIKS------- 313
Cdd:cd00825 215 LAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDKSPavsatKAMTGNLSSAAVVLAVDEAVLMLEHGFippsihi 294
|
330 340 350
....*....|....*....|....*....|....*...
gi 2236732263 314 ------------------GDTVVLAAFGSGFTWASAII 333
Cdd:cd00825 295 eeldeaglnivtettpreLRTALLNGFGLGGTNATLVL 332
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
3-327 |
8.51e-22 |
|
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: 94.60 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 3 HSKIAGLGYYVPSNVVTNDDLS-----KIMDTNDE-------WIQERTGIQERRHII-RGEDTTTS-------------- 55
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVdfyrrLFSSDHLPelkeklkRLCAKTGIETRYLVLpGGEETYAPrpemspslderndi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 56 -------MGVKAAKIAIERSGVAKEDIDFVVFATlSPDYYFPGPGVLVQRDLGLRTvgalDVR----NQ--CSGFVYAIS 122
Cdd:cd00831 81 aleeareLAEEAARGALDEAGLRPSDIDHLVVNT-STGNPTPSLDAMLINRLGLRP----DVKrynlGGmgCSAGAIALD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 123 VADQYIKTGMYKNILVIGSEVHSTGLDMT-TRGRGVS-VIFGDGAGAAVLSREEDLSKG------ILSTHLHSEGEHAEE 194
Cdd:cd00831 156 LAKDLLEANPGARVLVVSTELCSLWYRGPdHRSMLVGnALFGDGAAAVLLSNDPRDRRRerplfeLVRAASTLLPDSEDA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 195 LALQAPGMGARWVTDIiadndpndesYYPYMNGQFVFKNAVVRFAEVInegleaNGLQVSDIDMLIPHQANLRISQFIQN 274
Cdd:cd00831 236 MGWHLGEEGLTFVLSR----------DVPRLVEKNLERVLRKLLARLG------IGLFKLAFDHWCVHPGGRAVLDAVEK 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2236732263 275 KFKLTDDQVH---NNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVLAAFGSGFT 327
Cdd:cd00831 300 ALGLSPEDLEasrMVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFT 355
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
6-319 |
1.48e-16 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 79.57 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 6 IAGLGYYVPSNVVTNDD----LSKIMDTNdewiqERT--------GIQERRHIIRGEDTTT----SMGVKAAKIAIERSG 69
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEmeayLGLINGKP-----SRArriilrnnGIKTRHYALDPEGRPThsnaQMAAEAIRDLLDDAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 70 VAKEDIDFVVFATLSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGL- 148
Cdd:PRK06816 80 FSLGDIELLACGTSQPDQLMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVATASELASRWFr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 149 ---------DMTTRGRGVSVIF---------GDGAGAAVLS---REEDLSKGILSTHLHSegeHAEELalqAPGM--GAr 205
Cdd:PRK06816 160 asrfeaeeeKLAELEENPEIAFekdflrwmlSDGAGAVLLEnkpRPDGLSLRIDWIDLRS---YAGEL---PVCMyaGA- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 206 wvtDIIADNDPNDESYYP----YMNGQFVFK--------NAVVRFAEVINEGLEANGLQVSDIDMLIPH--QANLR---I 268
Cdd:PRK06816 233 ---EKNEDGSLKGWSDYPpeeaEAASALSLKqdvrllneNIVVYTIKPLLELVDKRNLDPDDIDYFLPHysSEYFRekiV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2236732263 269 SQFIQNKFKLTDDQVHNNIQKYGNTTAASIPIALTEAWEQGKIKSGDTVVL 319
Cdd:PRK06816 310 ELLAKAGFMIPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPGQKILC 360
|
|
| PRK04262 |
PRK04262 |
hypothetical protein; Provisional |
6-325 |
9.76e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 235266 [Multi-domain] Cd Length: 347 Bit Score: 71.09 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 6 IAGLGYYVPSNVVTNDDLSKIMDTNDEWIQERTGIQERRHIIRGEDTTTsMGVKAAKIAIERSGVAKEDIDFVVFATLSP 85
Cdd:PRK04262 5 IVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTAT-IAVEAARNALKRAGIDPKEIGAVYVGSESH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 86 DYYFPGPGVLVQRDLGL-RTVGALDVRNQCSGFVYAISVADQYIKTGMYKNILVIGSEvhstgldmTTRGR-GVSVIFGD 163
Cdd:PRK04262 84 PYAVKPTATIVAEALGAtPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGAD--------TAQGApGDALEYTA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 164 GAGAA--VLSREEDLskgilsthlhSEGEHAeelalqapgmgARWVTDiIADNDPNDESYYPYMNGQFVFKNAVvrFAEV 241
Cdd:PRK04262 156 AAGGAafIIGKEEVI----------AEIEAT-----------YSYTTD-TPDFWRREGEPYPRHGGRFTGEPAY--FKHI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 242 IN--EGL-EANGLQVSDIDMLIPHQANLRISQFIQNKFKLTDDQVHNNI--QKYGNTTAASIPIALTEAWEQGkiKSGDT 316
Cdd:PRK04262 212 ISaaKGLmEKLGLKPSDYDYAVFHQPNGKFPLRVAKMLGFTKEQVKPGLltPYIGNTYSGSALLGLAAVLDVA--KPGDR 289
|
....*....
gi 2236732263 317 VVLAAFGSG 325
Cdd:PRK04262 290 ILVVSFGSG 298
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
39-147 |
1.60e-10 |
|
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: 61.51 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 39 GIQERRHIIRGEDTTTSMGVKAAKIAIERSGVAKEDIDFVVFATLSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFV 118
Cdd:cd00829 2 GVGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPATRVEAAGASGS 81
|
90 100
....*....|....*....|....*....
gi 2236732263 119 YAISVADQYIKTGMYKNILVIGSEVHSTG 147
Cdd:cd00829 82 AAVRAAAAAIASGLADVVLVVGAEKMSDV 110
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
50-199 |
2.87e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 48.40 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 50 EDTTTSMGVKAAKIAIERSGVAKEDIDFVVFAT----LSPDYyFPGPGVLvQRDLGLRTVGALDVRNQCSGFVYAISVAD 125
Cdd:PRK07516 19 AETLESLIVRVAREALAHAGIAAGDVDGIFLGHfnagFSPQD-FPASLVL-QADPALRFKPATRVENACATGSAAVYAAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 126 QYIKTGMYKNILVIGSEvhstglDMT-TRGRGVSVIFgdgAGAAVLSREEDLSKG-------ILSTHLHSEGEHAEELAL 197
Cdd:PRK07516 97 DAIEAGRARIVLVVGAE------KMTaTPTAEVGDIL---LGASYLKEEGDTPGGfagvfgrIAQAYFQRYGDQSDALAM 167
|
..
gi 2236732263 198 QA 199
Cdd:PRK07516 168 IA 169
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
56-196 |
6.07e-06 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 47.47 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 56 MGVKAAKIAIERSGVAKEDIDFVVFATLSPdyyfPGPGVLVQRDLGLR-----TVGALDVRNQC-SGFVyAISVADQYIK 129
Cdd:cd00751 25 LGAAVIKALLERAGLDPEEVDDVIMGNVLQ----AGEGQNPARQAALLaglpeSVPATTVNRVCgSGLQ-AVALAAQSIA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2236732263 130 TGMYKNILVIGSEVHSTGLDMTTRGRGVSVIFGDGAGAAVLSREEDLSKGIlsthlhSEGEHAEELA 196
Cdd:cd00751 100 AGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGL------SMGITAENVA 160
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
23-170 |
9.30e-06 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 47.00 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 23 LSK-IMDTNDEWIQERTGIQERRHIIRGEdTTTSMGVKAAKIAIERSGVAKEDIDFVVFATlSPDYYFPGPGVLVQRDLG 101
Cdd:PLN03169 76 MSKeILDKYPELATEGTPTIKQRLDIANE-AVTQMAVEASLACIKEWGRPVSDITHLVYVS-SSEARLPGGDLYLAKQLG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 102 LRTvgalDVRN------QCSGFVYAISVADQYIKTGMYKNILVIGSEVHSTGLDMTTRGR-----GVSvIFGDGAGAAVL 170
Cdd:PLN03169 154 LSP----DVQRvmlyflGCSGGVAGLRVAKDIAENNPGSRVLLTTSETTILGFRPPSPDRpydlvGAA-LFGDGAAAVII 228
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
263-334 |
1.88e-04 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 43.02 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2236732263 263 QANLRISQFIQNKFKLTddqvhnnIQKYGNTTAASI--PIALTEAweQGKIKSGDTVVLAAFGSGFTWASAIIK 334
Cdd:PLN02854 428 QKNLQLSDWHMEPSRMT-------LHRFGNTSSSSLwyELAYTEA--KGRVSAGDRVWQIAFGSGFKCNSAVWK 492
|
|
| PLN02192 |
PLN02192 |
3-ketoacyl-CoA synthase |
272-334 |
7.44e-04 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215123 Cd Length: 511 Bit Score: 41.11 E-value: 7.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2236732263 272 IQNKFKLTD---DQVHNNIQKYGNTTAASI--PIALTEAweQGKIKSGDTVVLAAFGSGFTWASAIIK 334
Cdd:PLN02192 415 LEKNLQLSDwhmEPSRMTLYRFGNTSSSSLwyELAYSEA--KGRIKKGDRTWQIAFGSGFKCNSAVWK 480
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
56-170 |
1.07e-03 |
|
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.
Pssm-ID: 395142 Cd Length: 225 Bit Score: 39.84 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 56 MGVKAAKIAIERSGVAKEDIDFVVFATLSpDYYFPGPGVLVQRDLGLR-TVGALDVRNQ-CSGFVYAISVADQYIKTGMY 133
Cdd:pfam00195 102 LGAEAALKAIKEWGQPKSKITHLVFCTTS-GVRMPGADYQLAKLLGLRpSVKRVMLYFQgCYGGATVLRTAKDIAENNPG 180
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2236732263 134 KNILVIGSEVHSTGLDMTTRGRGVSVI----FGDGAGAAVL 170
Cdd:pfam00195 181 ARVLVVCSEITVLGFRGPSKDRLDSLVgaalFGDGAAAVII 221
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
56-196 |
1.11e-03 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 40.43 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 56 MGVKAAKIAIERSGVAKEDIDFVVFATLSPDYYFPGPGVLVQRDLGL-RTVGALDVRNQC-SGFvYAISVADQYIKTGMY 133
Cdd:COG0183 29 LGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLpESVPAVTVNRVCgSGL-QAVALAAQAIAAGDA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2236732263 134 KNILVIGSEVHST---GLDMTTRGRGVSVIFGDGAGAAVLsreEDLSKGIlsthlhSEGEHAEELA 196
Cdd:COG0183 108 DVVIAGGVESMSRapmLLPKARWGYRMNAKLVDPMINPGL---TDPYTGL------SMGETAENVA 164
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
58-142 |
1.61e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 39.88 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 58 VKAAKIAIERSGVAKEDIDFVVFATLSPDYYF--PGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQYIKTGMYKN 135
Cdd:PRK06064 27 VEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVsqEHIAALIADYAGLAPIPATRVEAACASGGAALRQAYLAVASGEADV 106
|
....*..
gi 2236732263 136 ILVIGSE 142
Cdd:PRK06064 107 VLAAGVE 113
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
48-156 |
2.65e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 39.44 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 48 RGEDTTTSMGVKAAKIAIERSGVAKEDIDFVVFATLSPDYYFPGPGVLVQRDLGLRTVGALDVRNQCSGFVYAISVADQY 127
Cdd:PRK12578 16 RDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLRVEAMCATGLAASLTAYTA 95
|
90 100 110
....*....|....*....|....*....|...
gi 2236732263 128 IKTGMYKNILVIGSEvHSTGLDMTTR----GRG 156
Cdd:PRK12578 96 VASGLVDMAIAVGVD-KMTEVDTSTSlaigGRG 127
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
57-131 |
6.21e-03 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 38.21 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2236732263 57 GVKAAKIAIERSGVAKEDIDFVVF-----AtlspdyyfpGPGVLVQRDLGLR-----TVGALDVRNQC-SGFvYAISVAD 125
Cdd:PRK05790 30 GAIVIKAALERAGVPPEQVDEVIMgqvlqA---------GAGQNPARQAALKaglpvEVPALTINKVCgSGL-KAVALAA 99
|
....*.
gi 2236732263 126 QYIKTG 131
Cdd:PRK05790 100 QAIRAG 105
|
|
| |
