|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-394 |
2.02e-152 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 435.87 E-value: 2.02e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRASKASL-ELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGQVMSAAFSAADLNLGPIPATR 79
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVSLrDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIAALIADYAGLAPIPATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 80 YEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFATRTFAMACHAPTEGPVGLTFPAVFAMAAMRYAKNYDI 159
Cdd:PRK06064 81 VEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAGDYEWEEFFGATFPGLYALIARRYMHKYGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 160 PleklREKMAHVSIKNHKHGALNPLAQFYKKLgalKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEARKYTDEP 239
Cdd:PRK06064 161 T----EEDLALVAVKNHYNGSKNPYAQFQKEI---TVEQVLNSPPVADPLKLLDCSPITDGAAAVILASEEKAKEYTDTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 240 VYILGTGQGSGGP-LSKMEDLTKPVSRISSAKAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMGFFDWGEAADAVEEG 318
Cdd:PRK06064 234 VWIKASGQASDTIaLHDRKDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAKKGEGGKLAREG 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904408614 319 QTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAKGNQIDPVPEYGMTDTLGGDFGTLCHIILGRSK 394
Cdd:PRK06064 314 QTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAEKGRQQVIGAGYGLTHNVGGTGHTAVVHILSRKR 389
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
7-389 |
1.53e-122 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 359.27 E-value: 1.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 7 IGIGHTKFGRASKAS-LELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGqvMSAAFSAADLNLGPIPATRYEGACA 85
Cdd:cd00829 1 VGVGMTPFGRRSDRSpLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQS--FPGALIAEYLGLLGKPATRVEAAGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 86 SASIAIRDAAMWVGSGEYDMVIAGGMEK--ALTMGTLFATRTFAMAcHAPTEGPVGLTFPAVFAMAAMRYAKNYDIPlek 163
Cdd:cd00829 79 SGSAAVRAAAAAIASGLADVVLVVGAEKmsDVPTGDEAGGRASDLE-WEGPEPPGGLTPPALYALAARRYMHRYGTT--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 164 lREKMAHVSIKNHKHGALNPLAQFYKKLgalKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEARKYTDEPVYIL 243
Cdd:cd00829 155 -REDLAKVAVKNHRNAARNPYAQFRKPI---TVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTDRPVWIL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 244 GTGQGSGGP-LSKMEDLTKPVSRISSAKAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMGFFDWGEAADAVEEGQTEL 322
Cdd:cd00829 231 GVGAASDTPsLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREGDTAI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904408614 323 GGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEaAKGNQIdPVPEYGMTDTLGGDFGTLCHII 389
Cdd:cd00829 311 GGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGE-AGARQV-PGARVGLAHNIGGTGSAAVVTI 375
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
1-392 |
2.03e-95 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 290.78 E-value: 2.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFG-RASKASLELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGqvMSAAFSAADLNLGPIPATR 79
Cdd:PRK06157 6 KDKVAILGMGCTKFGeRWDAGAEDLMVEAFLEALADAGIEPKDIDAAWFGTHYDEIGSG--KSGTPLSRALRLPNIPVTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 80 YEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKalTMGTLFATRTFAmacHAPTEGP---VGLTFPAVFAMAAMRYAKN 156
Cdd:PRK06157 84 VENFCATGSEAFRGAVYAVASGAYDIALALGVEK--LKDTGYGGLPVA---NPGTLADmtmPNVTAPGNFAQLASAYAAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 157 YDIPLEKLREKMAHVSIKNHKHGALNPLAQFYKklgALKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEARKYT 236
Cdd:PRK06157 159 YGVSREDLKRAMAHVSVKSHANGARNPKAHLRK---AVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARALG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 237 D-EPVYI------LGTGQGSGGPlsKMEDLTKPVSRISsAKAAFKQAGLT-P-KDIDLVEVHDCFTIAELIALECMGFFD 307
Cdd:PRK06157 236 KkDPVYVkalqlaVSNGWELQYN--GWDGSYFPTTRIA-ARKAYREAGITdPrEELSMAEVHDCFSITELVTMEDLGLSE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 308 WGEAADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAKgNQIDPvPEYGMTDTLGG-DFGTLC 386
Cdd:PRK06157 313 RGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGE-RQLKN-PRLALTHNLGGaPGQNVC 390
|
....*..
gi 1904408614 387 HI-ILGR 392
Cdd:PRK06157 391 SVsIVGR 397
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
2-380 |
1.16e-86 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 267.87 E-value: 1.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 2 RDVAIIGIGHTKFGRASKASL-ELFSESVLQAIDDAGVELKDIEALFQG-AALAGFEegqVMSAAFSAADLNL---GPIp 76
Cdd:PRK12578 1 RRVAVIGVGNSKFGRRDDVSVqELAWESIKEALNDAGVSQTDIELVVVGsTAYRGIE---LYPAPIVAEYSGLtgkVPL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 77 atRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKaltMGTLFATRTFAMACHAPTE----GPVGLTFPAVFAMAAMR 152
Cdd:PRK12578 77 --RVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDK---MTEVDTSTSLAIGGRGGNYqweyHFYGTTFPTYYALYATR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 153 YAKNYDIPleklREKMAHVSIKNHKHGALNPLAQFYKKLgalKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEA 232
Cdd:PRK12578 152 HMAVYGTT----EEQMALVSVKAHKYGAMNPKAHFQKPV---TVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 233 RKY-TDEPVYILGTGQGSG-GPLSKMEDLTKPVSRISSAKAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMGFFDWGE 310
Cdd:PRK12578 225 KELkIDSPVWITGIGYANDyAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKGK 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904408614 311 AADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAKGNQidPVPEY-GMTDTLGG 380
Cdd:PRK12578 305 GGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQ--PLKKYiGLVHNVGG 373
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-360 |
2.25e-80 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 251.79 E-value: 2.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRASKASLE-LFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGQVMSAAFSAADLNLGPIPATR 79
Cdd:PRK07516 1 MMTASIVGWAHTPFGKLDAETLEsLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDFPASLVLQADPALRFKPATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 80 YEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFATRTFAMACHAPTEGPVGLTFPAVFAMAAMRYAKNYDI 159
Cdd:PRK07516 81 VENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTAEVGDILLGASYLKEEGDTPGGFAGVFGRIAQAYFQRYGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 160 PLEKLrekmAHVSIKNHKHGALNPLAQFYKKLGALKLEEVIDSK-MVADPLSLLDCCPFSDGASALVLCAAEEARKyTDE 238
Cdd:PRK07516 161 QSDAL----AMIAAKNHANGVANPYAQMRKDLGFEFCRTVSEKNpLVAGPLRRTDCSLVSDGAAALVLADAETARA-LQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 239 PVYILGTGQGSGG-PLSKMEDLTKPVSRISSAKAaFKQAGLTPKDIDLVEVHDCFTIAELIALECMGFFDWGEAADAVEE 317
Cdd:PRK07516 236 AVRFRARAHVNDFlPLSRRDPLAFEGPRRAWQRA-LAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPGQGARAIRE 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1904408614 318 GQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEA 360
Cdd:PRK07516 315 GWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEA 357
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
2-362 |
7.29e-67 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 217.07 E-value: 7.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 2 RDVAIIGIGHTKFGR--ASKASLELFSESVLQAIDDAGVELKDIEAlfqgaALAGFEEGQVMSAAFSAADLNLGPIPATR 79
Cdd:PRK08256 1 NKVFVAGVGMTPFEKpgASWDYPDMAAEAGRAALADAGIDYDAVQQ-----AYVGYVYGDSTSGQRALYEVGMTGIPIVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 80 YEGACASASIAIRDAAMWVGSGEYDMVIAGGMEK----ALtmGTLFATRTFAMACH--------APTEGPVGLTFpavFA 147
Cdd:PRK08256 76 VNNNCSTGSTALFLARQAVRSGAADCALALGFEQmqpgAL--GSVWDDRPSPLERFdkalaelqGFDPAPPALRM---FG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 148 MAAMRYAKNYDIPLEKLrekmAHVSIKNHKHGALNPLAQFYKklgALKLEEVIDSKMVADPLSLLDCCPFSDGASALVLC 227
Cdd:PRK08256 151 GAGREHMEKYGTTAETF----AKIGVKARRHAANNPYAQFRD---EYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 228 AAEEARKY-TDEPVYILGTGQGSGGPLS-KMEDLTKPVSRISSAKAA---FKQAGLTPKDIDLVEVHDCFTIAELIALEC 302
Cdd:PRK08256 224 SEEFARKHgLDRAVEIVAQAMTTDTPSTfDGRSMIDLVGYDMTRAAAqqvYEQAGIGPEDIDVVELHDCFSANELLTYEA 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 303 MGFFDWGEAADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAK 362
Cdd:PRK08256 304 LGLCPEGEAEKFIDDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGA 363
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
1-362 |
5.89e-62 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 205.53 E-value: 5.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRAS--KASLELFSESVLQAIDDAGVELKDIEAlFQGAALAGFEEGQVMSAAFSAADLNLGPIPAT 78
Cdd:PRK06365 15 SRDVYMVAAGVTKFDKASpyMDFRERVKKAFDYAMNDAGLTLADIDG-SVASYFSDHFQRQLLAGIMVQDYLGLVPKPSK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 79 RYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFATRTFAMACHAPTEGPVGLTFPAVFAMAAMRYAKNYD 158
Cdd:PRK06365 94 RIEGGGATGGLAFQAGYEEIASGRMDCVAVYGFETMSHVNTWKGNEFIALASDTNFDYPLGGFYTGYYAMMAVRHMYEFG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 159 ipleKLREKMAHVSIKNHKHGALNPLAQFYKKLgalKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEARKYTDE 238
Cdd:PRK06365 174 ----TTVEQLAKVSVKNHGNAIHNPFAQSPMKI---TVEDVRKSPMVSYPLTRLDVCAMSDGAACAILASEDKAFEITDK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 239 PVYILGTGQGSGG-----------PL------SKMEDLTKP------VSRISsAKAAFKQAGLTP--KDIDLVEVHDCFT 293
Cdd:PRK06365 247 PVLIKAIGTGSDTlrladrpfgevPLlpnespDDYKDLRYPgvhsfrAGRMA-AKEAYEMAGITDplNDLDLIELHDAYT 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904408614 294 IAELIALECMGFFDWGEAADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAK 362
Cdd:PRK06365 326 SSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQGRIKK 394
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
4-361 |
1.29e-54 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 184.85 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 4 VAIIGIGHTKFGRA-SKASLELFSESVLQAIDDAGVELKDIEALFQGAALAGFeegQVMSAAfsaADLNLGP--IPATRY 80
Cdd:PRK06158 10 TAIVGAATAGLGEApGLSAMELLAQAAHRALADAGLTMADVDGLFTASPDDAL---WGLSVA---EYLGIRPrfVDGTMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 81 EGACASASIAIrdAAMWVGSGEYDMV-IAGGMEKALTMGTLFAtrtfaMACHAPTEGPVGLTFPA-VFAMAAMRYAKNYD 158
Cdd:PRK06158 84 GGSSFLAHLLP--AALALEAGLCDVAlICYGSNQRSAGGKLRS-----MLDPQPYEAPYKPVNPVsAYALAAARHMHQYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 159 IPleklREKMAHVSIKNHKHGALNPLAqfYKKlGALKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEARKYTDE 238
Cdd:PRK06158 157 TT----REQLAEVAVAARQWAQLNPEA--FMR-DPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMVRADRARDLPRP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 239 PVYILGTGQGSG-GPLSKMEDLTKPVSRISSAKAaFKQAGLTPKDIDLVEVHDCFTIAELIALECMGFFDWGEAADAVEE 317
Cdd:PRK06158 230 PVYVLGAAAATWhRQISSMPDLTVTAAAESGPRA-FAMAGLTPADIDVVELYDAFTINTILFLEDLGFCAKGEGGAFVEG 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1904408614 318 GQTELGGEIPVNMSGGLIGKGHPiGATGASQIYWIIKQMRGEAA 361
Cdd:PRK06158 309 GRIAPGGRLPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAG 351
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
5-369 |
3.90e-54 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 183.64 E-value: 3.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 5 AIIGIGHTKFGRASKAS-LELFSESVLQAIDDAGVELKDIEALfqgAALAGFEEGQVMSA-AFSAADLN-LGPIPatrYE 81
Cdd:PRK07855 7 AIVGIGATEFSKNSGRSeLRLACEAVLAALDDAGLAPSDVDGL---VTFTMDTNPEIAVArALGIGELKfFSRIH---YG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 82 GACASASIAirDAAMWVGSGEYDMVIA--------GGMEKALTMGtlFATRTFAMACHAPTEGPVGLTFPAVF-AMAAMR 152
Cdd:PRK07855 81 GGAACATVQ--QAAMAVATGVADVVVCyrafnersGMRFGQGQTG--LAENPTSTGVDYGWSYPHGLLTPAAWvAMLARR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 153 YAKNYDIPleklREKMAHVSIKNHKHGALNPLAQFYKKlgALKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEA 232
Cdd:PRK07855 157 YMHEYGAT----SEDFGRVAVADRKHAATNPKAWFYGR--PITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 233 RKYTDEPVYILGTGQGSGGPLSKM-----EDLTKPVSRISSAKAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMGFFD 307
Cdd:PRK07855 231 RDLKQRPAVIKAAAQGSGADQYMMtsyyrDDITGLPEMGLVARQLWAQSGLGPADIDTAILYDHFTPFVLMQLEELGFCG 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1904408614 308 WGEAADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQiywIIKQMRGEAAkgNQIDPV 369
Cdd:PRK07855 311 RGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGIAE---AVRQLRGTSV--NQVPGV 367
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
1-360 |
6.96e-53 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 181.04 E-value: 6.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGR----ASKASLELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGQ-VMSAAFSAADLNLGPI 75
Cdd:PRK06289 2 SDDVWVLGGYQSDFARnwtkEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGELFAGQgHLGAMPATVHPALWGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 76 PATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFATRTFAMACHAPTEGP-VGLTFPAVFAMAAMRYA 154
Cdd:PRK06289 82 PASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVPGDVAAEHLGAAAWTGHEGQdARFPWPSMFARVADEYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 155 KNYDIPLEKLREkmahVSIKNHKHGALNPLAQ----FYKKLGALKLEEVidSKMVADPLSLLDCCPFSDGASALVLCAAE 230
Cdd:PRK06289 162 RRYGLDEEHLRA----IAEINFANARRNPNAQtrgwAFPDEATNDDDAT--NPVVEGRLRRQDCSQVTDGGAGVVLASDA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 231 EARKYTDEPVY--ILGTGQGSGGPL-------SKMEDLTKPVSRiSSAKAAFKQAGLTPKDIDLVEVHDCFTIAELIALE 301
Cdd:PRK06289 236 YLRDYADARPIprIKGWGHRTAPLGleqkldrSAGDPYVLPHVR-QAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAID 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1904408614 302 CMGFFDWGEAADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEA 360
Cdd:PRK06289 315 HIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTA 373
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
1-392 |
6.49e-52 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 178.42 E-value: 6.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRASKASLELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGQVMSAAFSAAdLNLGPIPATRY 80
Cdd:PRK06059 3 PEPVYILGAGMHPWGKWGRDFVEYGVVAARAALADAGLDWRDVQLVVGADTIRNGYPGFVAGATFAQA-LGWNGAPVSSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 81 EGACASASIAIRDAAMWVGSGEYDMVIAGGmekALTMGTLFatrtFAMACHAPTEGP-------VGLTFPAVFAMAAMRY 153
Cdd:PRK06059 82 YAACASGSQALQSARAQILAGLCDVALVVG---ADTTPKGF----FAPVGGERPDDPdwlrfhlIGATNPVYFALLARRR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 154 AKNYDIPLEKLrekmAHVSIKNHKHGALNPLAQFYKKLGAlklEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEAR 233
Cdd:PRK06059 155 MDLYGATVEDF----AQVKVKNARHGLLNPNARYRKEVTV---EDVLASPVVSDPLRLLDICATSDGAAALIVASKSFAR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 234 KYT---DEPVYI----LGTGQgSGGPLSKMEDLTKPVS----------RISSAKAAFKQAGLTPKDIDLVEVHDCFTIAE 296
Cdd:PRK06059 228 RHLgsvAGVPSVraisTVTPR-YPQHLPELPDIATDSTaavpapervfKDQILDAAYAEAGIGPEDLSLAEVYDLSTALE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 297 LIALECMGFFDWGEAADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAkGNQIdPVPEYGMTD 376
Cdd:PRK06059 307 LDWYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAG-GRQV-EGARVGITA 384
|
410
....*....|....*.
gi 1904408614 377 TLgGDFGTLCHIILGR 392
Cdd:PRK06059 385 NQ-GLFGHGSSVIVAR 399
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
2-369 |
6.96e-51 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 175.40 E-value: 6.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 2 RDVAIIGIGHTKF-GRASKASLELFSESVLQAIDDAGVELKDIEALFQGAALAGFEeGQVMSAAFSAADLNLGPIPATR- 79
Cdd:PRK06065 9 KRVAVIGAGLTLFrRRLLETPQELAWEAASKALDEAGLELKDIDCVVIGSAPDAFD-GVHMKGEYLSHGSGGIRKPVSRv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 80 YEGACASASIAIrdAAMW-VGSGEYDMVIAGGMEKaLTMGTLFATRTFAMACHAPTEGPVGLTFPAVFAMAAMRYAKNYD 158
Cdd:PRK06065 88 YVGGATGVMTAI--AGWYhVASGLCQKVLAVAEEK-MSPARPHPQAVFRYIWDPILEKPLNPNLIWIFAMEMHRYMATYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 159 IPleklREKMAHVSIKNHKHGALNPLAQFYKKLgalKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEARKYTDE 238
Cdd:PRK06065 165 IK----KEEIALVSVKNKRNALNNPYAQLGSKI---TVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRYTDT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 239 PVYILGTGQGSGGPLSKMEDLTKPVSRISSAKAAFKQAGLTP--KDIDLVEVHDCFTIAELIALECMGFFDWGEAADAVE 316
Cdd:PRK06065 238 PVWVEGVGWTLDNTEWPNRDLAYPRYVEFAARMAYKMAGIERprKEIDVAEPYDPFDYKELHHLEGLQLAKRGEAPKLLK 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1904408614 317 EGQTELGGEIPVNMSGGLIGKGHPIGATG---ASQIYWiikQMRGEAAKGNQIDPV 369
Cdd:PRK06065 318 EGVFDIDGDIPSSPSGGLLGVGNPIAAAGlmkVISIYW---QLKGTAGKMQVKKPV 370
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
11-381 |
1.17e-49 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 173.54 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 11 HTKFGRASKASLE-LFSESVLQAIDDAGVELKD--IEALFQGAALAGF--EEGQVMSAAF-----SAADLNLGPIPATRY 80
Cdd:PTZ00455 37 HPDFGKKENKTLEeLLATAIQGTLENTGLDGKAalVDKVVVGNFLGELfsSQGHLGPAAVgslgqSGASNALLYKPAMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 81 EGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFATRTFAMACHAPTEGPVG-LTFPAVFAmAAMRYAKNYDi 159
Cdd:PTZ00455 117 EGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVGGDYLARAADYRRQRKLDdFTFPCLFA-KRMKYIQEHG- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 160 plEKLREKMAHVSIKNHKHGALNPLAQFYKKlgALKLEEVIDS-----KMVADP-----LSLLDCCPFSDGASALVLCAA 229
Cdd:PTZ00455 195 --HFTMEDTARVAAKAYANGNKNPLAHMHTR--KLSLEFCTGAsdknpKFLGNEtykpfLRMTDCSQVSDGGAGLVLASE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 230 EEARKYTDEP-----VYILGTGQGSGGPLSKMEDLTKPVSRISSAKAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMG 304
Cdd:PTZ00455 271 EGLQKMGLSPndsrlVEIKSLACASGNLYEDPPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALG 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904408614 305 FFDWGEAADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAKgNQIDPVPEYGMTDTLGGD 381
Cdd:PTZ00455 351 IAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGE-YQMKNIPALGATLNMGGD 426
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
1-360 |
2.68e-46 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 162.98 E-value: 2.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKF-GRASKASL-ELFSESVLQAIDDAGVELKDIEALFQGAAlAGFEEGQVMSAAFSAADLNLGPIPAT 78
Cdd:PRK08313 2 KRLAAVLGTGQTKYvAKRQDVSMaGLVREAIDRALADAGLTWDDIDAVVVGKA-PDFFEGVMMPELFLADALGATGKPLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 79 R-YEGACASASIAIRdAAMWVGSGEYDMVIAGGMEKALTmgtlfATRTFAMACHAPTEGPVGLTFPAVFAMAAMRYAKNY 157
Cdd:PRK08313 81 RvHTAGSVGGSTAVV-AASLVQSGVYRRVLAVAWEKQSE-----SNAMWALSIPVPFTKPVGAGAGGYFAPHVRAYIRRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 158 DIPLEKlrekMAHVSIKNHKHGALNPLAQFYKKlgALKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEARKYTD 237
Cdd:PRK08313 155 GAPEHI----GAMVAVKDRLNGAKNPYAHLHQP--DITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 238 EPV-YILGTGQGSGGPLSKMEDLTKPVSRISSAKAAFKQAGLTP--KDIDLVEVHDCFTIAELIALECMGFFDWGEAADA 314
Cdd:PRK08313 229 RPVaWIHGTAMRTEPLAFAGRDQVNPQAGRDAAAALWKAAGITDprDEIDVAEIYVPFSWFEPMWLENLGFAPEGEGWKL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1904408614 315 VEEGQTELGGEIPVNMSGGLIGkGHPIGATGASQIYWIIKQMRGEA 360
Cdd:PRK08313 309 TEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKA 353
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
1-362 |
1.94e-41 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 150.29 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFgRASKASL---ELFSESVLQAIDDAGV--ELKDIEALFQGAAlaGFEEGQVMSAAFsAADlnlgPI 75
Cdd:PRK06066 3 LNRVAIVGIGWYGF-RPTTPEVsfrEMMFEAASRAYKDAGNinPRRDVDSFISCQE--DFWEGIAIADEF-APD----QI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 76 -PATRYEGACASASI-AIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFATRTFAM-ACHAPTEGPVGLTFPAvfAMAAMR 152
Cdd:PRK06066 75 gGAMRPTMTVAGDGLqGLAHAVMHINSGLANVVVVEAHSKPSDILTFSDVVKFAMdPIYVRPIGPPNPHFIA--GLDAVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 153 YAKNYDIPleklREKMAHVSIKNHKHGALNPLAQFYKKLgalKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEA 232
Cdd:PRK06066 153 FMSRKGIT----REDLALVVEKNKKAGLSNPRASYASNI---SLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 233 RKYTDEPVYILGTGQGSGGPLSKMEDLTKPVSRISSAKAAFKQAGLTP--KDIDLVEVHDCFTIAELIALECMGFFDWGE 310
Cdd:PRK06066 226 KKLTDDPVWIKGIGWSTESSNLETAELGKANYMRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPE 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1904408614 311 AADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAK 362
Cdd:PRK06066 306 KDSLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGA 357
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
19-366 |
2.39e-41 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 149.85 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 19 KASLELFSESVLQAIDDAGVELKDIEALFQGAALAGFeegqvmsAAFSAAD---LNLGPIPATRYEGACASASIAIRDAA 95
Cdd:PRK08142 23 KSVAQLHAEVAKGALADAGLSLADVDGYFCAGDAPGL-------GPASMVDylgLKLRHVDSTETGGSSYLAHVGHAAQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 96 MWVGSGEYDMVIAGGMEKALTMGTLFATRTFAMACHAPTEGPVGLTFPAVFAMAAMRYAKNYDIPLEKLrekmAHVSIKN 175
Cdd:PRK08142 96 IAAGKCSVALITLAGRPRSEGSSGTEPRNWGADAPDAPFEAPYGPTTHNLYAMCAMRHMHEYGTTSEQL----AWIKVAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 176 HKHGALNPLAQFYKklgALKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEARKYTDEPVYILGTGQGSGGPLSK 255
Cdd:PRK08142 172 SHHAQHNPHAMLRD---VVTVEDVLNSPMIADPLHRLDCCVVTDGGGALVVVRPEIARSLKRPLVKVLGAGEAIKGQMGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 256 MEDLTKPVSRISSAkAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMGFFDWGEAADAVEEGQTELG-GEIPVNMSGGL 334
Cdd:PRK08142 249 KVDLTYSGAAWSGP-AAFAEAGVTPADIKYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGG 327
|
330 340 350
....*....|....*....|....*....|..
gi 1904408614 335 IGKGHPIGATGASQIYWIIKQMRGEAAKGNQI 366
Cdd:PRK08142 328 LCNNHPANRGGMTKVIEAVRQLRGEAHPAVQV 359
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-362 |
9.83e-34 |
|
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238422 [Multi-domain] Cd Length: 393 Bit Score: 129.54 E-value: 9.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 7 IGIGHTKFGR--------ASKASLELFSESVLQAIDDAGVELKDIEALFQGAALAgfeEGQVMSAAFSAADLNLGP--IP 76
Cdd:cd00826 1 AGAAMTAFGKfggengadANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLG---AGEGQNCAQQAAMHAGGLqeAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 77 ATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFATRTFAMACHAPTEGPVGLTFPAVFAMAAMRYAKN 156
Cdd:cd00826 78 AIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAEAAEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 157 YDipleKLREKMAHVSIKN---HKHGALNPLAQFYKKLgalKLEEVIDSKMVADP---LSLLDCCPFSDGASALVLCAAE 230
Cdd:cd00826 158 DG----RFKDEFAKFGVKGrkgDIHSDADEYIQFGDEA---SLDEIAKLRPAFDKedfLTAGNACGLNDGAAAAILMSEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 231 EARKYTDEP-----------VYILGTGQGSGGPLSKMEDLTKPVSRissakAAFKQAGLTPKDIDLVEVHDCFTIAELIA 299
Cdd:cd00826 231 EAQKHGLQSkareiqalemiTDMASTFEDKKVIKMVGGDGPIEAAR-----KALEKAGLGIGDLDLIEAHDAFAANACAT 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1904408614 300 LECMGFFDWGEAADAVEEGQTELGGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAK 362
Cdd:cd00826 306 NEALGLCPEGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGK 368
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-230 |
4.15e-24 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 100.07 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 4 VAIIGIGHTKFGR-----ASKASLELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGQVMSAAFSAADLNLgPIPAT 78
Cdd:pfam00108 1 VVIVSAARTPFGSfggslKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPD-SAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 79 RYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFATRTFAMACHaPTEGPVGLTFPAVFA---------MA 149
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKH-GDEKKHDLLIPDGLTdafngyhmgLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 150 AMRYAKNYDIPleklREKMAHVSIKNHKHGALNPLAQFYKK------------LGALKLEEVIDSKMVADPLSLL----- 212
Cdd:pfam00108 159 AENVAKKYGIS----REEQDAFAVKSHQKAAAAPKAGKFKDeivpvtvkgrkgKPTVDKDEGIRPPTTAEPLAKLkpafd 234
|
250 260
....*....|....*....|....*.
gi 1904408614 213 --------DCCPFSDGASALVLCAAE 230
Cdd:pfam00108 235 kegtvtagNASPINDGAAAVLLMSES 260
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
1-362 |
1.15e-21 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 95.14 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRASKAS---LELFSESVLQAIDDAGVELKDIEALFQGAA--LAGfeegqvmsAAFS--AADLNLG 73
Cdd:PRK07937 1 MRDVAVVGFAQAPHVRRTDGTtngVEMLMPCFAELYAELGITKSDIGFWCSGSSdyLAG--------RAFSfiSAIDSIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 74 PIPATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKAlTMGTLfaTRTFAMACHAPTEGPVGltfPAVFAMAAMRY 153
Cdd:PRK07937 73 AVPPINESHVEMDAAWALYEAWVKLLTGEVDTALVYGFGKS-SAGTL--RRVLALQLDPYTVAPLW---PDSVSMAGLQA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 154 AKNYDIPLEKlREKMAHVSIKNHKHGALNPLAQfykklGALKLEEVIDSKMVADPLSLLDCCPFSDGASALVLCAAEEAR 233
Cdd:PRK07937 147 RAGLDAGKWT-EEQMAEVAARSRADARRNPSAE-----PSISVDELLARPYFADPLRRHDIAPITDGAAAVVLAAGDRAR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 234 KYTDEPVYILGTGQGSGGPLSKMEDLTKPVSRISSAKAAfkqAGLTPKDIDLVEVHDCFTIAELIALECMGffdwgeaad 313
Cdd:PRK07937 221 ELRERPAWITGIEHRIESPSLGARDLTRSPSTALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALG--------- 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1904408614 314 aveegqteLGGEIPVNMSGGLIgKGHPIGATGASQIywiikqmrGEAAK 362
Cdd:PRK07937 289 --------LGDKTKVNPSGGAL-AANPMFAAGLERI--------GEAAR 320
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-386 |
1.32e-19 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 89.78 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRASKASL-----------ELFSESVLQAIDDAGVELKDIEALFQGAALAGFEE----GQVmsAAF 65
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKDPqkdvfnnirpeELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwlygGRH--PIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 66 SAadlNLGP-IPATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKA--LTMG--------TLFATRTFAMACHAPT 134
Cdd:PRK06445 79 LA---RLPYnIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMtrTPMGdnphiepnPKLLTDPKYIEYDLTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 135 EGPVGLTFPAVFAMAAMRyaknydipleklREKMAHVSIKNHKHGAlNPLAQFYKKLGALKLEEVID-SKMVAD------ 207
Cdd:PRK06445 156 GYVMGLTAEKLAEEAGIK------------REEMDRWSLRSHQLAA-KAIQEGYFKDEILPIEVEVEgKKKVVDvdqsvr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 208 PLSLLD-------------------CCPFSDGASALVLCAAEEARKYTDEPVYILGTGQGSGGPLSKMEDLTKPVSRiss 268
Cdd:PRK06445 223 PDTSLEklaklppafkpdgvitagnSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASK--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 269 akAAFKQAGLTPKDIDLVEVHDCFTIAELIALEcmgffdwgeaadaveegqtELG-GEIPVNMSGGLIGKGHPIGATGAS 347
Cdd:PRK06445 300 --KALEKAGLSVKDIDLWEINEAFAVVVLYAIK-------------------ELGlDPETVNIKGGAIAIGHPLGATGAR 358
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1904408614 348 QIYWIIKQMrgeaakgnQIDpvpeygmtdtlGGDFG--TLC 386
Cdd:PRK06445 359 IVGTLARQL--------QIK-----------GKDYGvaTLC 380
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
12-346 |
2.95e-18 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 85.61 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 12 TKFGRASKA-----SLELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGQVMSAAFSAADLNLgPIPATRYEGACAS 86
Cdd:cd00751 8 TPIGRFGGAlkdvsADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPE-SVPATTVNRVCGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 87 ASIAIRDAAMWVGSGEYDMVIAGGMEkalTMGT----LFATRTFAMACHAPTEGPV--GLTFPAV-FAM--AAMRYAKNY 157
Cdd:cd00751 87 GLQAVALAAQSIAAGEADVVVAGGVE---SMSRapylLPKARRGGRLGLNTLDGMLddGLTDPFTgLSMgiTAENVAEKY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 158 DIPleklREKMAHVSIKNHKhgalnpLAQFYKKLGALKLEEV---IDSKMVADPLSLLDC-------------------- 214
Cdd:cd00751 164 GIS----REEQDEFALRSHQ------RAAAAQEAGRFKDEIVpveVPGRKGPVVVDRDEGprpdttleklaklkpafkkd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 215 --------CPFSDGASALVLCAAEEARKYTDEP-VYILGTGQGSGGPlSKMedLTKPVSrisSAKAAFKQAGLTPKDIDL 285
Cdd:cd00751 234 gtvtagnaSGINDGAAAVLLMSEEKAKELGLKPlARIVGYAVAGVDP-AIM--GIGPVP---AIPKALKRAGLTLDDIDL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904408614 286 VEVHDCFTIaelIALECMGFFDWGEAAdaveegqtelggeipVNMSGGLIGKGHPIGATGA 346
Cdd:cd00751 308 IEINEAFAA---QALACLKELGLDPEK---------------VNVNGGAIALGHPLGASGA 350
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
23-357 |
3.71e-18 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 85.36 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 23 ELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGQVMSAAFSAADLNLGpIPATRYEGACASASIAIRDAAMWVGSGE 102
Cdd:TIGR01930 23 DLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPES-VPAYTVNRQCASGLQAVILAAQLIRAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 103 YDMVIAGGMEkalTMGT--------------LFATRTFAMACHAPTEGPVGLtfpaVFAMAAMRYAKNYDIPleklREKM 168
Cdd:TIGR01930 102 ADVVVAGGVE---SMSRvpygvprslrwgvkPGNAELEDARLKDLTDANTGL----PMGVTAENLAKKYGIS----REEQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 169 AHVSIKNHKhgalnpLAQFYKKLGALKLE----EVIDSKMV--------------ADPLSLL-------------DCCPF 217
Cdd:TIGR01930 171 DEYALRSHQ------RAAKAWEEGLFKDEivpvTVKGRKGPvtvssdegirpnttLEKLAKLkpafdpdgtvtagNSSPL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 218 SDGASALVLCAAEEARKYTDEPVYILGTGQGSGGPLSKMedltkPVSRISSAKAAFKQAGLTPKDIDLVEVHDCFtiael 297
Cdd:TIGR01930 245 NDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIM-----GLGPVPAIPKALKKAGLSISDIDLFEINEAF----- 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904408614 298 iALECMGFfdwgeaadaveegQTELG-GEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMR 357
Cdd:TIGR01930 315 -AAQVLAC-------------IKELGlDLEKVNVNGGAIALGHPLGASGARIVTTLLHELK 361
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-357 |
9.21e-15 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 75.05 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHT---KFGRA-SK-ASLELFSESVLQAIDDAGVELKDIEALFQGAAL-AGFEEGQVMSAAFSAADlnlgP 74
Cdd:PRK06366 1 MKDVYIVSAKRTaigKFGRSfSKiKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIqAGVGQNPAGQAAYHAGL----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 75 IPATRY--EGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLFAT-----------RTFAMACHAPTEGPVGLT 141
Cdd:PRK06366 77 FGVTKYtvNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSdlrwgpkhllhKNYKIDDAMLVDGLIDAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 142 FPAVFAMAAMRYAKNYDIPleklREKMAHVSIKNHKHG--ALNPlAQFYKKL---GALKLEEVIDSKMVAD-----P--- 208
Cdd:PRK06366 157 YFEHMGVSAERTARKYGIT----REMADEYSVQSYERAirATES-GEFRNEIvpfNDLDRDEGIRKTTMEDlaklpPafd 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 209 ----LSLLDCCPFSDGASALVLCAAEEARKYTDEPV-YILGTGQGSGGPLSKMEdltkpvSRISSAKAAFKQAGLTPKDI 283
Cdd:PRK06366 232 kngiLTAGNSAQLSDGGSALVMASEKAINEYGLKPIaRITGYESASLDPLDFVE------APIPATRKLLEKQNKSIDYY 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1904408614 284 DLVEVHDCFTIAELIAlecmgffdwgeaadaveEGQTELGGEiPVNMSGGLIGKGHPIGATGASQIYWIIKQMR 357
Cdd:PRK06366 306 DLVEHNEAFSIASIIV-----------------RDQLKIDNE-RFNVNGGAVAIGHPIGNSGSRIIVTLINALK 361
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-346 |
2.15e-14 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 73.95 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRASKA-----SLELFSESVLQAIDDAGVELKDIEALFQGAAL-AGfeEGQVMS--AAFSAadlNL 72
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGAladvrADDLGAAVIKALLERAGLDPEAVDDVILGCVLqAG--QGQNPArqAALLA---GL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 73 GP-IPATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEkalTMGT---LFATRTFAMACHAPTEGPVGL-TFPAVFA 147
Cdd:COG0183 76 PEsVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVE---SMSRapmLLPKARWGYRMNAKLVDPMINpGLTDPYT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 148 MAAM-----RYAKNYDIPLE--------------------KLREKMAHVSIKNHKHGAL-----NPLAQF-YKKLGALKl 196
Cdd:COG0183 153 GLSMgetaeNVAERYGISREeqdafalrshqraaaaiaagRFDDEIVPVEVPDRKGEVVvdrdeGPRPDTtLEKLAKLK- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 197 eevidskmvadPLSLLD-------CCPFSDGASALVLCAAEEARKYTDEP-VYILGTGQgSGGPLSKMedLTKPVSrisS 268
Cdd:COG0183 232 -----------PAFKKDgtvtagnASGINDGAAALLLMSEEAAKELGLKPlARIVAYAV-AGVDPEIM--GIGPVP---A 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904408614 269 AKAAFKQAGLTPKDIDLVEVHDCFTIaelIALECMGffDWGEAADAveegqtelggeipVNMSGGLIGKGHPIGATGA 346
Cdd:COG0183 295 TRKALARAGLTLDDIDLIEINEAFAA---QVLAVLR--ELGLDPDK-------------VNVNGGAIALGHPLGASGA 354
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-346 |
3.13e-13 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 70.42 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRASKASL------ELFSESVLQAIDDA-GVELKDIEALFQGAALAGFEEGQVMsAAFSAADLNLG 73
Cdd:PRK07851 1 MPEAVIVSTARSPIGRAFKGSLkdmrpdDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEQGFNM-ARVVAVLLGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 74 PIPA---TRYegaCASASIAIRDAAMWVGSGEYDMVIAGGME--KALTMGT----------LFA---TRTFAMAC----- 130
Cdd:PRK07851 80 FLPGttvNRY---CSSSLQTTRMAFHAIKAGEGDVFISAGVEtvSRFAKGNsdslpdtknpLFAeaqARTAARAEggaea 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 131 -HAPTEGpvGLTFPAVFAMA--AMRYAKNYDIPleklREKMAH--VSIKNHKHGALNplAQFYKK--------------- 190
Cdd:PRK07851 157 wHDPRED--GLLPDVYIAMGqtAENVAQLTGIS----REEQDEwgVRSQNRAEEAIA--NGFFEReitpvtlpdgtvvst 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 191 ----LGALKLEEVIDSKMVADPLSLL---DCCPFSDGASALVLCAAEEARKYTDEPV-YILGTGQgSG--------GPls 254
Cdd:PRK07851 229 ddgpRAGTTYEKVSQLKPVFRPDGTVtagNACPLNDGAAAVVIMSDTKARELGLTPLaRIVSTGV-SGlspeimglGP-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 255 kmedltkpvsrISSAKAAFKQAGLTPKDIDLVEVHDCFtiaelialecmgffdwgeAADAVEEGQtELGgeIP---VNMS 331
Cdd:PRK07851 306 -----------VEASKQALARAGMSIDDIDLVEINEAF------------------AAQVLPSAR-ELG--IDedkLNVS 353
|
410
....*....|....*
gi 1904408614 332 GGLIGKGHPIGATGA 346
Cdd:PRK07851 354 GGAIALGHPFGMTGA 368
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
213-362 |
1.81e-11 |
|
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: 64.00 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 213 DCCPFSDGASALVLCAAEEARKYTDEPVY-ILGTGQGSGGPlsKMEDLTKPVSRISSAKAAFKQAGLTPKDIDLVEVHDC 291
Cdd:cd00327 96 EEFVFGDGAAAAVVESEEHALRRGAHPQAeIVSTAATFDGA--SMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904408614 292 FTiAELIALEcmgffdwgEAADAVEEGQTElggeipVNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAK 362
Cdd:cd00327 174 GT-PIGDAVE--------LALGLDPDGVRS------PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIP 229
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
75-346 |
1.94e-11 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 65.11 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 75 IPATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKaLTMGTLFATRTFAmachapteGPVGLTFPAVFAM------ 148
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQN-MSQIPISSAMTAG--------EQLGFTSPFAESKgwlhry 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 149 ---------AAMRYAKNYDIPleklREKMAHVSIKNHKHgALNPLAQFYKK-----LGALKLEE-VIDS---KMVA-DPL 209
Cdd:PRK07801 151 gdqevsqfrGAELIAEKWGIS----REEMERFALESHRR-AFAAIRAGRFDneivpVGGVTVDEgPRETsleKMAGlKPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 210 ----SLLDCCP--FSDGASALVLCAAEEARKYT--------------DEPVYILgtgqgsggplskmedlTKPvsrISSA 269
Cdd:PRK07801 226 veggRLTAAVAsqISDGASAVLLASERAVKRHGltprarihhlsvrgDDPVFML----------------TAP---IPAT 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904408614 270 KAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMGffdwgeaADAVEegqtelggeipVNMSGGLIGKGHPIGATGA 346
Cdd:PRK07801 287 RYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETG-------ADPAK-----------VNPNGGAIALGHPLGATGA 345
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-357 |
6.75e-11 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 63.19 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFG------RASKASlELFSESVLQAIDDAGVELKDIEALFQGAALAGfEEGQVMS-AAFSAADLNLG 73
Cdd:PRK08235 1 MSKTVIVSAARTPFGkfggslKDVKAT-ELGGIAIKEALERANVSAEDVEEVIMGTVLQG-GQGQIPSrQAARAAGIPWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 74 pIPATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLF--ATRTFAMACHAPTEGPV--GLT--FPAV-F 146
Cdd:PRK08235 79 -VQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILpgARWGYRMGDNEVIDLMVadGLTcaFSGVhM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 147 AMAAMRYAKNYDIPLE--------------------KLREKMAHVSIKNHKhGALNPLAQFYKKLGALKLEEVIDSKMVA 206
Cdd:PRK08235 158 GVYGGEVAKELGISREaqdewayrshqravsaheegRFEEEIVPVTIPQRK-GDPIVVAKDEAPRKDTTIEKLAKLKPVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 207 DP---LSLLDCCPFSDGASALVLCAAEEARKYTDEPV-YILGTGQGSGGPlskmEDLTKPVSRISSAkaAFKQAGLTPKD 282
Cdd:PRK08235 237 DKtgtITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLaTILAHTAIAVEA----KDFPRTPGYAINA--LLEKTGKTVED 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1904408614 283 IDLVEVHDCFTIAELIALECMGFfdwgeaadaveegqtelgGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMR 357
Cdd:PRK08235 311 IDLFEINEAFAAVALASTEIAGI------------------DPEKVNVNGGAVALGHPIGASGARIIVTLIHELK 367
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
218-346 |
2.06e-10 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 61.71 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 218 SDGASALVLCAAEEARKYTDEPVYILGTGQGSGGPLSKMEdlTKPVSRIssaKAAFKQAGLTPKDIDLVEVHDCFtiael 297
Cdd:PRK05790 251 NDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMG--IGPVPAI---RKALEKAGWSLADLDLIEINEAF----- 320
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1904408614 298 ialecmgffdwgeAADAVEEGQtELG-GEIPVNMSGGLIGKGHPIGATGA 346
Cdd:PRK05790 321 -------------AAQALAVEK-ELGlDPEKVNVNGGAIALGHPIGASGA 356
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-346 |
5.88e-09 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 57.41 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 2 RDVAIIGIGHTKFGR-----ASKASLELFSESVLQAIDDAGVELKDIEALFQGAAL-AGFEEGQVMSAAFSAADLNlgPI 75
Cdd:PLN02644 1 RDVCIVGVARTPIGGflgslSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLsANLGQAPARQAALGAGLPP--ST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 76 PATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEkalTMGT----LFATRTFAMACHAP-TEGPV--GLTFP-AVFA 147
Cdd:PLN02644 79 ICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGME---SMSNapkyLPEARKGSRLGHDTvVDGMLkdGLWDVyNDFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 148 M--AAMRYAKNYDIPleklREKMAHVSIKNHKHG-ALNPLAQFYKKL-------GALKLEEVID-----SKMVADPLSLL 212
Cdd:PLN02644 156 MgvCAELCADQYSIS----REEQDAYAIQSYERAiAAQEAGAFAWEIvpvevpgGRGRPSVIVDkdeglGKFDPAKLRKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 213 --------------DCCPFSDGASALVLCAAEEARKYTDEPV-YILGTGQGSGGPlskmEDLTKpvsriSSAKA---AFK 274
Cdd:PLN02644 232 rpsfkedggsvtagNASSISDGAAALVLVSGEKALELGLQVIaKIRGYADAAQAP----ELFTT-----APALAipkALK 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1904408614 275 QAGLTPKDIDLVEVHDCFTIAELIALECMGffdwgeaadaveegqteLGGEiPVNMSGGLIGKGHPIGATGA 346
Cdd:PLN02644 303 HAGLEASQVDYYEINEAFSVVALANQKLLG-----------------LDPE-KVNVHGGAVSLGHPIGCSGA 356
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
84-346 |
7.49e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 56.92 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 84 CASASIAIRDAAMWVGSGEYDMVIAGGMEKA-----LTMGTLFATRTFAMACH-APTEGPV---GLTFPAVFAM--AAMR 152
Cdd:PRK06205 88 CGSGLQAVITAAMQVQTGAADVVIAGGAESMsnvefYTTDMRWGVRGGGVQLHdRLARGREtagGRRFPVPGGMieTAEN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 153 YAKNYDIPLE--------------------KLREKMAHVSIKNHKHGAL------NPLAQF-YKKLGALKleeVIDSKMv 205
Cdd:PRK06205 168 LRREYGISREeqdalavrshqravaaqeagRFDDEIVPVTVPQRKGDPTvvdrdeHPRADTtLESLAKLR---PIMGKQ- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 206 aDPLSLL---DCCPFSDGASALVLCAAEEARKYTDEPVYILGTGQGSGGPLSKMEdlTKPVSrisSAKAAFKQAGLTPKD 282
Cdd:PRK06205 244 -DPEATVtagNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMG--IGPVP---ATEKALARAGLTLDD 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1904408614 283 IDLVEVHDCFTIAeliALECMGFFDWGEAADAveegqtelggEIPVNMSGglIGKGHPIGATGA 346
Cdd:PRK06205 318 IDLIELNEAFAAQ---VLAVLKEWGFGADDEE----------RLNVNGSG--ISLGHPVGATGG 366
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
270-362 |
3.20e-08 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 51.49 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 270 KAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMGFfDWGEaadaveegqtelggeipVNMSGGLIGKGHPIGATGASQI 349
Cdd:pfam02803 29 PKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGI-DPEK-----------------VNVNGGAIALGHPLGASGARIL 90
|
90
....*....|...
gi 1904408614 350 YWIIKQMRGEAAK 362
Cdd:pfam02803 91 VTLLHELKRRGGK 103
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
216-349 |
1.21e-07 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 53.45 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 216 PFSDGASALVLCAAEEARKYTDEPV-YILGTGQGSGGPLSKMedLTKPVSrisSAKAAFKQAGLTPKDIDLVEVHDCF-- 292
Cdd:PRK08963 266 PLTDGAAAVLLMSESRAKALGLTPLgYLRSYAFAAIDVWQDM--LLGPAY---ATPLALERAGLTLADLTLIDMHEAFaa 340
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904408614 293 -TIAELIALECMGFfdwgeAADAVeeGQTELGGEI---PVNMSGGLIGKGHPIGATGASQI 349
Cdd:PRK08963 341 qTLANLQMFASERF-----AREKL--GRSQAIGEVdmsKFNVLGGSIAYGHPFAATGARMI 394
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
219-346 |
1.74e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 52.96 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 219 DGAsALVLCAAEEA-RKYTDEP-VYILGTGQgSGGPLSKMedLTKPVSrisSAKAAFKQAGLTPKDIDLVEVHDCFtiae 296
Cdd:PRK08242 261 DGA-AAVLIGSEEAgKALGLKPrARIVATAT-IGSDPTIM--LTGPVP---ATRKALAKAGLTVDDIDLFELNEAF---- 329
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1904408614 297 lialecmgffdwgeaADAVEEGQTELGgeIP---VNMSGGLIGKGHPIGATGA 346
Cdd:PRK08242 330 ---------------ASVVLRFMQALD--IPhdkVNVNGGAIAMGHPLGATGA 365
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-357 |
2.08e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 52.45 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRASKASL------ELFSESVLQAIDDAGVELKDIEALFQGAALAGFEEGQVMSAAFSAadlnLGP 74
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKKGSLktvrpdDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGA----LAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 75 IPAT-------RYegaCASASIAIRDAAMWVGSGEYDMVIAGGMEKA--LTMGTLFATRTFAMACHAP--------TEGP 137
Cdd:PRK07661 77 LPYTvpaitinRY---CSSGLQSIAYGAERIMLGHSEAVIAGGAESMslVPMMGHVVRPNPRLVEAAPeyymgmghTAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 138 VGLTFPA------VFAMAAMRYAKNyDIPLEKLREKMAHVSIKNHKHGALNPLAQfykKLGALKLEEVIDSKMVADPLSL 211
Cdd:PRK07661 154 VAVKYGIsredqdAFAVRSHQRAAK-ALAEGKFADEIVPVDVTLRTVGENNKLQE---ETITFSQDEGVRADTTLEILGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 212 L-------------DCCPFSDGASALVLCAAEEARKYTDEPVYILGTGQGSGGPLSKMEdlTKPVSRISSAkaaFKQAGL 278
Cdd:PRK07661 230 LrpafnvkgsvtagNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMG--IGPIAAIPKA---LKLAGL 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904408614 279 TPKDIDLVEVHDCFTIAELIALECMGFfdwgeaadaveegqtelgGEIPVNMSGGLIGKGHPIGATGASQIYWIIKQMR 357
Cdd:PRK07661 305 ELSDIGLFELNEAFASQSIQVIRELGL------------------DEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMK 365
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-346 |
2.14e-07 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 52.27 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGRaSKASL------ELFSESVLQAI--DDAGVELKDIEALFQGAALAGFEEGqvMSAAFSAADLNL 72
Cdd:PRK08947 1 MEDVVIVDAIRTPMGR-SKGGAfrnvraEDLSAHLMRSLlaRNPALDPAEIDDIIWGCVQQTLEQG--FNIARNAALLAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 73 GP--IPATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKaltMGTLFATRTF----AMACH-APTEGPVGLTfpav 145
Cdd:PRK08947 78 IPhsVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEH---MGHVPMNHGVdfhpGLSKNvAKAAGMMGLT---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 146 famAAMrYAKNYDIPleklREKMAHVSIKNHKHGALNPLAQFYKKL----------GALKL---EEVIDSKMVADPLSLL 212
Cdd:PRK08947 151 ---AEM-LGKMHGIS----REQQDAFAARSHQRAWAATQEGRFKNEiipteghdadGVLKLfdyDEVIRPETTVEALAAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 213 --------------DCCPFSDGASALVLCAAEEARKYTDEPVYILGTGQGSGGPLSKMEdlTKPVSrisSAKAAFKQAGL 278
Cdd:PRK08947 223 rpafdpvngtvtagTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMG--YGPVP---ATQKALKRAGL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904408614 279 TPKDIDLVEVHDCFTIAELIALECMGFFdwgeaaDAVEEgqtelggeiPVNMSGGLIGKGHPIGATGA 346
Cdd:PRK08947 298 SISDIDVFELNEAFAAQSLPCLKDLGLL------DKMDE---------KVNLNGGAIALGHPLGCSGA 350
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
61-346 |
5.55e-07 |
|
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: 51.39 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 61 MSAAFSAADLNL-GPI--PATryegACASASIAIRDAAMWVGSGEYDMVIAGGMEKALTMGTLfatrtfamachaptegp 137
Cdd:cd00834 139 MAAGQVAIRLGLrGPNytVST----ACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTL----------------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 138 vgltfpAVFAmaamryaknydipleklrekmahvsiknhkhgalnplaqfykKLGALkleevidSKMVADPLSLldCCPF 217
Cdd:cd00834 198 ------AGFA------------------------------------------ALRAL-------STRNDDPEKA--SRPF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 218 S---------DGASALVLCAAEEARKyTDEPVY--ILGTGQGSGGplskmEDLTKPVSRISSA----KAAFKQAGLTPKD 282
Cdd:cd00834 221 DkdrdgfvlgEGAGVLVLESLEHAKA-RGAKIYaeILGYGASSDA-----YHITAPDPDGEGAaramRAALADAGLSPED 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904408614 283 IDLVEVH-------DcftIAELIALEcmGFFdwGEAADaveegqtelggEIPVNMSGGLIgkGHPIGATGA 346
Cdd:cd00834 295 IDYINAHgtstplnD---AAESKAIK--RVF--GEHAK-----------KVPVSSTKSMT--GHLLGAAGA 345
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
6-304 |
1.26e-06 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 50.30 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 6 IIGIG----HTKFGRASKASLELFSESVLQAIDDAGVE--LKDIEALfqgAALAGFEEGQVMSAAFSAADLNLGPiPATR 79
Cdd:PRK08257 8 IVGVGqvteRPDDPAYGLEPVDLMAAAARAAAADAGADavLEAIDSV---AVVNQLSWRYRDPPGLLAERLGADP-ARTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 80 YEGACASASIA-IRDAAMWVGSGEYDMVIAGGME------KALTMG-----TLFATRTFA------MACHAPTEGPVGLT 141
Cdd:PRK08257 84 YSPVGGNSPQRlVNEAALRIAAGEADVALVAGAEaqstatKLRKAGekldwTPQDEGPLAdrggdpRPMASPAELRHGLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 142 FPA-VFAM--AAMRYAKNYDIP--LEKLREKMAHVSiknhKHGALNPLAQFYKKLGAlklEEVI----DSKMVADPLS-L 211
Cdd:PRK08257 164 RPVyVYPLfeNALRAALGRSPEehRAEMGELWAPFS----AVAAKNPHAWIPRERSA---EEIVtptpDNRMIAWPYTkL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 212 LDCCPFSDGASALVLCAAEEARKY---TDEPVYILGtGQGSGGPLSKME--DLTKPVSRISSAKAAFKQAGLTPKDIDLV 286
Cdd:PRK08257 237 MNANDMVDQGAAVLLTSVAKARRLgvpEDRWVYLHG-GADAHDPYDILErpDLHRSPAIRAAGRRALALAGLGIDDIDAF 315
|
330
....*....|....*...
gi 1904408614 287 EVHDCFTIAELIALECMG 304
Cdd:PRK08257 316 DLYSCFPSAVQVAARELG 333
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
219-346 |
3.81e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 48.62 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 219 DGASALVLCAAEEARKYTDEP-VYILGTGQGSGGPlSKMedLTKPVSrisSAKAAFKQAGLTPKDIDLVEVHDCFTIAel 297
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPrARIVAMANMGDDP-TLM--LNAPVP---AAKKVLAKAGLTKDDIDLWEINEAFAVV-- 347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1904408614 298 ialecmgffdwgeaadaVEEGQTELG-GEIPVNMSGGLIGKGHPIGATGA 346
Cdd:PRK06025 348 -----------------AEKFIRDLDlDRDKVNVNGGAIALGHPIGATGS 380
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
219-346 |
3.98e-06 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 48.42 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 219 DGASALVLCAAEEARKYTDEPVY-ILGTGQgSGGPLSKMEdltkpVSRISSAKAAFKQAGLTPKDIDLVEVHDCFtiael 297
Cdd:PRK09051 253 DGAAAVVLAEADAAEARGLKPLArLVGYAH-AGVDPEYMG-----IGPVPATQKALERAGLTVADLDVIEANEAF----- 321
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1904408614 298 ialecmgffdwgeAADAVEEGQtELG-GEIPVNMSGGLIGKGHPIGATGA 346
Cdd:PRK09051 322 -------------AAQACAVTR-ELGlDPAKVNPNGSGISLGHPVGATGA 357
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
94-362 |
1.03e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 47.19 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 94 AAMWVGSGE-YDMVIAGGMEKALTMGTLFATrtFAMACHAPtegpVGLTFPA--VFAMAAMRYAK--NYDiplEKLREKM 168
Cdd:PRK06954 135 GGMRMGHGQvLDHMFLDGLEDAYDKGRLMGT--FAEECAGE----YGFTREAqdAFAIESLARAKraNED---GSFAWEI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 169 AHVSIKNHKHGAL-----NPLAQFYKKLGALKLEEVIDSKMVADPLSLLdccpfSDGASALVLCAAEEARKYTDEPV-YI 242
Cdd:PRK06954 206 APVTVAGKKGDTVidrdeQPFKANPEKIPTLKPAFSKTGTVTAANSSSI-----SDGAAALVMMRASTAKRLGLAPLaRV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 243 LGTGQGSGGPlSKMEdlTKPVSRIssaKAAFKQAGLTPKDIDLVEVHDCFTIAELIALECMGffdwgeaadaveegqtel 322
Cdd:PRK06954 281 VGHSTFAQAP-SKFT--TAPVGAI---RKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHG------------------ 336
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1904408614 323 ggeIP---VNMSGGLIGKGHPIGATGASQIYWIIKQMRGEAAK 362
Cdd:PRK06954 337 ---LPhekVNVNGGACALGHPIGASGARILVTLIGALRARGGK 376
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
75-346 |
3.23e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 45.49 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 75 IPATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKA--LTMG---TLFATRTFAmacHAPTEGpVGLTFPAV---- 145
Cdd:PRK06504 80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMtrVPMGspsTLPAKNGLG---HYKSPG-MEERYPGIqfsq 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 146 FAMAAMrYAKNYDIPLEKLREkmahVSIKNHKHG-ALNPLAQFYKKLGALK----------------------LEEVIDS 202
Cdd:PRK06504 156 FTGAEM-MAKKYGLSKDQLDE----FALQSHQRAiAATQAGKFKAEIVPLEitradgsgemhtvdegirfdatLEGIAGV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 203 KMVAD--PLSLLDCCPFSDGASAlVLCAAEEARKytdepvyILGTgqgsgGPLSKMEDLT----KPV----SRISSAKAA 272
Cdd:PRK06504 231 KLIAEggRLTAATASQICDGASG-VMVVNERGLK-------ALGV-----KPLARIHHMTviggDPVimleAPLPATERA 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1904408614 273 FKQAGLTPKDIDLVEVHDCFTIAELIALECMGffdwgeaADAVEegqtelggeipVNMSGGLIGKGHPIGATGA 346
Cdd:PRK06504 298 LKKAGMKIDDIDLYEVNEAFASVPLAWLKATG-------ADPER-----------LNVNGGAIALGHPLGASGT 353
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
31-116 |
3.54e-05 |
|
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: 45.47 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 31 QAIDDAGVELKDIE----ALFQGAALAGFE--EGQV----------------------MSAAFSAADLNL-GPI--PATr 79
Cdd:COG0304 81 EALADAGLDLDEVDpdrtGVIIGSGIGGLDtlEEAYrallekgprrvspffvpmmmpnMAAGHVSIRFGLkGPNytVST- 159
|
90 100 110
....*....|....*....|....*....|....*..
gi 1904408614 80 yegACASASIAIRDAAMWVGSGEYDMVIAGGMEKALT 116
Cdd:COG0304 160 ---ACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT 193
|
|
| PRK08304 |
PRK08304 |
stage V sporulation protein AD; Validated |
19-109 |
4.69e-05 |
|
stage V sporulation protein AD; Validated
Pssm-ID: 236230 Cd Length: 337 Bit Score: 44.83 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 19 KASLELFSESVLQAIDDAGVELKDIEALFQGAALagfeeGQVMSAAFSAADLNlgpIPATRYEGACASASIAIRDAAMWV 98
Cdd:PRK08304 54 KAERKMMEDAIQQALQKANLKKSDIDYLLAGDLL-----NQIISANFAARELG---IPFLGLYGACSTMMESLALGSMLI 125
|
90
....*....|.
gi 1904408614 99 GSGEYDMVIAG 109
Cdd:PRK08304 126 DGGFADRVLAA 136
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
7-109 |
5.35e-05 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 44.73 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 7 IGIGHTKFGRASKASLELFSESVLQAIDDAGVELKDIEALfqgaaLAGFEEGQVMSAAFS---AADLNLGPIPATRYEGA 83
Cdd:cd00827 34 TGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLL-----IVATESPIDKGKSAAtylAELLGLTNAEAFDLKQA 108
|
90 100
....*....|....*....|....*...
gi 1904408614 84 CASASIAIRDAAMWVGSGEYD--MVIAG 109
Cdd:cd00827 109 CYGGTAALQLAANLVESGPWRyaLVVAS 136
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-363 |
7.67e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 44.49 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 1 MRDVAIIGIGHTKFGR-----ASKASLELFSESVLQAIDDAGVELKDIEALFQGAAL-AGFEEGQVMSAAFSAADLNlgP 74
Cdd:PRK05656 1 MQDVVIVAATRTAIGSfqgslANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLtAGAGQNPARQAAIKAGLPH--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 75 IPATRYEGACASASIAIRDAAMWVGSGEYDMVIAGGMEK-ALTMGTLFATRTFAMACHAP------TEG----------- 136
Cdd:PRK05656 79 VPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENmSLAPYVLPGARTGLRMGHAQlvdsmiTDGlwdafndyhmg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 137 --------PVGLTFPAVFAMAAMRYAKNYD-IPLEKLREKMAHVSIKNHKHGAL------NPLAQFY-KKLGALKLEEVI 200
Cdd:PRK05656 159 itaenlveKYGISREAQDAFAAASQQKAVAaIEAGRFDDEITPILIPQRKGEPLafatdeQPRAGTTaESLAKLKPAFKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 201 DSKMVADPLSLLDccpfsDGASALVLCAAEEARKYtDEPVYILGTGQGSGGplskMEDLTKPVSRISSAKAAFKQAGLTP 280
Cdd:PRK05656 239 DGSVTAGNASSLN-----DGAAAVLLMSAAKAKAL-GLPVLAKIAAYANAG----VDPAIMGIGPVSATRRCLDKAGWSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 281 KDIDLVEVHDCFtiaelialecmgffdwgeAADAVEEGQtELGGEIP-VNMSGGLIGKGHPIGATGASQIYWIIKQM-RG 358
Cdd:PRK05656 309 AELDLIEANEAF------------------AAQSLAVGK-ELGWDAAkVNVNGGAIALGHPIGASGCRVLVTLLHEMiRR 369
|
....*
gi 1904408614 359 EAAKG 363
Cdd:PRK05656 370 DAKKG 374
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
218-362 |
1.05e-04 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 43.98 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408614 218 SDGASALVLCAAEEARKytdEPVYILGTGQG---SGGPLSKMEdlTKPVSRISsakAAFKQAGLTPKDIDLVEVHDCFti 294
Cdd:PLN02287 291 SDGAGAVLLMKRSVAMQ---KGLPILGVFRSfaaVGVDPAVMG--IGPAVAIP---AAVKAAGLELDDIDLFEINEAF-- 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904408614 295 aelialecmgffdwgeAADAVEEGQtELG-GEIPVNMSGGLIGKGHPIGATGASQIYWIIKQM--RGEAAK 362
Cdd:PLN02287 361 ----------------ASQFVYCCK-KLGlDPEKVNVNGGAIALGHPLGATGARCVATLLHEMkrRGKDCR 414
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
61-116 |
1.82e-03 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 40.06 E-value: 1.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1904408614 61 MSAAFSAADLNL-GPIPATryEGACASASIAIRDAAMWVGSGEYDMVIAGGMEKALT 116
Cdd:PTZ00050 146 MAAGLVAIKHKLkGPSGSA--VTACATGAHCIGEAFRWIKYGEADIMICGGTEASIT 200
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
217-289 |
3.69e-03 |
|
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: 39.08 E-value: 3.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904408614 217 FSDGASALVLCAAEEARKYTDePVY--ILGTGQGSGGplsKMEDLTKPVSRISSA--KAAFKQAGLTPKDIDLVEVH 289
Cdd:cd00833 233 RGEGVGVVVLKRLSDALRDGD-RIYavIRGSAVNQDG---RTKGITAPSGEAQAAliRRAYARAGVDPSDIDYVEAH 305
|
|
| |
