|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-677 |
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: 874.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:COG3321 303 VDYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNP 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 81 CIPWNKFPIIIPQSQMPWLRGEKPRLAGVSSFGFSGTNAHVVLEEAPVVEPVPPTVVRPIHLLTLSAKTEAALQELATRY 160
Cdd:COG3321 383 HIDFENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 161 QNHLATFADLDLGDICFNANIGRSHFNHRLAIVASSSTELKQKLADFTTKEEVTGIFRGQLPSvitRPKIAFLFTGQGSQ 240
Cdd:COG3321 463 AAFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAA---APKVAFLFPGQGSQ 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 241 YLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLLHILYPQAGEtSPIDDTAYTQPTLFALEYALAELWKSWGIEPDVVM 320
Cdd:COG3321 540 YVGMGRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDEEE-SRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVI 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 321 GHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGEMVAVLASENQVRDLIKPYEsQVSIAAVNGLQSVVISGATH 400
Cdd:COG3321 619 GHSVGEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYD-GVSIAAVNGPRSTVVSGPAE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 401 AICTLCAMLESQGVKTKPLQVSHAFHSPLMEPMIAAFAAVVSEVTYSQPCIPIVSNVTGELADEEIATAEYWVDHVQQPV 480
Cdd:COG3321 698 AVEALAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALDADYWVRHLRQPV 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 481 RFADGMQTLHQQGCELFVEIGPKPVLLGMGRQCLTE-DVAVWLPSLCPRQGEWQQMLQSLAQLYVRGVAVNWLGFDQGYA 559
Cdd:COG3321 778 RFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAaGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRG 857
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 560 RRKVMLPTYPFQRQsyWFETTDTPHQTQLLSRGKIFHPLLGQKLNLAGLKHQIRFESQISAKAPAYLSHHQVFGKPLLPA 639
Cdd:COG3321 858 RRRVPLPTYPFQRE--DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVAL 935
|
650 660 670
....*....|....*....|....*....|....*...
gi 1489830778 640 AAYLEMALAAGSTLFQIEGLMLEDVVIQQGLILSEEEA 677
Cdd:COG3321 936 AAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAA 973
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
233-525 |
9.15e-148 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 433.75 E-value: 9.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 233 LFTGQGSQYLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLLHILYPQAGETSpIDDTAYTQPTLFALEYALAELWKSW 312
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAAS-LLDTEVAQPALFAVQVALARLLRSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 313 GIEPDVVMGHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGEMVAVLASENQVRDLIKPYESQVSIAAVNGLQS 392
Cdd:smart00827 80 GVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGVPDRVSVAAVNSPSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 393 VVISGATHAICTLCAMLESQGVKTKPLQVSHAFHSPLMEPMIAAFAAVVSEVTYSQPCIPIVSNVTGELAD-EEIATAEY 471
Cdd:smart00827 160 VVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDgAELDDADY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1489830778 472 WVDHVQQPVRFADGMQTLH-QQGCELFVEIGPKPVLLGMGRQCLTE-DVAVWLPSL 525
Cdd:smart00827 240 WVRNLREPVRFADAVRALLaEGGVTVFLEVGPHPVLTGPIKQTLAAaGSAVVLPSL 295
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
1-547 |
3.91e-89 |
|
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: 308.09 E-value: 3.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:TIGR02813 335 CGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNP 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 81 CIPWNKFPIIIPQSQMPWLRGEK--PRLAGVSSFGFSGTNAHVVLEE--APVVEPVPPTVVRPIHLLTLSAKTEAALQEL 156
Cdd:TIGR02813 415 KLDIENSPFYLNTETRPWMQREDgtPRRAGISSFGFGGTNFHMVLEEysPKHQRDDQYRQRAVAQTLLFTAANEKALVSS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 157 ATRYQNhlATFADLDLGDICFNA--------NIGRSHfnHRLAIVASSSTELKQKLADFTTKEEVTGIFRGQLPS----- 223
Cdd:TIGR02813 495 LKDWKN--KLSAKADDQPYAFNAlaventlrTIAVAL--ARLGFVAKNADELITMLEQAITQLEAKSCEEWQLPSgisyr 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 224 ----VITRPKIAFLFTGQGSQYLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLLHILYP---------QAGETSpIDD 290
Cdd:TIGR02813 571 ksalVVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLYPipvfndesrKAQEEA-LTN 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 291 TAYTQPTLFALEYALAELWKSWGIEPDVVMGHSVGEYVAACVAGVFSLEEGLKLIANRGRFM-QTLVKG--GEMVAVLAS 367
Cdd:TIGR02813 650 TQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMaAPTGEAdiGFMYAVILA 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 368 ENQVRDLIKPYESQ---VSIAAVNGLQSVVISGATHAICTLCAMLESQGVKTKPLQVSHAFHSPLMEPMIAAFAAVVSEV 444
Cdd:TIGR02813 730 VVGSPTVIANCIKDfegVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPLVAHAQKPFSAAIDKA 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 445 TYSQPCIPIVSNVTGEL-ADEEIATAEYWVDHVQQPVRFADGMQTLHQQGCELFVEIGPKPVLlgmgrQCLTEDV-AVWL 522
Cdd:TIGR02813 810 KFNTPLVPLYSNGTGKLhSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNIL-----QKLVENTlKDKE 884
|
570 580 590
....*....|....*....|....*....|..
gi 1489830778 523 PSLC-------PRQGEWQQMLQSLAQLYVRGV 547
Cdd:TIGR02813 885 NELCaisinpnPKGDSDMQLRQAAVQLAVLGL 916
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
1-123 |
3.64e-65 |
|
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: 222.82 E-value: 3.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:cd00833 299 IDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNP 378
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1489830778 81 CIPWNKFPIIIPQSQMPWLRGEKPRLAGVSSFGFSGTNAHVVL 123
Cdd:cd00833 379 KIDFEESPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
232-549 |
2.34e-58 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 201.16 E-value: 2.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 232 FLFTGQGSQYLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLLHILypQAGETSPIDDTAYTQPTLFALEYALAELWKS 311
Cdd:pfam00698 2 FVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVL--RNNPEGTLDGTQFVQPALFAMQIALAALLQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 312 WGIEPDVVMGHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGEMVAVLASENQVRdliKPYESQVSIAAVNGLQ 391
Cdd:pfam00698 80 YGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVE---QRWPDDVVGAVVNSPR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 392 SVVISGATHAICTLCAMLESQGVKTKPLQVSHAFHSPLMEPMIAAFAAVVSEVTYSQPCIPIVSNVTGELADEEIATAEY 471
Cdd:pfam00698 157 SVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 472 WVDHVQQPVRFADGMQTLHQQGCELFVEIGPKPVLLGMGRQCLTED----VAVWLPSLCPRQGEWQQ-MLQSLAQLYVRG 546
Cdd:pfam00698 237 WVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSAsdgkVATLVGTLIRDQTDFLVtFLYILAVAHLTG 316
|
...
gi 1489830778 547 VAV 549
Cdd:pfam00698 317 SAP 319
|
|
| PKS_DH |
smart00826 |
Dehydratase domain in polyketide synthase (PKS) enzymes; |
596-763 |
2.76e-39 |
|
Dehydratase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214837 Cd Length: 167 Bit Score: 142.75 E-value: 2.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 596 HPLLGQKLNLAGLKhQIRFESQISAKAPAYLSHHQVFGKPLLPAAAYLEMALAAGSTLFQIEGLMLEDVVIQQGLILSEE 675
Cdd:smart00826 1 HPLLGARVELADGG-GVVLTGRLSLRTHPWLADHRVGGTVVLPGAAYVELALAAADEVGGGAPARLEELTLEAPLVLPED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 676 EAKTVQVILTIS-ETQVYDFQIFSLNLEEAqkepRWTLHTEGKLRIENLETLPSKANLETWQIQCNQQVSVTNYYQQYHD 754
Cdd:smart00826 80 GAVRVQVVVGAPdEDGRRTFTVYSRPDGDG----PWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVDDLYERLAA 155
|
....*....
gi 1489830778 755 LGIDYGSSF 763
Cdd:smart00826 156 RGLEYGPAF 164
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
227-509 |
5.15e-39 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 147.99 E-value: 5.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 227 RPKIAFLFTGQGSQYLHMGRQLYETqPTFRKALEQCDAILrNYlekPLLHILYpqAGETSPIDDTAYTQPTLFALEYALA 306
Cdd:PLN02752 37 KPTTAFLFPGQGAQAVGMGKEAAEV-PAAKALFDKASEIL-GY---DLLDVCV--NGPKEKLDSTVVSQPAIYVASLAAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 307 ELWKSWGIEPDVV------MGHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGE--MVAVL------------A 366
Cdd:PLN02752 110 EKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAADAGPsgMVSVIgldsdkvqelcaA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 367 SENQVRDlikpyESQVSIAavNGL--QSVVISGATHAICTLCAMLESQGV-KTKPLQVSHAFHSPLMEPMIAAFAAVVSE 443
Cdd:PLN02752 190 ANEEVGE-----DDVVQIA--NYLcpGNYAVSGGKKGIDAVEAKAKSFKArMTVRLAVAGAFHTSFMEPAVDALEAALAA 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1489830778 444 VTYSQPCIPIVSNVTGELADEEIATAEYWVDHVQQPVRFADGMQTLHQQGCELFVEIGPKPVLLGM 509
Cdd:PLN02752 263 VEIRTPRIPVISNVDAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGI 328
|
|
| PS-DH |
pfam14765 |
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ... |
596-763 |
2.38e-38 |
|
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: 144.44 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 596 HPLLGQKLNLAGlKHQIRFESQISAKAPAYLSHHQVFGKPLLPAAAYLEMALAAGSTLFQI-EGLMLEDVVIQQGLILSE 674
Cdd:pfam14765 1 HPLLGSRVPSPS-DLEPVWRNRLRLADLPWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGsGAVALRDVSILKALVLPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 675 EEAKTVQVILTISE---TQVYDFQIFSLNLEEAQkeprWTLHTEGKLRIENLETLPSkANLETWQIQCNQQ-----VSVT 746
Cdd:pfam14765 80 DDPVEVQTSLTPEEdgaDSWWEFEIFSRAGGGWE----WTLHATGTVRLAPGEPAAP-VDLESLPARCAQPadprsVSSA 154
|
170
....*....|....*..
gi 1489830778 747 NYYQQYHDLGIDYGSSF 763
Cdd:pfam14765 155 EFYERLAARGLFYGPAF 171
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-677 |
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: 874.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:COG3321 303 VDYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNP 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 81 CIPWNKFPIIIPQSQMPWLRGEKPRLAGVSSFGFSGTNAHVVLEEAPVVEPVPPTVVRPIHLLTLSAKTEAALQELATRY 160
Cdd:COG3321 383 HIDFENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 161 QNHLATFADLDLGDICFNANIGRSHFNHRLAIVASSSTELKQKLADFTTKEEVTGIFRGQLPSvitRPKIAFLFTGQGSQ 240
Cdd:COG3321 463 AAFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAA---APKVAFLFPGQGSQ 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 241 YLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLLHILYPQAGEtSPIDDTAYTQPTLFALEYALAELWKSWGIEPDVVM 320
Cdd:COG3321 540 YVGMGRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDEEE-SRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVI 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 321 GHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGEMVAVLASENQVRDLIKPYEsQVSIAAVNGLQSVVISGATH 400
Cdd:COG3321 619 GHSVGEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYD-GVSIAAVNGPRSTVVSGPAE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 401 AICTLCAMLESQGVKTKPLQVSHAFHSPLMEPMIAAFAAVVSEVTYSQPCIPIVSNVTGELADEEIATAEYWVDHVQQPV 480
Cdd:COG3321 698 AVEALAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALDADYWVRHLRQPV 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 481 RFADGMQTLHQQGCELFVEIGPKPVLLGMGRQCLTE-DVAVWLPSLCPRQGEWQQMLQSLAQLYVRGVAVNWLGFDQGYA 559
Cdd:COG3321 778 RFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAaGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRG 857
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 560 RRKVMLPTYPFQRQsyWFETTDTPHQTQLLSRGKIFHPLLGQKLNLAGLKHQIRFESQISAKAPAYLSHHQVFGKPLLPA 639
Cdd:COG3321 858 RRRVPLPTYPFQRE--DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVAL 935
|
650 660 670
....*....|....*....|....*....|....*...
gi 1489830778 640 AAYLEMALAAGSTLFQIEGLMLEDVVIQQGLILSEEEA 677
Cdd:COG3321 936 AAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAA 973
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
233-525 |
9.15e-148 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 433.75 E-value: 9.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 233 LFTGQGSQYLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLLHILYPQAGETSpIDDTAYTQPTLFALEYALAELWKSW 312
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAAS-LLDTEVAQPALFAVQVALARLLRSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 313 GIEPDVVMGHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGEMVAVLASENQVRDLIKPYESQVSIAAVNGLQS 392
Cdd:smart00827 80 GVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGVPDRVSVAAVNSPSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 393 VVISGATHAICTLCAMLESQGVKTKPLQVSHAFHSPLMEPMIAAFAAVVSEVTYSQPCIPIVSNVTGELAD-EEIATAEY 471
Cdd:smart00827 160 VVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDgAELDDADY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1489830778 472 WVDHVQQPVRFADGMQTLH-QQGCELFVEIGPKPVLLGMGRQCLTE-DVAVWLPSL 525
Cdd:smart00827 240 WVRNLREPVRFADAVRALLaEGGVTVFLEVGPHPVLTGPIKQTLAAaGSAVVLPSL 295
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
1-547 |
3.91e-89 |
|
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: 308.09 E-value: 3.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:TIGR02813 335 CGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNP 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 81 CIPWNKFPIIIPQSQMPWLRGEK--PRLAGVSSFGFSGTNAHVVLEE--APVVEPVPPTVVRPIHLLTLSAKTEAALQEL 156
Cdd:TIGR02813 415 KLDIENSPFYLNTETRPWMQREDgtPRRAGISSFGFGGTNFHMVLEEysPKHQRDDQYRQRAVAQTLLFTAANEKALVSS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 157 ATRYQNhlATFADLDLGDICFNA--------NIGRSHfnHRLAIVASSSTELKQKLADFTTKEEVTGIFRGQLPS----- 223
Cdd:TIGR02813 495 LKDWKN--KLSAKADDQPYAFNAlaventlrTIAVAL--ARLGFVAKNADELITMLEQAITQLEAKSCEEWQLPSgisyr 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 224 ----VITRPKIAFLFTGQGSQYLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLLHILYP---------QAGETSpIDD 290
Cdd:TIGR02813 571 ksalVVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLYPipvfndesrKAQEEA-LTN 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 291 TAYTQPTLFALEYALAELWKSWGIEPDVVMGHSVGEYVAACVAGVFSLEEGLKLIANRGRFM-QTLVKG--GEMVAVLAS 367
Cdd:TIGR02813 650 TQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMaAPTGEAdiGFMYAVILA 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 368 ENQVRDLIKPYESQ---VSIAAVNGLQSVVISGATHAICTLCAMLESQGVKTKPLQVSHAFHSPLMEPMIAAFAAVVSEV 444
Cdd:TIGR02813 730 VVGSPTVIANCIKDfegVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPLVAHAQKPFSAAIDKA 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 445 TYSQPCIPIVSNVTGEL-ADEEIATAEYWVDHVQQPVRFADGMQTLHQQGCELFVEIGPKPVLlgmgrQCLTEDV-AVWL 522
Cdd:TIGR02813 810 KFNTPLVPLYSNGTGKLhSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNIL-----QKLVENTlKDKE 884
|
570 580 590
....*....|....*....|....*....|..
gi 1489830778 523 PSLC-------PRQGEWQQMLQSLAQLYVRGV 547
Cdd:TIGR02813 885 NELCaisinpnPKGDSDMQLRQAAVQLAVLGL 916
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
229-509 |
4.48e-86 |
|
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: 274.31 E-value: 4.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 229 KIAFLFTGQGSQYLHMGRQLYETQPTFRKALEQCDAILrnylEKPLLHILypQAGETSPIDDTAYTQPTLFALEYALAEL 308
Cdd:COG0331 2 KLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEAL----GYDLSALC--FEGPEEELNLTENTQPAILAASVAAYRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 309 WKSWGIEPDVVMGHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGE--MVAVL-ASENQVRDLIKPYES--QVS 383
Cdd:COG0331 76 LEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGPggMAAVLgLDDEEVEALCAEAAQgeVVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 384 IAAVNGLQSVVISGATHAICTLCAMLESQGVK-TKPLQVSHAFHSPLMEPMIAAFAAVVSEVTYSQPCIPIVSNVTGELA 462
Cdd:COG0331 156 IANYNSPGQIVISGEKEAVEAAAELAKEAGAKrAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1489830778 463 DEEIATAEYWVDHVQQPVRFADGMQTLHQQGCELFVEIGPKPVLLGM 509
Cdd:COG0331 236 TDPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGL 282
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
1-123 |
3.64e-65 |
|
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: 222.82 E-value: 3.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:cd00833 299 IDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNP 378
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1489830778 81 CIPWNKFPIIIPQSQMPWLRGEKPRLAGVSSFGFSGTNAHVVL 123
Cdd:cd00833 379 KIDFEESPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
229-509 |
6.30e-63 |
|
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: 212.33 E-value: 6.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 229 KIAFLFTGQGSQYLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLlhilypQAGETSPIDDTAYTQPTLFALEYALAEL 308
Cdd:TIGR00128 2 KIAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEALGYDLKKLC------QEGPAEELNKTQYTQPALYVVSAILYLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 309 WK-SWGIEPDVVMGHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLV--KGGEMVAVLA-SENQVRDLIKPY-ESQVS 383
Cdd:TIGR00128 76 LKeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVpeGGGAMAAVIGlDEEQLAQACEEAtENDVD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 384 IAAVNGLQSVVISGATHAICTLCAMLESQGVK-TKPLQVSHAFHSPLMEPMIAAFAAVVSEVTYSQPCIPIVSNVTGELA 462
Cdd:TIGR00128 156 LANFNSPGQVVISGTKDGVEAAAALFKEMGAKrAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPY 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1489830778 463 DEEIATAEYWVDHVQQPVRFADGMQTLHQQGCELFVEIGPKPVLLGM 509
Cdd:TIGR00128 236 TNGDRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGL 282
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
232-549 |
2.34e-58 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 201.16 E-value: 2.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 232 FLFTGQGSQYLHMGRQLYETQPTFRKALEQCDAILRNYLEKPLLHILypQAGETSPIDDTAYTQPTLFALEYALAELWKS 311
Cdd:pfam00698 2 FVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVL--RNNPEGTLDGTQFVQPALFAMQIALAALLQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 312 WGIEPDVVMGHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGEMVAVLASENQVRdliKPYESQVSIAAVNGLQ 391
Cdd:pfam00698 80 YGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVE---QRWPDDVVGAVVNSPR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 392 SVVISGATHAICTLCAMLESQGVKTKPLQVSHAFHSPLMEPMIAAFAAVVSEVTYSQPCIPIVSNVTGELADEEIATAEY 471
Cdd:pfam00698 157 SVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 472 WVDHVQQPVRFADGMQTLHQQGCELFVEIGPKPVLLGMGRQCLTED----VAVWLPSLCPRQGEWQQ-MLQSLAQLYVRG 546
Cdd:pfam00698 237 WVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSAsdgkVATLVGTLIRDQTDFLVtFLYILAVAHLTG 316
|
...
gi 1489830778 547 VAV 549
Cdd:pfam00698 317 SAP 319
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
36-125 |
1.13e-48 |
|
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: 173.67 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 36 LTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNPCIPWNKFPIIIPQSQMPWLRGEKPRLAGVSSFGFS 115
Cdd:smart00825 209 LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPPPGRPRRAGVSSFGFG 288
|
90
....*....|
gi 1489830778 116 GTNAHVVLEE 125
Cdd:smart00825 289 GTNAHVILEE 298
|
|
| PKS_DH |
smart00826 |
Dehydratase domain in polyketide synthase (PKS) enzymes; |
596-763 |
2.76e-39 |
|
Dehydratase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214837 Cd Length: 167 Bit Score: 142.75 E-value: 2.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 596 HPLLGQKLNLAGLKhQIRFESQISAKAPAYLSHHQVFGKPLLPAAAYLEMALAAGSTLFQIEGLMLEDVVIQQGLILSEE 675
Cdd:smart00826 1 HPLLGARVELADGG-GVVLTGRLSLRTHPWLADHRVGGTVVLPGAAYVELALAAADEVGGGAPARLEELTLEAPLVLPED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 676 EAKTVQVILTIS-ETQVYDFQIFSLNLEEAqkepRWTLHTEGKLRIENLETLPSKANLETWQIQCNQQVSVTNYYQQYHD 754
Cdd:smart00826 80 GAVRVQVVVGAPdEDGRRTFTVYSRPDGDG----PWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVDDLYERLAA 155
|
....*....
gi 1489830778 755 LGIDYGSSF 763
Cdd:smart00826 156 RGLEYGPAF 164
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
227-509 |
5.15e-39 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 147.99 E-value: 5.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 227 RPKIAFLFTGQGSQYLHMGRQLYETqPTFRKALEQCDAILrNYlekPLLHILYpqAGETSPIDDTAYTQPTLFALEYALA 306
Cdd:PLN02752 37 KPTTAFLFPGQGAQAVGMGKEAAEV-PAAKALFDKASEIL-GY---DLLDVCV--NGPKEKLDSTVVSQPAIYVASLAAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 307 ELWKSWGIEPDVV------MGHSVGEYVAACVAGVFSLEEGLKLIANRGRFMQTLVKGGE--MVAVL------------A 366
Cdd:PLN02752 110 EKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAADAGPsgMVSVIgldsdkvqelcaA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 367 SENQVRDlikpyESQVSIAavNGL--QSVVISGATHAICTLCAMLESQGV-KTKPLQVSHAFHSPLMEPMIAAFAAVVSE 443
Cdd:PLN02752 190 ANEEVGE-----DDVVQIA--NYLcpGNYAVSGGKKGIDAVEAKAKSFKArMTVRLAVAGAFHTSFMEPAVDALEAALAA 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1489830778 444 VTYSQPCIPIVSNVTGELADEEIATAEYWVDHVQQPVRFADGMQTLHQQGCELFVEIGPKPVLLGM 509
Cdd:PLN02752 263 VEIRTPRIPVISNVDAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGI 328
|
|
| PS-DH |
pfam14765 |
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ... |
596-763 |
2.38e-38 |
|
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: 144.44 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 596 HPLLGQKLNLAGlKHQIRFESQISAKAPAYLSHHQVFGKPLLPAAAYLEMALAAGSTLFQI-EGLMLEDVVIQQGLILSE 674
Cdd:pfam14765 1 HPLLGSRVPSPS-DLEPVWRNRLRLADLPWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGsGAVALRDVSILKALVLPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 675 EEAKTVQVILTISE---TQVYDFQIFSLNLEEAQkeprWTLHTEGKLRIENLETLPSkANLETWQIQCNQQ-----VSVT 746
Cdd:pfam14765 80 DDPVEVQTSLTPEEdgaDSWWEFEIFSRAGGGWE----WTLHATGTVRLAPGEPAAP-VDLESLPARCAQPadprsVSSA 154
|
170
....*....|....*..
gi 1489830778 747 NYYQQYHDLGIDYGSSF 763
Cdd:pfam14765 155 EFYERLAARGLFYGPAF 171
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
1-75 |
1.28e-34 |
|
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: 127.68 E-value: 1.28e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENcPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHF 75
Cdd:pfam02801 44 VDYVEAHGTGTPLGDPIEAEALKRVFGSG-ARKQPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
78-189 |
1.50e-23 |
|
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: 96.07 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 78 PNPCIP-WNKFPIIIPQSQMPWLRGekprLAGVSSFGFSGTNAHVVLEEAPVVEPVPPTVVRPIHLLTLSAKTEAALQEL 156
Cdd:pfam16197 1 PNPDIPaLLDGRLKVVTEPTPWPGG----IVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKAL 76
|
90 100 110
....*....|....*....|....*....|...
gi 1489830778 157 ATRYQNHLATFADLDLGDICFNANIgrSHFNHR 189
Cdd:pfam16197 77 LEKLENHLDDAEFLSLLNDIHSLPI--SGHPYR 107
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1-123 |
1.91e-21 |
|
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: 97.61 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFwenCPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:cd00834 295 IDYINAHGTSTPLNDAAESKAIKRVF---GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDP 371
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1489830778 81 CIPwnkFPIIIPQSQmpwlrgEKPRLAGVS-SFGFSGTNAHVVL 123
Cdd:cd00834 372 ECD---LDYVPNEAR------EAPIRYALSnSFGFGGHNASLVF 406
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
1-123 |
8.42e-20 |
|
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: 91.54 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFwencpRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:cd00825 225 IDYLVAHGTGTPIGDVKELKLLRSEF-----GDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE 299
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1489830778 81 cipwNKFPIIIPQsqmpwlRGEKPRLAGVSSFGFSGTNAHVVL 123
Cdd:cd00825 300 ----AGLNIVTET------TPRELRTALLNGFGLGGTNATLVL 332
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
1-123 |
1.92e-19 |
|
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: 91.31 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRLqPLTigSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:COG0304 295 IDYINAHGTSTPLGDAAETKAIKRVFGDHAYKV-PVS--STKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDP 371
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1489830778 81 CIPWNkfpiIIPqsqmpwlrgEKPRLAGVS-----SFGFSGTNAHVVL 123
Cdd:COG0304 372 ECDLD----YVP---------NEAREAKIDyalsnSFGFGGHNASLVF 406
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
1-123 |
5.59e-16 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 80.99 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRlQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSEHATS-GGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDP 397
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1489830778 81 CIPWNKFPIIIPQsqmpwlrgEKPRLAGVS-SFGFSGTNAHVVL 123
Cdd:PLN02836 398 IFDDGFVPLTASK--------AMLIRAALSnSFGFGGTNASLLF 433
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
1-123 |
8.56e-16 |
|
"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: 80.18 E-value: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWEncpRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:cd00828 294 LDVISAHGTSTPANDVAESRAIAEVAGA---LGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDP 370
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1489830778 81 CIPwnkFPIIIPQSQMPwlrGEKPRLAGVSSFGFSGTNAHVVL 123
Cdd:cd00828 371 DVE---HLSVVGLSRDL---NLKVRAALVNAFGFGGSNAALVL 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
1-119 |
3.48e-15 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 78.58 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRlqPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PTZ00050 304 VDYVNAHATSTPIGDKIELKAIKKVFGDSGAP--KLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDA 381
|
90 100 110
....*....|....*....|....*....|....*....
gi 1489830778 81 CIPWNkfpiIIPQSQMPWLRGEKPRLAgvSSFGFSGTNA 119
Cdd:PTZ00050 382 ECDLN----LVQGKTAHPLQSIDAVLS--TSFGFGGVNT 414
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-123 |
1.20e-14 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 76.75 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRlqpLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PRK07314 296 IDYINAHGTSTPAGDKAETQAIKRVFGEHAYK---VAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDE 372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1489830778 81 CIPWNKFPiiipqsqmpwlrgEKPRLAGV-----SSFGFSGTNAHVVL 123
Cdd:PRK07314 373 ECDLDYVP-------------NEARERKIdyalsNSFGFGGTNASLVF 407
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
1-123 |
5.19e-14 |
|
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: 72.48 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFwencpRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPhlhfskpnp 80
Cdd:cd00327 165 IDYVEAHGTGTPIGDAVELALGLDPD-----GVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP--------- 230
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1489830778 81 cipwnkfpiiipqsqmpwlRGEKPRLAGVSSFGFSGTNAHVVL 123
Cdd:cd00327 231 -------------------TPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
1-123 |
6.15e-14 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 74.67 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWEncpRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PRK06501 309 IDYINAHGTSTPENDKMEYLGLSAVFGE---RLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDP 385
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1489830778 81 CIPWNKFPiiipqsqmpwlrgEKPRLAGVS-----SFGFSGTNAHVVL 123
Cdd:PRK06501 386 AIPLDVVP-------------NVARDARVTavlsnSFGFGGQNASLVL 420
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-123 |
9.07e-14 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 74.26 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFwencPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PRK06333 308 VQHLNAHATSTPVGDLGEVAAIKKVF----GHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDP 383
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1489830778 81 CIpwnKFPIIIPQSQMPWlrgeKPRLAGVSSFGFSGTNAHVVL 123
Cdd:PRK06333 384 AA---EGLDVVANKARPM----DMDYALSNGFGFGGVNASILF 419
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-123 |
1.21e-12 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 70.47 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPrlqplTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PRK07967 291 IDYINTHGTSTPVGDVKELGAIREVFGDKSP-----AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP 365
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1489830778 81 cipwnKFpiiipqSQMPWLRG--EKPRLAGV--SSFGFSGTNAHVVL 123
Cdd:PRK07967 366 -----QA------AGMPIVTEttDNAELTTVmsNSFGFGGTNATLVF 401
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-122 |
4.80e-11 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 65.52 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFW--ENCPrlqplTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKP 78
Cdd:PRK08439 292 IDYINAHGTSTPYNDKNETAALKELFGskEKVP-----PVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETP 366
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1489830778 79 NP-C----IPwNKfpiiipqsqmpwLRGEKPRLAGVSSFGFSGTNAHVV 122
Cdd:PRK08439 367 DPeCdldyIP-NV------------ARKAELNVVMSNSFGFGGTNGVVI 402
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1-124 |
1.58e-10 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 63.90 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEvfwencPRLQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPnp 80
Cdd:PRK07103 301 IDYVNPHGTGSPLGDETELAALFA------SGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEP-- 372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1489830778 81 cipwnkfpiIIPQSQmpWLrGEKPRLAGV-----SSFGFSGTNAHVVLE 124
Cdd:PRK07103 373 ---------IDERFR--WV-GSTAESARIryalsLSFGFGGINTALVLE 409
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-123 |
4.94e-09 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 59.09 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPrlqpltIGSAKTNIGHLEAAAGVAGLVKVVLALQHQeIPPH-LHFSKPN 79
Cdd:PRK09185 280 IGYINLHGTATPLNDAMESRAVAAVFGDGVP------CSSTKGLTGHTLGAAGAVEAAICWLALRHG-LPPHgWNTGQPD 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1489830778 80 PCIPwnkfPIIIPQSQmpwlRGEKPRLAGVSSFGFSGTNAHVVL 123
Cdd:PRK09185 353 PALP----PLYLVENA----QALAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
1-124 |
6.00e-09 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 58.59 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENcprlQPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PRK14691 226 VQHLNAHATSTPVGDLGEINAIKHLFGES----NALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDP 301
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1489830778 81 CIpwnKFPIIIPQSQMPwlrgEKPRLAGVSSFGFSGTNAHVVLE 124
Cdd:PRK14691 302 AA---KGLNIIAGNAQP----HDMTYALSNGFGFAGVNASILLK 338
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-123 |
9.88e-09 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 58.14 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPrlqpltIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNp 80
Cdd:PRK05952 274 IDYIHAHGTATRLNDQREANLIQALFPHRVA------VSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE- 346
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1489830778 81 cipwnkFPIIIPQsqmpwlrgeKPRLAGVS-----SFGFSGTNAHVVL 123
Cdd:PRK05952 347 ------FDLNFVR---------QAQQSPLQnvlclSFGFGGQNAAIAL 379
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1-123 |
7.64e-08 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 55.76 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENcPRLQpltIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PLN02787 425 VNYINAHATSTKAGDLKEYQALMRCFGQN-PELR---VNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPES 500
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1489830778 81 CIPWNKFpiiipqsqmpwLRGEKPRL----AGVSSFGFSGTNAHVVL 123
Cdd:PLN02787 501 GVDTKVL-----------VGPKKERLdikvALSNSFGFGGHNSSILF 536
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1-125 |
1.23e-07 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 54.62 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPRlqPLTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PRK08722 298 IGYVNAHGTSTPAGDVAEIKGIKRALGEAGSK--QVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEE 375
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1489830778 81 CIPWNKFPIIIPQSqmpwlrgEKPRLAGVSSFGFSGTNAHVVLEE 125
Cdd:PRK08722 376 GLDIDLVPHTARKV-------ESMEYAICNSFGFGGTNGSLIFKK 413
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
1-83 |
5.26e-06 |
|
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: 49.67 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWencPRLQPLTIgsAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:cd00832 290 VDVVFADAAGVPELDRAEAAALAAVFG---PRGVPVTA--PKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPP 364
|
...
gi 1489830778 81 CIP 83
Cdd:cd00832 365 AYG 367
|
|
| PT_fungal_PKS |
TIGR04532 |
iterative type I PKS product template domain; Sequences found by this model are the so-called ... |
610-689 |
1.72e-05 |
|
iterative type I PKS product template domain; Sequences found by this model are the so-called product template (PT) domain of various fungal iterative type I polyketide synthases. This domain resembles pfam14765, designated polyketide synthase dehydratase by Pfam, but members of that family are primarily bacterial, where type I PKS are predominantly modular, not iterative. The dehydratase active site residues well-conserved in pfam14765 (His in the first hot dog domain, Asp in the second hot dog domain) seem well conserved in this family also.
Pssm-ID: 275325 Cd Length: 324 Bit Score: 47.62 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 610 HQIRFESQISAKAP----AYLSH---------HQVFGKPLLPAAAYLEMALAAGSTLFQ---------IEGLMLEDVVIQ 667
Cdd:TIGR04532 5 HRVVEETSDGSKATvvfeSDLSDpdllaaiqgHRVNGVPLCPSSVYADMALTAAKYLLKrlrgskdaaDVGLDVRDMEVD 84
|
90 100
....*....|....*....|..
gi 1489830778 668 QGLILSEEEAKTVQVILTISET 689
Cdd:TIGR04532 85 KPLVADPSDSDPQLLRVTATAD 106
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
1-118 |
4.49e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 46.65 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPrlqplTIGSAKTNIGHLEAAAGVAGLVKVVLALQHQEIPPHLHFSKPNP 80
Cdd:PRK07910 306 IDHVNAHATGTSVGDVAEGKAINNALGGHRP-----AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDP 380
|
90 100 110
....*....|....*....|....*....|....*...
gi 1489830778 81 CIpwnKFPIIIPQSqmpwlRGEKPRLAGVSSFGFSGTN 118
Cdd:PRK07910 381 EI---DLDVVAGEP-----RPGNYRYAINNSFGFGGHN 410
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-53 |
1.62e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 41.51 E-value: 1.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1489830778 1 VSYIEAHGTGTRLGDPVEVEALGEVFWENCPrlqpltIGSAKTNIGHLEAAAG 53
Cdd:PRK09116 295 IGYVNAHGTATDRGDIAESQATAAVFGARMP------ISSLKSYFGHTLGACG 341
|
|
| |
