|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-610 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 586.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDWSSGAVELLTAAREWPETeGRPRRAGVSSFGVSGTNAHIILEQAPDP 80
Cdd:COG3321 353 AAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRPWPAG-GGPRRAGVSSFGFGGTNAHVVLEEAPAA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 81 DADAEEEPRsapetptielPAVPWMVSGHGAAALREQAARLLARVEGDAGLSPVDVGWSLASGRAALEHRAVVTGGTRAE 160
Cdd:COG3321 432 APAAAAAAR----------PPQLLVLSAKTEEALRALAARLAAFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREE 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 161 LLHGLGALARGEAATGVVTGPEETGngGRVVFVFPGQGSQWAGMARDLWESSPVFAERMEECERLLSGLVDWSLRDA--- 237
Cdd:COG3321 502 LAAKLRALAAGEAAPGVVTGAAAAA--PKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHLGWSLREVlfp 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 238 LADEAALARVDVVQPVLFSMMVSLAEVWRSYGVEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRALLAIAGRGGM 317
Cdd:COG3321 580 DEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAM 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 318 LSIVASQDWVRERIEPFgDRISIAAVNGPKAVVVSGDADALQELGAVLAKAGVMRWNVPgVDFSAHSAHVESLEGELAEI 397
Cdd:COG3321 660 LAVGLSEEEVEALLAGY-DGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLP-VSHAFHSPLMEPALEEFRAA 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 398 LAGVELRAAEVPFYSTVTAAPLNTAELDSGYWYRNLRQPVRFEETVRALADDGHGVFVEVSPHPILTMGVLETLEDPErs 477
Cdd:COG3321 738 LAGVTPRAPRIPLISNVTGTWLTGEALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAG-- 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 478 APAVVSTLRRDDGGLDRIVASLSEAWVHGVDVDWPRVFTGTGASRVELPTYAFQRRRYWLDGAYGGGEAAVSGLGVASAE 557
Cdd:COG3321 816 DAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGAL 895
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1369099469 558 HPLLGAAVELPDASGVVFTGRLSTRTHAWLADHAVGDVVLLPGTGFVELAVRA 610
Cdd:COG3321 896 LLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
193-488 |
4.08e-128 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 378.28 E-value: 4.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 193 VFPGQGSQWAGMARDLWESSPVFAERMEECERLLSGLVDWSLRD---ALADEAALARVDVVQPVLFSMMVSLAEVWRSYG 269
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDvllGEDGAASLLDTEVAQPALFAVQVALARLLRSWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 270 VEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRALLAIAGRGGMLSIVASQDWVRERIEPFGDRISIAAVNGPKAV 349
Cdd:smart00827 81 VRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGVPDRVSVAAVNSPSSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 350 VVSGDADALQELGAVLAKAGVmRWNVPGVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTAAPLNTAELDS-GY 428
Cdd:smart00827 161 VLSGDEDAVDELAARLEAEGI-FARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELDDaDY 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1369099469 429 WYRNLRQPVRFEETVRALAD-DGHGVFVEVSPHPILTMGVLETLedPERSAPAVVSTLRRD 488
Cdd:smart00827 240 WVRNLREPVRFADAVRALLAeGGVTVFLEVGPHPVLTGPIKQTL--AAAGSAVVLPSLRRG 298
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
191-509 |
1.75e-78 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 251.24 E-value: 1.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 191 VFVFPGQGSQWAGMARDLWESSPVFAERMEECERLLSGLVDWSLR--DALADEAALARVDVVQPVLFSMMVSLAEVWRSY 268
Cdd:pfam00698 1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSdvLRNNPEGTLDGTQFVQPALFAMQIALAALLQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 269 GVEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRALLAIAGRGGMLSIVASQDWVRERIEPfgdRISIAAVNGPKA 348
Cdd:pfam00698 81 GVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPD---DVVGAVVNSPRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 349 VVVSGDADALQELGAVLAKAGVmRWNVPGVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTAAPLNTAELDSGY 428
Cdd:pfam00698 158 VVISGPQEAVRELVERVSKEGV-GALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 429 WYRNLRQPVRFEETVRALADDGHGVFVEVSPHPILTMGVLETLEDPERSAPA-VVSTLRRD-DGGLDRIVASLSEAWVHG 506
Cdd:pfam00698 237 WVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSASDGKVAtLVGTLIRDqTDFLVTFLYILAVAHLTG 316
|
...
gi 1369099469 507 VDV 509
Cdd:pfam00698 317 SAP 319
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
1-475 |
2.41e-42 |
|
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: 2.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDWSSGAVELLTAAREWPETE-GRPRRAGVSSFGVSGTNAHIILEQ-AP 78
Cdd:TIGR02813 385 TAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQREdGTPRRAGISSFGFGGTNFHMVLEEySP 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 79 DPDADAEEEPRSAPETptielpavpWMVSGHGAAALREQAARLLARVEGDAGLSPVD-----VGWSLASGRAALEhRAVV 153
Cdd:TIGR02813 465 KHQRDDQYRQRAVAQT---------LLFTAANEKALVSSLKDWKNKLSAKADDQPYAfnalaVENTLRTIAVALA-RLGF 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 154 TGGTRAELLHGL-GALARGEAATG----VVTGPEETGNG-----GRVVFVFPGQGSQWAGMARDLWESSPVFAERMEECE 223
Cdd:TIGR02813 535 VAKNADELITMLeQAITQLEAKSCeewqLPSGISYRKSAlvvesGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 224 RLLS--GLVDWSL----------RDALADEAALARVDVVQPVLFSMMVSLAEVWRSYGVEPSAVVGHSQGEVAAACVAGV 291
Cdd:TIGR02813 615 SVFTqaGKGALSPvlypipvfndESRKAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGV 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 292 LSLEDAIRVVALRSRALLAIAGRGG-------MLSIVASQDWVRERIEPFGDrISIAAVNGPKAVVVSGDADALQELGAV 364
Cdd:TIGR02813 695 ISDDDYMMLAFSRGQAMAAPTGEADigfmyavILAVVGSPTVIANCIKDFEG-VSIANYNSPTQLVIAGVSTQIQIAAKA 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 365 LAKAGVMRWNVPgVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTA-APLNTAELDSGYWYRNLRQPVRFEETV 443
Cdd:TIGR02813 774 LKEKGFKAIPLP-VSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGkLHSNDAAAIKKALKNHMLQSVHFSEQL 852
|
490 500 510
....*....|....*....|....*....|..
gi 1369099469 444 RALADDGHGVFVEVSPHPILTMGVLETLEDPE 475
Cdd:TIGR02813 853 EAMYAAGARVFVEFGPKNILQKLVENTLKDKE 884
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
1-74 |
3.17e-25 |
|
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: 108.41 E-value: 3.17e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDWSSGAVELLTAAREWPETeGRPRRAGVSSFGVSGTNAHIIL 74
Cdd:cd00833 349 AAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWPAP-AGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
188-459 |
1.43e-22 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 99.45 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 188 GRVVFVFPGQGSQWAGMARDLwESSPVFAERMEECERLLS-GLVDWSLRDALAdeaalaRVD---VVQPVLFsmMVSLA- 262
Cdd:PLN02752 38 PTTAFLFPGQGAQAVGMGKEA-AEVPAAKALFDKASEILGyDLLDVCVNGPKE------KLDstvVSQPAIY--VASLAa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 263 -EVWRSYGVEPSAV------VGHSQGEVAAACVAGVLSLEDAIRVVALRSRAL--LAIAGRGGMLSIVASQDwvrERIEP 333
Cdd:PLN02752 109 vEKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMqaAADAGPSGMVSVIGLDS---DKVQE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 334 F----------GDRISIAAVNGPKAVVVSGDADALQELGAvLAKAGVMRWNVP-GVDFSAHSAHVESLEGELAEILAGVE 402
Cdd:PLN02752 186 LcaaaneevgeDDVVQIANYLCPGNYAVSGGKKGIDAVEA-KAKSFKARMTVRlAVAGAFHTSFMEPAVDALEAALAAVE 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1369099469 403 LRAAEVPFYSTVTAAPLNTAELDSGYWYRNLRQPVRFEETVRALADDGHGVFVEVSP 459
Cdd:PLN02752 265 IRTPRIPVISNVDAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGP 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-610 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 586.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDWSSGAVELLTAAREWPETeGRPRRAGVSSFGVSGTNAHIILEQAPDP 80
Cdd:COG3321 353 AAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRPWPAG-GGPRRAGVSSFGFGGTNAHVVLEEAPAA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 81 DADAEEEPRsapetptielPAVPWMVSGHGAAALREQAARLLARVEGDAGLSPVDVGWSLASGRAALEHRAVVTGGTRAE 160
Cdd:COG3321 432 APAAAAAAR----------PPQLLVLSAKTEEALRALAARLAAFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREE 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 161 LLHGLGALARGEAATGVVTGPEETGngGRVVFVFPGQGSQWAGMARDLWESSPVFAERMEECERLLSGLVDWSLRDA--- 237
Cdd:COG3321 502 LAAKLRALAAGEAAPGVVTGAAAAA--PKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHLGWSLREVlfp 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 238 LADEAALARVDVVQPVLFSMMVSLAEVWRSYGVEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRALLAIAGRGGM 317
Cdd:COG3321 580 DEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAM 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 318 LSIVASQDWVRERIEPFgDRISIAAVNGPKAVVVSGDADALQELGAVLAKAGVMRWNVPgVDFSAHSAHVESLEGELAEI 397
Cdd:COG3321 660 LAVGLSEEEVEALLAGY-DGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLP-VSHAFHSPLMEPALEEFRAA 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 398 LAGVELRAAEVPFYSTVTAAPLNTAELDSGYWYRNLRQPVRFEETVRALADDGHGVFVEVSPHPILTMGVLETLEDPErs 477
Cdd:COG3321 738 LAGVTPRAPRIPLISNVTGTWLTGEALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAG-- 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 478 APAVVSTLRRDDGGLDRIVASLSEAWVHGVDVDWPRVFTGTGASRVELPTYAFQRRRYWLDGAYGGGEAAVSGLGVASAE 557
Cdd:COG3321 816 DAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGAL 895
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1369099469 558 HPLLGAAVELPDASGVVFTGRLSTRTHAWLADHAVGDVVLLPGTGFVELAVRA 610
Cdd:COG3321 896 LLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
193-488 |
4.08e-128 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 378.28 E-value: 4.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 193 VFPGQGSQWAGMARDLWESSPVFAERMEECERLLSGLVDWSLRD---ALADEAALARVDVVQPVLFSMMVSLAEVWRSYG 269
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDvllGEDGAASLLDTEVAQPALFAVQVALARLLRSWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 270 VEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRALLAIAGRGGMLSIVASQDWVRERIEPFGDRISIAAVNGPKAV 349
Cdd:smart00827 81 VRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGVPDRVSVAAVNSPSSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 350 VVSGDADALQELGAVLAKAGVmRWNVPGVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTAAPLNTAELDS-GY 428
Cdd:smart00827 161 VLSGDEDAVDELAARLEAEGI-FARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELDDaDY 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1369099469 429 WYRNLRQPVRFEETVRALAD-DGHGVFVEVSPHPILTMGVLETLedPERSAPAVVSTLRRD 488
Cdd:smart00827 240 WVRNLREPVRFADAVRALLAeGGVTVFLEVGPHPVLTGPIKQTL--AAAGSAVVLPSLRRG 298
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
191-509 |
1.75e-78 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 251.24 E-value: 1.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 191 VFVFPGQGSQWAGMARDLWESSPVFAERMEECERLLSGLVDWSLR--DALADEAALARVDVVQPVLFSMMVSLAEVWRSY 268
Cdd:pfam00698 1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSdvLRNNPEGTLDGTQFVQPALFAMQIALAALLQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 269 GVEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRALLAIAGRGGMLSIVASQDWVRERIEPfgdRISIAAVNGPKA 348
Cdd:pfam00698 81 GVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPD---DVVGAVVNSPRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 349 VVVSGDADALQELGAVLAKAGVmRWNVPGVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTAAPLNTAELDSGY 428
Cdd:pfam00698 158 VVISGPQEAVRELVERVSKEGV-GALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 429 WYRNLRQPVRFEETVRALADDGHGVFVEVSPHPILTMGVLETLEDPERSAPA-VVSTLRRD-DGGLDRIVASLSEAWVHG 506
Cdd:pfam00698 237 WVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSASDGKVAtLVGTLIRDqTDFLVTFLYILAVAHLTG 316
|
...
gi 1369099469 507 VDV 509
Cdd:pfam00698 317 SAP 319
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
188-464 |
1.73e-54 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 187.64 E-value: 1.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 188 GRVVFVFPGQGSQWAGMARDLWESSPVFAERMEECERLLSglVDWSLRDALADEAALARVDVVQPVLFSMMVSLAEVWRS 267
Cdd:COG0331 1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALG--YDLSALCFEGPEEELNLTENTQPAILAASVAAYRALEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 268 YGVEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRAL--LAIAGRGGMLSIV-ASQDWVRERIE--PFGDRISIAA 342
Cdd:COG0331 79 EGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMqeAVPAGPGGMAAVLgLDDEEVEALCAeaAQGEVVEIAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 343 VNGPKAVVVSGDADALQELGAVLAKAG---VMRWNVPGVdfsAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTAAPL 419
Cdd:COG0331 159 YNSPGQIVISGEKEAVEAAAELAKEAGakrAVPLPVSGP---FHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1369099469 420 NTAELDSGYWYRNLRQPVRFEETVRALADDGHGVFVEVSPHPILT 464
Cdd:COG0331 236 TDPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLS 280
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
1-475 |
2.41e-42 |
|
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: 2.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDWSSGAVELLTAAREWPETE-GRPRRAGVSSFGVSGTNAHIILEQ-AP 78
Cdd:TIGR02813 385 TAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQREdGTPRRAGISSFGFGGTNFHMVLEEySP 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 79 DPDADAEEEPRSAPETptielpavpWMVSGHGAAALREQAARLLARVEGDAGLSPVD-----VGWSLASGRAALEhRAVV 153
Cdd:TIGR02813 465 KHQRDDQYRQRAVAQT---------LLFTAANEKALVSSLKDWKNKLSAKADDQPYAfnalaVENTLRTIAVALA-RLGF 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 154 TGGTRAELLHGL-GALARGEAATG----VVTGPEETGNG-----GRVVFVFPGQGSQWAGMARDLWESSPVFAERMEECE 223
Cdd:TIGR02813 535 VAKNADELITMLeQAITQLEAKSCeewqLPSGISYRKSAlvvesGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 224 RLLS--GLVDWSL----------RDALADEAALARVDVVQPVLFSMMVSLAEVWRSYGVEPSAVVGHSQGEVAAACVAGV 291
Cdd:TIGR02813 615 SVFTqaGKGALSPvlypipvfndESRKAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGV 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 292 LSLEDAIRVVALRSRALLAIAGRGG-------MLSIVASQDWVRERIEPFGDrISIAAVNGPKAVVVSGDADALQELGAV 364
Cdd:TIGR02813 695 ISDDDYMMLAFSRGQAMAAPTGEADigfmyavILAVVGSPTVIANCIKDFEG-VSIANYNSPTQLVIAGVSTQIQIAAKA 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 365 LAKAGVMRWNVPgVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTA-APLNTAELDSGYWYRNLRQPVRFEETV 443
Cdd:TIGR02813 774 LKEKGFKAIPLP-VSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGkLHSNDAAAIKKALKNHMLQSVHFSEQL 852
|
490 500 510
....*....|....*....|....*....|..
gi 1369099469 444 RALADDGHGVFVEVSPHPILTMGVLETLEDPE 475
Cdd:TIGR02813 853 EAMYAAGARVFVEFGPKNILQKLVENTLKDKE 884
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
192-464 |
9.15e-37 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 138.75 E-value: 9.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 192 FVFPGQGSQWAGMARDLWESSPVFAERMEECERLLsGLVDWSLrDALADEAALARVDVVQPVLFSMMVSLAEVWR-SYGV 270
Cdd:TIGR00128 5 YVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEAL-GYDLKKL-CQEGPAEELNKTQYTQPALYVVSAILYLKLKeQGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 271 EPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRAL-LAIAGRGGMLSIVASQDwvRERIEPFGDR-----ISIAAVN 344
Cdd:TIGR00128 83 KPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMqEAVPEGGGAMAAVIGLD--EEQLAQACEEatendVDLANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 345 GPKAVVVSGDADALQELGAVLAKAGVMRWNVPGVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTAAPLNTAEL 424
Cdd:TIGR00128 161 SPGQVVISGTKDGVEAAAALFKEMGAKRAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYTNGDR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1369099469 425 DSGYWYRNLRQPVRFEETVRALADDGHGVFVEVSPHPILT 464
Cdd:TIGR00128 241 IKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLT 280
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
1-76 |
5.06e-34 |
|
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: 131.30 E-value: 5.06e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDWSSGAVELLTAAREWPETeGRPRRAGVSSFGVSGTNAHIILEQ 76
Cdd:smart00825 224 AAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPPP-GRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| malonate_mdcH |
TIGR03131 |
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ... |
190-464 |
2.13e-25 |
|
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon subunit of malonate decarboxylase. This subunit has malonyl-CoA/dephospho-CoA acyltransferase activity. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. The epsilon subunit is closely related to the malonyl CoA-acyl carrier protein (ACP) transacylase family described by TIGR00128, but acts on an ACP subunit of malonate decarboxylase that has an unusual coenzyme A derivative as its prothetic group.
Pssm-ID: 132175 Cd Length: 295 Bit Score: 106.63 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 190 VVFVFPGQGSQWAGM---ARDLWESSPVFAERMEECERLLSGLVDWSLRDALADeaalarvdvVQPVLFSMMVSLAEVWR 266
Cdd:TIGR03131 1 IALLFPGQGSQRAGMlaeLPDHPAVAAVLAEASDVLGIDPRELDDAEALASTRS---------AQLCILAAGVAAWRALL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 267 SYGVEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRALLAIAGRG-GMLSIVASQdwvRERIEPF--GDRISIAAV 343
Cdd:TIGR03131 72 ALLPRPSAVAGYSVGEYAAAVVAGVLTFDDALRLVALRAALMDQAVPGGyGMLAVLGLD---LAAVEALiaKHGVYLAII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 344 NGPKAVVVSGDADALQELGAVLAKAGVMRWNVPGVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTAAPLNTAE 423
Cdd:TIGR03131 149 NAPDQVVIAGSRAALRAVAELARAAGASRAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDARLVRDAA 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1369099469 424 LDSGYWYRNLRQPVRFEETVRALADDGHGVFVEVSPHPILT 464
Cdd:TIGR03131 229 QIRDDLARQIATPVDWHDCMQAAYERGARLVIELGPGDVLT 269
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
1-74 |
3.17e-25 |
|
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: 108.41 E-value: 3.17e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDWSSGAVELLTAAREWPETeGRPRRAGVSSFGVSGTNAHIIL 74
Cdd:cd00833 349 AAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWPAP-AGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
188-459 |
1.43e-22 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 99.45 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 188 GRVVFVFPGQGSQWAGMARDLwESSPVFAERMEECERLLS-GLVDWSLRDALAdeaalaRVD---VVQPVLFsmMVSLA- 262
Cdd:PLN02752 38 PTTAFLFPGQGAQAVGMGKEA-AEVPAAKALFDKASEILGyDLLDVCVNGPKE------KLDstvVSQPAIY--VASLAa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 263 -EVWRSYGVEPSAV------VGHSQGEVAAACVAGVLSLEDAIRVVALRSRAL--LAIAGRGGMLSIVASQDwvrERIEP 333
Cdd:PLN02752 109 vEKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMqaAADAGPSGMVSVIGLDS---DKVQE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 334 F----------GDRISIAAVNGPKAVVVSGDADALQELGAvLAKAGVMRWNVP-GVDFSAHSAHVESLEGELAEILAGVE 402
Cdd:PLN02752 186 LcaaaneevgeDDVVQIANYLCPGNYAVSGGKKGIDAVEA-KAKSFKARMTVRlAVAGAFHTSFMEPAVDALEAALAAVE 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1369099469 403 LRAAEVPFYSTVTAAPLNTAELDSGYWYRNLRQPVRFEETVRALADDGHGVFVEVSP 459
Cdd:PLN02752 265 IRTPRIPVISNVDAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGP 321
|
|
| PKS_DH |
smart00826 |
Dehydratase domain in polyketide synthase (PKS) enzymes; |
558-611 |
1.68e-20 |
|
Dehydratase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214837 Cd Length: 167 Bit Score: 88.82 E-value: 1.68e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1369099469 558 HPLLGAAVELPDASGVVFTGRLSTRTHAWLADHAVGDVVLLPGTGFVELAVRAG 611
Cdd:smart00826 1 HPLLGARVELADGGGVVLTGRLSLRTHPWLADHRVGGTVVLPGAAYVELALAAA 54
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
28-153 |
4.79e-13 |
|
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: 65.64 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 28 PSTKVD-WSSGAVELLTAAREWPETegrprRAGVSSFGVSGTNAHIILEQAPDPDADaeeePRSAPETPTIelpaVPWmv 106
Cdd:pfam16197 1 PNPDIPaLLDGRLKVVTEPTPWPGG-----IVGVNSFGFGGANAHVILKSNPKPKIP----PESPDNLPRL----VLL-- 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1369099469 107 SGHGAAALREQAARLLARVEGDAGLSPVDVGWSLAsgRAALEHRAVV 153
Cdd:pfam16197 66 SGRTEEAVKALLEKLENHLDDAEFLSLLNDIHSLP--ISGHPYRGYA 110
|
|
| PS-DH |
pfam14765 |
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ... |
558-611 |
3.35e-11 |
|
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.
Pssm-ID: 434191 Cd Length: 296 Bit Score: 64.70 E-value: 3.35e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1369099469 558 HPLLGAAVELPDASGVVFTGRLSTRTHAWLADHAVGDVVLLPGTGFVELAVRAG 611
Cdd:pfam14765 1 HPLLGSRVPSPSDLEPVWRNRLRLADLPWLRDHRVGGTVVLPGAGYLEMALEAA 54
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
97-611 |
9.48e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 52.18 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 97 IELPAVPWMVSGHGAAALREQAARLLARVEGDAGLSPVDVGWSLASGRAALEHRAVVTGGTRAELLHGLGALARGEAATG 176
Cdd:COG3321 861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 177 VVTGPEETGNGGRVVFVFPGQGSQWAGmARDLWESSPVFAERMEECERLLSGLVDWSLRDALADEAALARVDVVQPVLFS 256
Cdd:COG3321 941 ALLALAAAAAAAAAALAAAEAGALLLL-AAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAA 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 257 MMVSLAEVWRSYGVEPSAVVGHSQGEVAAACVAGVLSLEDAIRVVALRSRALLAIAGRGGMLSIVASQDWVRERIEPFGD 336
Cdd:COG3321 1020 ALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALAL 1099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 337 RISIAAVNGPKAVVVSGDADALQELGAVLAKAGVMRWNVPGVDFSAHSAHVESLEGELAEILAGVELRAAEVPFYSTVTA 416
Cdd:COG3321 1100 AALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALAL 1179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 417 APLNTAELDSGYWYRNLRQPVRFEETVRALADDGHGVFVEVSPHPILTMGVLETLEDPERSAPAVVSTLRRDDGGLDRIV 496
Cdd:COG3321 1180 ALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAAL 1259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 497 ASLSEAWVHGVDVDWPRVFTGTGASRVELPTYAFQRRRYWLDGAYGGGEAAVSGLGVASAEHPLLGAAVELPDASGVVFT 576
Cdd:COG3321 1260 AALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAA 1339
|
490 500 510
....*....|....*....|....*....|....*
gi 1369099469 577 GRLSTRTHAWLADHAVGDVVLLPGTGFVELAVRAG 611
Cdd:COG3321 1340 ALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAA 1374
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
1-26 |
1.48e-05 |
|
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: 44.48 E-value: 1.48e-05
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
1-78 |
1.04e-03 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 41.70 E-value: 1.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDwssGAVELLTAAREwpetegRPRRAGVS-SFGVSGTNAHIILEQAP 78
Cdd:PLN02836 368 AAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFD---DGFVPLTASKA------MLIRAALSnSFGFGGTNASLLFTSPP 437
|
|
| SAT |
pfam16073 |
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit: ... |
271-361 |
2.13e-03 |
|
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit:ACP transacylase of the aflatoxin biosynthesis pathway. SAT selects the hexanoyl starter unit from a pair of specialized fungal fatty acid synthase subunits (HexA/HexB) and transfers it onto the polyketide synthase A acyl-carrier protein to prime polyketide chain elongation. The family is found in association with pfam02801, pfam00109, pfam00550, pfam00975, pfam00698.
Pssm-ID: 465005 Cd Length: 239 Bit Score: 40.28 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1369099469 271 EPSAVVGHSQGEVAAACVAGVLSLED-------AIRV-------VALRSRALLAIAGRGG--MLSIVA-SQDWVRERIEP 333
Cdd:pfam16073 103 SSTYLVGLCTGLLAAAAVSCSRSLSElvplaveAVRIafrlgllVQRVADRLEGSSSSPGswSLVVPGlSEEEAEKALEQ 182
|
90 100 110
....*....|....*....|....*....|....*.
gi 1369099469 334 FGD--------RISIAAVNgPKAVVVSGDADALQEL 361
Cdd:pfam16073 183 FNEskgippasRPYISAVS-PSSVTISGPPSTLELL 217
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1-74 |
4.46e-03 |
|
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: 39.83 E-value: 4.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPSTKVDwssgaVELLT-AAREWpetegrPRRAGVS-SFGVSGTNAHIIL 74
Cdd:cd00834 342 AAGAVEAIATLLALRDGVLPPTINLEEPDPECD-----LDYVPnEAREA------PIRYALSnSFGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-74 |
9.03e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 38.62 E-value: 9.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1369099469 1 AAGAAGVIKMVLALRHGVLPSTLHADEPS--TKVDWSSGavelltaarewpetEGRPR--RAGVS-SFGVSGTNAHIIL 74
Cdd:PRK07314 343 AAGAVEAIFSVLAIRDQVIPPTINLDNPDeeCDLDYVPN--------------EARERkiDYALSnSFGFGGTNASLVF 407
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