|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
7-437 |
1.44e-141 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 438.15 E-value: 1.44e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 7 SNKIAIVGMAVKFPGANDLDEYWDLLKFGKEAVTKFSEE--QLHRSGISEQLIANPNYKPYRGILDDLESFDTAPFENTT 84
Cdd:COG3321 3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADrwDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 85 KNFELLGVQGKVMSHLTHRAL-------STMRSQehhsnnyikNTAVYIGANNQPAAHFLGAAYyQSIDTQKAIERYYSk 157
Cdd:COG3321 83 REAEAMDPQQRLLLEVAWEALedagydpESLAGS---------RTGVFVGASSNDYALLLLADP-EAIDAYALTGNAKS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 158 VIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDGHCHSFDAS 237
Cdd:COG3321 152 VLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 238 ACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSkeGFMAPGVHGQYTCLQSAWRNAEVEPDDLDYIAAH 317
Cdd:COG3321 232 ADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN--GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 318 GSSTKLGDATEIYALKKAF-KDVKKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFMLEDS 396
Cdd:COG3321 310 GTGTPLGDPIEAAALTAAFgQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 499250115 397 PIYIATEFQDFPTVKKHYLAGVSSYGAGGSNTHLVLRSYDE 437
Cdd:COG3321 390 PFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPA 430
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
8-432 |
6.72e-138 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 401.55 E-value: 6.72e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 8 NKIAIVGMAVKFPGANDLDEYWDLLKFGKEAVTKFSEEQL-HRSGISEQLIANPNYKPYRGILDDLESFDTAPFENTTKN 86
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWdADGYYPDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 87 FELLGVQGKVMSHLTHRALstmrsqEH----HSNNYIKNTAVYIGANN-----QPAAHFLGAAYYQSIDTQKAIeryysk 157
Cdd:cd00833 81 AEAMDPQQRLLLEVAWEAL------EDagysPESLAGSRTGVFVGASSsdyleLLARDPDEIDAYAATGTSRAF------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 158 vIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDGHCHSFDAS 237
Cdd:cd00833 149 -LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 238 ACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSkeGFMAPGVHGQYTCLQSAWRNAEVEPDDLDYIAAH 317
Cdd:cd00833 228 ADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTK--GITAPSGEAQAALIRRAYARAGVDPSDIDYVEAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 318 GSSTKLGDATEIYALKKAFKDVK-KTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFMLEDS 396
Cdd:cd00833 306 GTGTPLGDPIEVEALAKVFGGSRsADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEES 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 499250115 397 PIYIATEFQDFPTVKKHYLAGVSSYGAGGSNTHLVL 432
Cdd:cd00833 386 PLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
10-432 |
1.51e-92 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 281.52 E-value: 1.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 10 IAIVGMAVKFPGANDLDEYWDLLKFGkeavtkfseeqlhrsgiseqlianpnykpyrgiLDDLESFDTAPFENTTKNFEL 89
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAG---------------------------------LDDVDLFDAAFFGISPREAEA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 90 LGVQGKVMSHLTHRAL-------STMRSQehhsnnyikNTAVYIGANNQpaahflgaayyqsidtqkaierYYSkviapy 162
Cdd:smart00825 48 MDPQQRLLLEVAWEALedagidpESLRGS---------RTGVFVGVSSS----------------------DYS------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 163 isyqfgfqgSSIDlyTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDGHCHSFDASACGTL 242
Cdd:smart00825 91 ---------VTVD--TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYV 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 243 YSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSkeGFMAPGVHGQytclqsawrnaevepddldyiaahgsstk 322
Cdd:smart00825 160 RGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSN--GITAPSGPAQ----------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 323 lgdateiyalkkafkdvkktyrCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFMLEDSPIYIAT 402
Cdd:smart00825 209 ----------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPT 266
|
410 420 430
....*....|....*....|....*....|
gi 499250115 403 EFQDFPTVKKHYLAGVSSYGAGGSNTHLVL 432
Cdd:smart00825 267 ELTPWPPPGRPRRAGVSSFGFGGTNAHVIL 296
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
8-258 |
1.95e-44 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 155.49 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 8 NKIAIVGMAVKFPGANDLDEYWDLLKFGKEAVTKFSEEQLHRSG--ISEQLIANPNYKPYrGILDDLESFDtAPFENTTK 85
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKlyDPPSRIAGKIYTKW-GGLDDIFDFD-PLFFGISP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 86 N-------FELLGVQgkVMSHLTHRALSTMRSQEHhsnnyiKNTAVYIGANNQpaahflGAAYYQSIDTQKAIERYYSK- 157
Cdd:pfam00109 79 ReaermdpQQRLLLE--AAWEALEDAGITPDSLDG------SRTGVFIGSGIG------DYAALLLLDEDGGPRRGSPFa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 158 ------VIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDGHC 231
Cdd:pfam00109 145 vgtmpsVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPC 224
|
250 260
....*....|....*....|....*..
gi 499250115 232 HSFDASACGTLYSNGAGLVVLKRLEDA 258
Cdd:pfam00109 225 KAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
10-435 |
6.49e-44 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 164.79 E-value: 6.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 10 IAIVGMAVKFPGANDLDEYWDLLKFGKEAVT-----KFSEEQLHRSGISEqliANPNYKPYRGILDDLEsFDTAPFENTT 84
Cdd:TIGR02813 9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITdvpsdHWAKDDYYDSDKSE---ADKSYCKRGGFLPEVD-FNPMEFGLPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 85 KNFELLGVQGKVMSHLTHRALSTMRSQEHHSNNYIKNTaVYIGANnQPAAHFLGAAYYQSI-------------DTQKAI 151
Cdd:TIGR02813 85 NILELTDISQLLSLVVAKEVLNDAGLPDGYDRDKIGIT-LGVGGG-QKQSSSLNARLQYPVlkkvfkasgvedeDSEMLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 152 ERYYSK---------------VIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVG 216
Cdd:TIGR02813 163 KKFQDQyihweensfpgslgnVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 217 YLYEENGLFSSDGHCHSFDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSskEGFMAPGVHGQYTC 296
Cdd:TIGR02813 243 MSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKF--KSIYAPRPEGQAKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 297 LQSAWRNAEVEPDDLDYIAAHGSSTKLGDATEIYALKKAF-KDVKKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKN 375
Cdd:TIGR02813 321 LKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFsQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHH 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499250115 376 KAIVPSINFETPNPDFMLEDSPIYIATEFQdfPTVKKH----YLAGVSSYGAGGSNTHLVLRSY 435
Cdd:TIGR02813 401 KVLPPTINVDQPNPKLDIENSPFYLNTETR--PWMQREdgtpRRAGISSFGFGGTNFHMVLEEY 462
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
163-434 |
8.68e-28 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 113.97 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 163 ISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDL-PQEVGYLYEENGL----FSSDGH--CHSFD 235
Cdd:PRK07103 150 CSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLsYWECQALRSLGAMgsdrFADEPEaaCRPFD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 236 ASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKEgfmaPGVHGQYTCLQSAWRNAEVEPDDLDYIA 315
Cdd:PRK07103 230 QDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPD----PSLEGEMRVIRAALRRAGLGPEDIDYVN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 316 AHGSSTKLGDATEIYALKKAfkdvkKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPnpdfmled 395
Cdd:PRK07103 306 PHGTGSPLGDETELAALFAS-----GLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEP-------- 372
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499250115 396 spiyIATEFQdF--PTVKKHYL--AGVSSYGAGGSNTHLVLRS 434
Cdd:PRK07103 373 ----IDERFR-WvgSTAESARIryALSLSFGFGGINTALVLER 410
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
7-437 |
1.44e-141 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 438.15 E-value: 1.44e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 7 SNKIAIVGMAVKFPGANDLDEYWDLLKFGKEAVTKFSEE--QLHRSGISEQLIANPNYKPYRGILDDLESFDTAPFENTT 84
Cdd:COG3321 3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADrwDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGISP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 85 KNFELLGVQGKVMSHLTHRAL-------STMRSQehhsnnyikNTAVYIGANNQPAAHFLGAAYyQSIDTQKAIERYYSk 157
Cdd:COG3321 83 REAEAMDPQQRLLLEVAWEALedagydpESLAGS---------RTGVFVGASSNDYALLLLADP-EAIDAYALTGNAKS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 158 VIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDGHCHSFDAS 237
Cdd:COG3321 152 VLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 238 ACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSkeGFMAPGVHGQYTCLQSAWRNAEVEPDDLDYIAAH 317
Cdd:COG3321 232 ADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN--GLTAPNGPAQAAVIRRALADAGVDPATVDYVEAH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 318 GSSTKLGDATEIYALKKAF-KDVKKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFMLEDS 396
Cdd:COG3321 310 GTGTPLGDPIEAAALTAAFgQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 499250115 397 PIYIATEFQDFPTVKKHYLAGVSSYGAGGSNTHLVLRSYDE 437
Cdd:COG3321 390 PFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPA 430
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
8-432 |
6.72e-138 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 401.55 E-value: 6.72e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 8 NKIAIVGMAVKFPGANDLDEYWDLLKFGKEAVTKFSEEQL-HRSGISEQLIANPNYKPYRGILDDLESFDTAPFENTTKN 86
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWdADGYYPDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 87 FELLGVQGKVMSHLTHRALstmrsqEH----HSNNYIKNTAVYIGANN-----QPAAHFLGAAYYQSIDTQKAIeryysk 157
Cdd:cd00833 81 AEAMDPQQRLLLEVAWEAL------EDagysPESLAGSRTGVFVGASSsdyleLLARDPDEIDAYAATGTSRAF------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 158 vIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDGHCHSFDAS 237
Cdd:cd00833 149 -LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 238 ACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSkeGFMAPGVHGQYTCLQSAWRNAEVEPDDLDYIAAH 317
Cdd:cd00833 228 ADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTK--GITAPSGEAQAALIRRAYARAGVDPSDIDYVEAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 318 GSSTKLGDATEIYALKKAFKDVK-KTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFMLEDS 396
Cdd:cd00833 306 GTGTPLGDPIEVEALAKVFGGSRsADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEES 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 499250115 397 PIYIATEFQDFPTVKKHYLAGVSSYGAGGSNTHLVL 432
Cdd:cd00833 386 PLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
10-432 |
1.51e-92 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 281.52 E-value: 1.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 10 IAIVGMAVKFPGANDLDEYWDLLKFGkeavtkfseeqlhrsgiseqlianpnykpyrgiLDDLESFDTAPFENTTKNFEL 89
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAG---------------------------------LDDVDLFDAAFFGISPREAEA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 90 LGVQGKVMSHLTHRAL-------STMRSQehhsnnyikNTAVYIGANNQpaahflgaayyqsidtqkaierYYSkviapy 162
Cdd:smart00825 48 MDPQQRLLLEVAWEALedagidpESLRGS---------RTGVFVGVSSS----------------------DYS------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 163 isyqfgfqgSSIDlyTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDGHCHSFDASACGTL 242
Cdd:smart00825 91 ---------VTVD--TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYV 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 243 YSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSkeGFMAPGVHGQytclqsawrnaevepddldyiaahgsstk 322
Cdd:smart00825 160 RGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSN--GITAPSGPAQ----------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 323 lgdateiyalkkafkdvkktyrCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFMLEDSPIYIAT 402
Cdd:smart00825 209 ----------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPT 266
|
410 420 430
....*....|....*....|....*....|
gi 499250115 403 EFQDFPTVKKHYLAGVSSYGAGGSNTHLVL 432
Cdd:smart00825 267 ELTPWPPPGRPRRAGVSSFGFGGTNAHVIL 296
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
94-432 |
4.43e-47 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 164.73 E-value: 4.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 94 GKVMSHL----THRALSTMRSQEHHSNNYIknTAVYIGA-NNQPAAHFLGAAYYQSIDTQKAIERYYSKViAPYISYQFG 168
Cdd:cd00825 8 GSYVSILgfeaAERAIADAGLSREYQKNPI--VGVVVGTgGGSPRFQVFGADAMRAVGPYVVTKAMFPGA-SGQIATPLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 169 FQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGAC-----LIDLPQEVGYlyeenGLFSSDGHCHSFDASACGTLY 243
Cdd:cd00825 85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSeelaaPMDCEFDAMG-----ALSTPEKASRTFDAAADGFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 244 SNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSskEGFMAPGVHGQYTCLQSAWRNAEVEPDDLDYIAAHGSSTKL 323
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAG--MGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 324 GDATEIYALKKAFKDvkktYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFMLedspiyIATE 403
Cdd:cd00825 238 GDVKELKLLRSEFGD----KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLN------IVTE 307
|
330 340
....*....|....*....|....*....
gi 499250115 404 FQDFPTvkkhYLAGVSSYGAGGSNTHLVL 432
Cdd:cd00825 308 TTPREL----RTALLNGFGLGGTNATLVL 332
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
162-435 |
3.44e-46 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 164.50 E-value: 3.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 162 YISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDL-PQEVGylyeengLFSS-----------DG 229
Cdd:COG0304 143 HVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAItPLGLA-------GFDAlgalstrnddpEK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 230 HCHSFDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSskegfM---APGVHGQYTCLQSAWRNAEV 306
Cdd:COG0304 216 ASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYH-----ItapAPDGEGAARAMRAALKDAGL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 307 EPDDLDYIAAHGSSTKLGDATEIYALKKAFKDvkKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFET 386
Cdd:COG0304 291 SPEDIDYINAHGTSTPLGDAAETKAIKRVFGD--HAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLEN 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499250115 387 PNPDFMLEdspiYIATEFQDFPTvkKHYLagVSSYGAGGSNTHLVLRSY 435
Cdd:COG0304 369 PDPECDLD----YVPNEAREAKI--DYAL--SNSFGFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
8-432 |
5.82e-46 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 163.86 E-value: 5.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 8 NKIAIVGMAVKFPGANDLDEYWDLLKFGKEAVTKFSEEQlhRSGISEQLIANPNykpyrgiLDDLESFDTAPFENTTKNF 87
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFD--ASGFPSRIAGEVP-------DFDPEDYLDRKELRRMDRF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 88 ELLGVqgkvmsHLTHRALSTMRSQEHHSNNYikNTAVYIGANNQPAAHFLGAAYYQSIDTQKA-----IERYYSKVIAPY 162
Cdd:cd00834 72 AQFAL------AAAEEALADAGLDPEELDPE--RIGVVIGSGIGGLATIEEAYRALLEKGPRRvspffVPMALPNMAAGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 163 ISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDG-----HCHSFDAS 237
Cdd:cd00834 144 VAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNddpekASRPFDKD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 238 ACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNS----SKEGfmapgvHGQYTCLQSAWRNAEVEPDDLDY 313
Cdd:cd00834 224 RDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHitapDPDG------EGAARAMRAALADAGLSPEDIDY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 314 IAAHGSSTKLGDATEIYALKKAFKDvkKTYRCPISSVISNLGHT-GIVSGMASIIkTVLMLKNKAIVPSINFETPNPDFM 392
Cdd:cd00834 298 INAHGTSTPLNDAAESKAIKRVFGE--HAKKVPVSSTKSMTGHLlGAAGAVEAIA-TLLALRDGVLPPTINLEEPDPECD 374
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 499250115 393 LEdspiYIATEFQDFPTvkkhyLAGVS-SYGAGGSNTHLVL 432
Cdd:cd00834 375 LD----YVPNEAREAPI-----RYALSnSFGFGGHNASLVF 406
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
8-258 |
1.95e-44 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 155.49 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 8 NKIAIVGMAVKFPGANDLDEYWDLLKFGKEAVTKFSEEQLHRSG--ISEQLIANPNYKPYrGILDDLESFDtAPFENTTK 85
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKlyDPPSRIAGKIYTKW-GGLDDIFDFD-PLFFGISP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 86 N-------FELLGVQgkVMSHLTHRALSTMRSQEHhsnnyiKNTAVYIGANNQpaahflGAAYYQSIDTQKAIERYYSK- 157
Cdd:pfam00109 79 ReaermdpQQRLLLE--AAWEALEDAGITPDSLDG------SRTGVFIGSGIG------DYAALLLLDEDGGPRRGSPFa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 158 ------VIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVGYLYEENGLFSSDGHC 231
Cdd:pfam00109 145 vgtmpsVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPC 224
|
250 260
....*....|....*....|....*..
gi 499250115 232 HSFDASACGTLYSNGAGLVVLKRLEDA 258
Cdd:pfam00109 225 KAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
10-435 |
6.49e-44 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 164.79 E-value: 6.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 10 IAIVGMAVKFPGANDLDEYWDLLKFGKEAVT-----KFSEEQLHRSGISEqliANPNYKPYRGILDDLEsFDTAPFENTT 84
Cdd:TIGR02813 9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITdvpsdHWAKDDYYDSDKSE---ADKSYCKRGGFLPEVD-FNPMEFGLPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 85 KNFELLGVQGKVMSHLTHRALSTMRSQEHHSNNYIKNTaVYIGANnQPAAHFLGAAYYQSI-------------DTQKAI 151
Cdd:TIGR02813 85 NILELTDISQLLSLVVAKEVLNDAGLPDGYDRDKIGIT-LGVGGG-QKQSSSLNARLQYPVlkkvfkasgvedeDSEMLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 152 ERYYSK---------------VIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDLPQEVG 216
Cdd:TIGR02813 163 KKFQDQyihweensfpgslgnVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 217 YLYEENGLFSSDGHCHSFDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSskEGFMAPGVHGQYTC 296
Cdd:TIGR02813 243 MSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKF--KSIYAPRPEGQAKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 297 LQSAWRNAEVEPDDLDYIAAHGSSTKLGDATEIYALKKAF-KDVKKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKN 375
Cdd:TIGR02813 321 LKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFsQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHH 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499250115 376 KAIVPSINFETPNPDFMLEDSPIYIATEFQdfPTVKKH----YLAGVSSYGAGGSNTHLVLRSY 435
Cdd:TIGR02813 401 KVLPPTINVDQPNPKLDIENSPFYLNTETR--PWMQREdgtpRRAGISSFGFGGTNFHMVLEEY 462
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
266-385 |
1.55e-38 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 135.39 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 266 HAVIIGSAMNNDGNSskEGFMAPGVHGQYTCLQSAWRNAEVEPDDLDYIAAHGSSTKLGDATEIYALKKAFKDVKKTYRC 345
Cdd:pfam02801 1 YAVIKGSAVNHDGRH--NGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKQPL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499250115 346 PISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFE 385
Cdd:pfam02801 79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
179-432 |
4.53e-33 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 128.71 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 179 ACSSSLTAVIQSCRELNSHQCDMAIAGACliDLPQEVGyLYE-------ENGLFSSDGHCHSFDASACGTLYSNGAGLVV 251
Cdd:cd00828 161 ACATALEALDLAVEAIRSGKADIVVVGGV--EDPLEEG-LSGfanmgalSTAEEEPEEMSRPFDETRDGFVEAEGAGVLV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 252 LKRLEDAIADHDLIHAVIIGSAMNNDGNSskeGFMAPGVHGQYTCLQSAWRNAEVEPDDLDYIAAHGSSTKLGDATEIYA 331
Cdd:cd00828 238 LERAELALARGAPIYGRVAGTASTTDGAG---RSVPAGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 332 LKKAFKDvkKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDfmleDSPIYIATEFQDFPTVK 411
Cdd:cd00828 315 IAEVAGA--LGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPD----VEHLSVVGLSRDLNLKV 388
|
250 260
....*....|....*....|.
gi 499250115 412 KHylAGVSSYGAGGSNTHLVL 432
Cdd:cd00828 389 RA--ALVNAFGFGGSNAALVL 407
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
163-434 |
8.68e-28 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 113.97 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 163 ISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGACLIDL-PQEVGYLYEENGL----FSSDGH--CHSFD 235
Cdd:PRK07103 150 CSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLsYWECQALRSLGAMgsdrFADEPEaaCRPFD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 236 ASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKEgfmaPGVHGQYTCLQSAWRNAEVEPDDLDYIA 315
Cdd:PRK07103 230 QDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPD----PSLEGEMRVIRAALRRAGLGPEDIDYVN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 316 AHGSSTKLGDATEIYALKKAfkdvkKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPnpdfmled 395
Cdd:PRK07103 306 PHGTGSPLGDETELAALFAS-----GLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEP-------- 372
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499250115 396 spiyIATEFQdF--PTVKKHYL--AGVSSYGAGGSNTHLVLRS 434
Cdd:PRK07103 373 ----IDERFR-WvgSTAESARIryALSLSFGFGGINTALVLER 410
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
160-437 |
1.55e-26 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 110.86 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 160 APYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAG---AClIDLPQEVGYLyeENGLFSSDGH------ 230
Cdd:PRK06333 153 AGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGgteAA-IDRVSLAGFA--AARALSTRFNdapeqa 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 231 CHSFDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKEGfmAPGVHGQYTCLQSAWRNAEVEPDD 310
Cdd:PRK06333 230 SRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAG--PEDGEGARRAMLIALRQAGIPPEE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 311 LDYIAAHGSSTKLGDATEIYALKKAFKDVKKTyrcPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPD 390
Cdd:PRK06333 308 VQHLNAHATSTPVGDLGEVAAIKKVFGHVSGL---AVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPA 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499250115 391 FMLEDspiYIATEFQDFPTvkKHYLAgvSSYGAGGSNTHLVLRSYDE 437
Cdd:PRK06333 385 AEGLD---VVANKARPMDM--DYALS--NGFGFGGVNASILFRRWEP 424
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
20-435 |
3.14e-24 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 104.00 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 20 PGANDLDEYWDLLKFGKEAVTKFSEEQLHRSGISEQLIANPNY---------KPYRGILDDLESFDTAPFENTTKNFELL 90
Cdd:PTZ00050 4 PLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLvaampcqiaAEVDQSEFDPSDFAPTKRESRATHFAMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 91 GVQgkvmSHLTHRALSTmrsqehhSNNYIKNTA-VYIGANNqPAAHFLG-AAYYQSIDTQKAIERY-YSKVI----APYI 163
Cdd:PTZ00050 84 AAR----EALADAKLDI-------LSEKDQERIgVNIGSGI-GSLADLTdEMKTLYEKGHSRVSPYfIPKILgnmaAGLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 164 SYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAG---ACLIDLP-------QEVGYLYEENGLFSSdghcHS 233
Cdd:PTZ00050 152 AIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGgteASITPVSfagfsrmRALCTKYNDDPQRAS----RP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 234 FDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNS----SKEGfmapgvHGQYTCLQSAWRN-AEVEP 308
Cdd:PTZ00050 228 FDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHitapHPDG------RGARRCMENALKDgANINI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 309 DDLDYIAAHGSSTKLGDATEIYALKKAFKDvKKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPN 388
Cdd:PTZ00050 302 NDVDYVNAHATSTPIGDKIELKAIKKVFGD-SGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPD 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 499250115 389 PDFMLEDSPIYIATEFQDFPTVKKhylagvSSYGAGGSNTHLVLRSY 435
Cdd:PTZ00050 381 AECDLNLVQGKTAHPLQSIDAVLS------TSFGFGGVNTALLFTKY 421
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
159-436 |
3.18e-24 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 103.72 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 159 IAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAG---ACLIDLPQevgylyeenGLFSS-------- 227
Cdd:PRK07314 141 AAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGgaeAAITPLGI---------AGFAAaralstrn 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 228 ---DGHCHSFDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSskegfM---APGVHGQYTCLQSAW 301
Cdd:PRK07314 212 ddpERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYH-----MtapAPDGEGAARAMKLAL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 302 RNAEVEPDDLDYIAAHGSSTKLGDATEIYALKKAFKDvkKTYRCPISSVISNLGHT-GIVSGMASIIkTVLMLKNKAIVP 380
Cdd:PRK07314 287 KDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGE--HAYKVAVSSTKSMTGHLlGAAGAVEAIF-SVLAIRDQVIPP 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499250115 381 SINFETPNPDFMLEdspiYIATEFQDfptvKKHYLAGVSSYGAGGSNTHLVLRSYD 436
Cdd:PRK07314 364 TINLDNPDEECDLD----YVPNEARE----RKIDYALSNSFGFGGTNASLVFKRYE 411
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
200-436 |
8.37e-24 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 102.44 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 200 DMAIAGACLiDLPQEVGYLYEENGLFSS------DGHCHSFDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSA 273
Cdd:PRK07967 182 DIVFAGGGE-ELDWEMSCLFDAMGALSTkyndtpEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYG 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 274 MNNDGNSskegFMAPGVHGQYTCLQSAWRNAEvepDDLDYIAAHGSSTKLGDATEIYALKKAFKDvkktyRCP-ISSVIS 352
Cdd:PRK07967 261 ATSDGYD----MVAPSGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVKELGAIREVFGD-----KSPaISATKS 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 353 NLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFmlEDSPIYIAT-EFQDFPTVKKhylagvSSYGAGGSNTHLV 431
Cdd:PRK07967 329 LTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQA--AGMPIVTETtDNAELTTVMS------NSFGFGGTNATLV 400
|
....*
gi 499250115 432 LRSYD 436
Cdd:PRK07967 401 FRRYK 405
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
160-434 |
1.08e-23 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 102.56 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 160 APYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGA--CLIDLPQEVGYL--------YEENGLFSSdg 229
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGteSSIDALSIAGFSrsralstkFNSCPTEAS-- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 230 hcHSFDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKEGfmAPGVHGQYTCLQSAWRNAEVEPD 309
Cdd:PLN02836 242 --RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQP--HEDGRGAVLAMTRALQQSGLHPN 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 310 DLDYIAAHGSSTKLGDATEIYALKKAFKDVKKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNP 389
Cdd:PLN02836 318 QVDYVNAHATSTPLGDAVEARAIKTVFSEHATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDP 397
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499250115 390 DFMLEDSPIyiaTEFQDFPTVkkhylAGVS-SYGAGGSNTHLVLRS 434
Cdd:PLN02836 398 IFDDGFVPL---TASKAMLIR-----AALSnSFGFGGTNASLLFTS 435
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
163-432 |
2.88e-23 |
|
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: 98.29 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 163 ISYQFGFQ-GSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGAclidlpqevgylyeenglfssdghchsFDASACGt 241
Cdd:cd00327 50 LAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGG---------------------------SEEFVFG- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 242 lysNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKEgfmAPGVHGQYTCLQSAWRNAEVEPDDLDYIAAHGSST 321
Cdd:cd00327 102 ---DGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVP---AVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 322 KLGDATEIYALKKAFKDvkktYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPsinfeTPNPdfmledspiyia 401
Cdd:cd00327 176 PIGDAVELALGLDPDGV----RSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP-----TPRE------------ 234
|
250 260 270
....*....|....*....|....*....|.
gi 499250115 402 tefqdfPTvkkhyLAGVSSYGAGGSNTHLVL 432
Cdd:cd00327 235 ------PR-----TVLLLGFGLGGTNAAVVL 254
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
162-427 |
7.26e-22 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 96.73 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 162 YISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCD-MAIAGACLIDLPQEVGYLYEENGLFS-SDGHCHS---FDA 236
Cdd:PRK08439 144 FISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADkMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKAsrpFDK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 237 SACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSskegFMAPGVHGQYTCLQSAWRNAEVEPddLDYIAA 316
Cdd:PRK08439 224 DRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANH----ITSPAPEGPLRAMKAALEMAGNPK--IDYINA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 317 HGSSTKLGDATEIYALKKAFKDVKKtyrCPISSviSNLGHTGIVSGMASIIKTV--LMLKNKAIV-PSINFETPNPDFML 393
Cdd:PRK08439 298 HGTSTPYNDKNETAALKELFGSKEK---VPPVS--STKGQIGHCLGAAGAIEAVisIMAMRDGILpPTINQETPDPECDL 372
|
250 260 270
....*....|....*....|....*....|....*..
gi 499250115 394 EdspiYIatefqdfPTVKKHYLAGV---SSYGAGGSN 427
Cdd:PRK08439 373 D----YI-------PNVARKAELNVvmsNSFGFGGTN 398
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
234-433 |
1.26e-19 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 90.43 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 234 FDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKEgfmaPGVHGQYTCLQSAWRNAEVEPDDLDY 313
Cdd:PRK09116 222 FDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQ----PQAETMQIAMELALKDAGLAPEDIGY 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 314 IAAHGSSTKLGDATEIYALKKAFKDvkktyRCPISSVISNLGHT----GIVSGMASIiktvLMLKNKAIVPSINFETPNP 389
Cdd:PRK09116 298 VNAHGTATDRGDIAESQATAAVFGA-----RMPISSLKSYFGHTlgacGALEAWMSI----EMMNEGWFAPTLNLTQVDP 368
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499250115 390 DFMLEDspiYIATEFQdfpTVKKHYLAGvSSYGAGGSNTHLVLR 433
Cdd:PRK09116 369 ACGALD---YIMGEAR---EIDTEYVMS-NNFAFGGINTSLIFK 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
151-389 |
7.99e-19 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 87.09 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 151 IERYYSKVIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGAC--LIDLPQEVGYLYEE--NGLFS 226
Cdd:PRK14691 62 VPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAeaVIDTVSLAGFAAARalSTHFN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 227 S--DGHCHSFDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKEGfmAPGVHGQYTCLQSAWRNA 304
Cdd:PRK14691 142 StpEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSG--AEDGDGAYRAMKIALRQA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 305 EVEPDDLDYIAAHGSSTKLGDATEIYALKKAFKDvkkTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINF 384
Cdd:PRK14691 220 GITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE---SNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNL 296
|
....*
gi 499250115 385 ETPNP 389
Cdd:PRK14691 297 ENPDP 301
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
158-433 |
1.16e-18 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 87.37 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 158 VIAPYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAG-ACLIDLPQEVGYLYEENGLFSSDGHCHS--- 233
Cdd:PRK08722 142 MIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGgAEKASTPLGMAGFGAAKALSTRNDEPQKasr 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 234 -FDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDG----NSSKEGfmapgvHGQYTCLQSAWRNAEVEP 308
Cdd:PRK08722 222 pWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAyhmtSPSEDG------SGGALAMEAAMRDAGVTG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 309 DDLDYIAAHGSSTKLGDATEIYALKKAFKDvKKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPN 388
Cdd:PRK08722 296 EQIGYVNAHGTSTPAGDVAEIKGIKRALGE-AGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPE 374
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499250115 389 PDFMLEDSPiYIATEfqdfptVKKHYLAGVSSYGAGGSNTHLVLR 433
Cdd:PRK08722 375 EGLDIDLVP-HTARK------VESMEYAICNSFGFGGTNGSLIFK 412
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
159-435 |
2.27e-18 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 86.61 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 159 IAPYISYQFGFQGSSIDLYTACSSSLTAvIQSCRE-LNSHQCDMAIAGA--------CLI------------DLPQEVGY 217
Cdd:PRK06501 154 IADRLADRFGTRGLPISLSTACASGATA-IQLGVEaIRRGETDRALCIAtdgsvsaeALIrfsllsalstqnDPPEKASK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 218 LYEENglfsSDGhchsFdasacgtLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDG----NSSKEGFMAPGvhgq 293
Cdd:PRK06501 233 PFSKD----RDG----F-------VMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhrtRSSPDGSPAIG---- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 294 ytCLQSAWRNAEVEPDDLDYIAAHGSSTKLGDATEIYALKKAFKDVKKTyrCPISSVISNLGHTGIVSGMASIIKTVLML 373
Cdd:PRK06501 294 --AIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLAS--IPVSSNKSMIGHTLTAAGAVEAVFSLLTI 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499250115 374 KNKAIVPSINFETPNPdfmledspiyiATEFQDFPTVKKHylAGVS-----SYGAGGSNTHLVLRSY 435
Cdd:PRK06501 370 QTGRLPPTINYDNPDP-----------AIPLDVVPNVARD--ARVTavlsnSFGFGGQNASLVLTAE 423
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
160-432 |
1.55e-17 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 83.74 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 160 APYISYQFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGA----CLidLPqevgyLYEENGLFS-SDGHCHSF 234
Cdd:PRK09185 140 ADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGvdslCR--LT-----LNGFNSLESlSPQPCRPF 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 235 DASACGTLYSNGAGLVVLKRL-EDAIAdhdlihavIIGSamnndGNSSKEGFM-APgvH----GQYTCLQSAWRNAEVEP 308
Cdd:PRK09185 213 SANRDGINIGEAAAFFLLEREdDAAVA--------LLGV-----GESSDAHHMsAP--HpeglGAILAMQQALADAGLAP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 309 DDLDYIAAHGSSTKLGDATEIYALKKAFKDvkktyRCPISSVISNLGHTgivSGMASIIKTV---LMLKNKAIVPSINFE 385
Cdd:PRK09185 278 ADIGYINLHGTATPLNDAMESRAVAAVFGD-----GVPCSSTKGLTGHT---LGAAGAVEAAicwLALRHGLPPHGWNTG 349
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499250115 386 TPNPDFMledsPIYIATEFQdfPTVKKHYLAgvSSYGAGGSNTHLVL 432
Cdd:PRK09185 350 QPDPALP----PLYLVENAQ--ALAIRYVLS--NSFAFGGNNCSLIF 388
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
166-434 |
1.33e-16 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 80.87 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 166 QFGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAGAclIDLPqeVGYL----YEENGLFSSDGhCHSFDASACGT 241
Cdd:PRK05952 132 QIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGA--VEAP--ITPLtlagFQQMGALAKTG-AYPFDRQREGL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 242 LYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKegfmAPGV--HGQYTCLQSAWRNAEVEPDDLDYIAAHGS 319
Cdd:PRK05952 207 VLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMS----APEPdgKSAIAAIQQCLARSGLTPEDIDYIHAHGT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 320 STKLGDATEIYALKKAFkdvkkTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETpnPDFMLEdspiy 399
Cdd:PRK05952 283 ATRLNDQREANLIQALF-----PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLN----- 350
|
250 260 270
....*....|....*....|....*....|....*
gi 499250115 400 IATEFQDFPTvkKHYLAgvSSYGAGGSNTHLVLRS 434
Cdd:PRK05952 351 FVRQAQQSPL--QNVLC--LSFGFGGQNAAIALGK 381
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
178-435 |
2.61e-16 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 80.54 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 178 TACSSSLTAVIQSCRELNSHQCDMAIAGAC--LID-LPqeVGYLYEENGLFSSD-----GHCHSFDASACGTLYSNGAGL 249
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGVetRIEaVP--IAGFAQMRIVMSTNnddpaGACRPFDKDRDGFVFGEGGAL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 250 VVLKRLEDAIADHDLIHAVIIGSAMNNDGNSskegFMAPGVHGQYT--CLQSAWRNAEVEPDDLDYIAAHGSSTKLGDAT 327
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASITSDGFH----MVAPDPNGERAghAMTRAIELAGLTPGDIDHVNAHATGTSVGDVA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 328 EIYALKKAFKDVKKTYRCPISSvisnLGHT-GIVSGMASIIkTVLMLKNKAIVPSINFETPNPDFMLEdspiYIATEfqd 406
Cdd:PRK07910 323 EGKAINNALGGHRPAVYAPKSA----LGHSvGAVGAVESIL-TVLALRDGVIPPTLNLENLDPEIDLD----VVAGE--- 390
|
250 260
....*....|....*....|....*....
gi 499250115 407 fPTVKKHYLAGVSSYGAGGSNTHLVLRSY 435
Cdd:PRK07910 391 -PRPGNYRYAINNSFGFGGHNVALAFGRY 418
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
167-435 |
5.04e-12 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 67.70 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 167 FGFQGSSIDLYTACSSSLTAVIQSCRELNSHQCDMAIAG---ACLIdlPQEVGYLYEENGLFSSDGH----CHSFDASAC 239
Cdd:PLN02787 278 LGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGgsdAAII--PIGLGGFVACRALSQRNDDptkaSRPWDMNRD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 240 GTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGNSSKEGFmaPGVHGQYTCLQSAWRNAEVEPDDLDYIAAHGS 319
Cdd:PLN02787 356 GFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPH--PEGAGVILCIEKALAQSGVSKEDVNYINAHAT 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 320 STKLGDATEIYALKKAFkdvKKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPDFmleDSPIY 399
Cdd:PLN02787 434 STKAGDLKEYQALMRCF---GQNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGV---DTKVL 507
|
250 260 270
....*....|....*....|....*....|....*.
gi 499250115 400 IATEFQDFpTVKkhyLAGVSSYGAGGSNTHLVLRSY 435
Cdd:PLN02787 508 VGPKKERL-DIK---VALSNSFGFGGHNSSILFAPY 539
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
387-438 |
7.04e-07 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 47.54 E-value: 7.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499250115 387 PNPDFM-LEDSPIYIATEFQDFPTvkkhYLAGVSSYGAGGSNTHLVLRSYDEN 438
Cdd:pfam16197 1 PNPDIPaLLDGRLKVVTEPTPWPG----GIVGVNSFGFGGANAHVILKSNPKP 49
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
234-394 |
4.27e-04 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 42.35 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 234 FDASACGTLYSNGAGLVVLKRLEDAIADHDLIHAVIIGSAMNNDGnsskegfmAPGVH---GQYTCLQSAWRNAEVEPDD 310
Cdd:cd00832 218 FDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDP--------PPGSGrppGLARAIRLALADAGLTPED 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499250115 311 LDYIAAHGSSTKLGDATEIYALKKAFkdvkKTYRCPISSVISNLGHTGIVSGMASIIKTVLMLKNKAIVPSINFETPNPD 390
Cdd:cd00832 290 VDVVFADAAGVPELDRAEAAALAAVF----GPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPA 365
|
....
gi 499250115 391 FMLE 394
Cdd:cd00832 366 YGLD 369
|
|
| |
