|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
4-1396 |
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: 599.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 4 PRAEPVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPPGRWDAEEYYAPGgEARADRVYCRRGGFVDELAEVDVTEFG 83
Cdd:COG3321 1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPD-PDAPGKTYVRWGGFLDDVDEFDALFFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 84 IMPAAVPATEPDQlialrvaaaaladaggqgRL---------------PA--DRHRVGVVLGRGGyltpglvrldqrvrt 146
Cdd:COG3321 80 ISPREAEAMDPQQ------------------RLllevawealedagydPEslAGSRTGVFVGASS--------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 147 asqlvrtlGELLPDLGADRLEAVRQAFTdrlgpeapessiGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVR 226
Cdd:COG3321 127 --------NDYALLLLADPEAIDAYALT------------GNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 227 ELGSGRCDVMLAGGVH-HCHDITFwSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITG 305
Cdd:COG3321 187 SLRSGECDLALAGGVNlMLTPESF-ILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 306 TGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFGppsTDASGDAPdA 385
Cdd:COG3321 266 SAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPA---TVDYVEAHGTGTPLGDPIEAAALTAAFG---QGRPADQP-C 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 386 VIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPA--LARTRFTPIGAALPWRTDDRqpVRRAAVNAFGF 463
Cdd:COG3321 339 AIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHidFENSPFYVNTELRPWPAGGG--PRRAGVSSFGF 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 464 GGINAHVVLEEVAVARRPAEVYEPEP-VLRLTAPTPEAMAALLDRsdsaiiTAGLDERAPATD---------------PV 527
Cdd:COG3321 417 GGTNAHVVLEEAPAAAPAAAAAARPPqLLVLSAKTEEALRALAAR------LAAFLEAHPDLDladvaytlatgrahfEH 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 528 RIAVVGPTAKRLALARKAVAKGKGWRG--RGDvwfvprpllGPGGGRLAFVFPG--------------LEAEFAPNSEDI 591
Cdd:COG3321 491 RLAVVASSREELAAKLRALAAGEAAPGvvTGA---------AAAAPKVAFLFPGqgsqyvgmgrelyeTEPVFRAALDEC 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 592 ARHFG--LPWS-RAVTDATVGDVGRQGTGV-----FELGRLLDTALRRLGVVPDALAGHSLGEWTAMAAAGIHPPEevda 663
Cdd:COG3321 562 DALLRphLGWSlREVLFPDEEESRLDRTEVaqpalFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLE---- 637
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 664 fladfdpDALSV------------PGLAFAAIGAPSEVVLSELDGRGDVVLSHDNAPNQSMICGPEPAVAALVEVFRARA 731
Cdd:COG3321 638 -------DALRLvaargrlmqalpGGGAMLAVGLSEEEVEALLAGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARG 710
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 732 VISQILPFRSGFHTPMLEPYLDPIRKAAEAYTLRPAALPVWSATTVAPYpDEPAAIRELFIRHLLEPVRFRPLVETMYAA 811
Cdd:COG3321 711 IRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWL-TGEALDADYWVRHLRQPVRFADAVEALLAD 789
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 812 GFRAFVQLGAGQ-LGSLIDDTLHGR-DHLVVPAHSPHRPGLPQLHRVASALWADGATPDLVPLLGGASTVT---PARTVR 886
Cdd:COG3321 790 GVRVFLEVGPGPvLTGLVRQCLAAAgDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRvplPTYPFQ 869
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 887 RPSRPVRLDLGGANVSLDPETRERLSAALARPRHTAPQEADALAAQGPLGAELSALLRDATALASDVVTAGRRGRGAPTL 966
Cdd:COG3321 870 REDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAA 949
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 967 PRTGAGRPPHPRTGGTPAKNGADLRTAEPTTPEPQPQPQPLEATLHVSVDTMPYLLDHCFFRQPAQADPADRWPVVPGTT 1046
Cdd:COG3321 950 AAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLA 1029
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1047 VIAHLMEFAERAAPGRRAVAVHDVRLHQWITATPAVDIPVRIVPEGPDRVTASLGPYARAVVELAQDRPRFTPPGPWTFP 1126
Cdd:COG3321 1030 AAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLL 1109
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1127 AEREEKPELTAAELYSRRWMFHGPRFQGLAELTAVGDRHVRGVLVTPPAPGALLDNVGQLLGYWIMARQPVRTTVFPVGM 1206
Cdd:COG3321 1110 ALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAAL 1189
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1207 KEIRFHGPHPAPGERLECLIRITSVTDATLEADMQLVHRGRVWAEFSGWQDRRFDSNPRIRKVDREPERYTLSRMQPGGW 1286
Cdd:COG3321 1190 AGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAA 1269
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1287 ALVHEEWPDLATRELIMRNILAGEERERYAVHAPRGRRQWLLGRIAAKDAVRNVMWDAGAGPVYPAEVRVGNDPAGRPFV 1366
Cdd:COG3321 1270 GLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAA 1349
|
1450 1460 1470
....*....|....*....|....*....|
gi 1706746047 1367 TGGYGRTLPELHVSIAHRGETAVAMARAEG 1396
Cdd:COG3321 1350 AAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
7-472 |
4.52e-144 |
|
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: 447.77 E-value: 4.52e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 7 EPVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPPGRWDAEEYYAPGGEAraDRVYCRRGGFVDELAEVDVTEFGIMP 86
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKP--GKTYTRRGGFLDDVDAFDAAFFGISP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 87 AAVPATEPDQlialrvaaaaladaggqgRL-----------------PADRHRVGVVLGrggyltpglvrldqrvrtasq 149
Cdd:cd00833 79 REAEAMDPQQ------------------RLllevawealedagyspeSLAGSRTGVFVG--------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 150 lvrTLGELLPDLGADRLEAVRqaftdrlgpeaPESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELG 229
Cdd:cd00833 120 ---ASSSDYLELLARDPDEID-----------AYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 230 SGRCDVMLAGGVHHCHDITFWSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVA 309
Cdd:cd00833 186 SGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 310 SDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFGPPSTDASGdapdAVIGS 389
Cdd:cd00833 266 QDGRTKGITAPSGEAQAALIRRAYARAGVDPS---DIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQP----LLIGS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 390 VKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPAL--ARTRFTPIGAALPWRTDDRqpVRRAAVNAFGFGGIN 467
Cdd:cd00833 339 VKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIdfEESPLRVPTEARPWPAPAG--PRRAGVSSFGFGGTN 416
|
....*
gi 1706746047 468 AHVVL 472
Cdd:cd00833 417 AHVIL 421
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
8-915 |
5.17e-123 |
|
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: 427.50 E-value: 5.17e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 8 PVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPPGRWDAEEYYApGGEARADRVYCRRGGFVDELaEVDVTEFGIMPA 87
Cdd:TIGR02813 8 PIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYD-SDKSEADKSYCKRGGFLPEV-DFNPMEFGLPPN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 88 AVPATEPDQLIALRVAAAALADAGgqgrLPA--DRHRVGVVLGRGG---YLTPGLVRLDQRVrtasqlvrtLGELLPDLG 162
Cdd:TIGR02813 86 ILELTDISQLLSLVVAKEVLNDAG----LPDgyDRDKIGITLGVGGgqkQSSSLNARLQYPV---------LKKVFKASG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 163 ---ADRlEAVRQAFTDRLGPEAPESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAG 239
Cdd:TIGR02813 153 vedEDS-EMLIKKFQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 240 GVHHCHDITFWSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMA 319
Cdd:TIGR02813 232 GVCTDNSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 320 PDSGGQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFgppsTDASGDAPDAVIGSVKSMIGHTMP 399
Cdd:TIGR02813 312 PRPEGQAKALKRAYDDAGFAPH---TCGLIEAHGTGTAAGDVAEFGGLVSVF----SQDNDQKQHIALGSVKSQIGHTKS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 400 AAGVAGLIKAALAVHHQVLPPTLHCDDPHPAL--ARTRFTPIGAALPW--RTDDRQpvRRAAVNAFGFGGINAHVVLEEV 475
Cdd:TIGR02813 385 TAGTAGMIKAVLALHHKVLPPTINVDQPNPKLdiENSPFYLNTETRPWmqREDGTP--RRAGISSFGFGGTNFHMVLEEY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 476 AVARRPAEVYEPEPV---LRLTAPTPEAM-AALLDRSDSAIITAGLDE------------RAPATDPVRIAVVGPTAKRL 539
Cdd:TIGR02813 463 SPKHQRDDQYRQRAVaqtLLFTAANEKALvSSLKDWKNKLSAKADDQPyafnalaventlRTIAVALARLGFVAKNADEL 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 540 ------ALARKAVAKGKGWRGRGDVWFVPRPLLGpGGGRLAFVFPGLEAEFAPNSEDIARHFglPWSRAVTDATVGDVGR 613
Cdd:TIGR02813 543 itmleqAITQLEAKSCEEWQLPSGISYRKSALVV-ESGKVAALFAGQGSQYLNMGRELACNF--PEVRQAAADMDSVFTQ 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 614 QGTG----------VF--ELGRLLDTALR---------------------RLGVVPDALAGHSLGEWTAMAAAGIhpPEE 660
Cdd:TIGR02813 620 AGKGalspvlypipVFndESRKAQEEALTntqhaqsaigtlsmgqyklftQAGFKADMTAGHSFGELSALCAAGV--ISD 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 661 VDAFLADF-----------DPDALSVPGLAFAAIGAPsEVVLSELDGRGDVVLSHDNAPNQSMICGPEPAVAALVEVFRA 729
Cdd:TIGR02813 698 DDYMMLAFsrgqamaaptgEADIGFMYAVILAVVGSP-TVIANCIKDFEGVSIANYNSPTQLVIAGVSTQIQIAAKALKE 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 730 RAVISQILPFRSGFHTPMLEPYLDPIRKAAEAYTLRPAALPVWSATTVAPYPDEPAAIRELFIRHLLEPVRFRPLVETMY 809
Cdd:TIGR02813 777 KGFKAIPLPVSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMY 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 810 AAGFRAFVQLGAGQ-LGSLIDDTLHGR-DHLVVPAHSPHRPGLP--QLHRVASALWADGATPDlvpllggasTVTPARTV 885
Cdd:TIGR02813 857 AAGARVFVEFGPKNiLQKLVENTLKDKeNELCAISINPNPKGDSdmQLRQAAVQLAVLGLELT---------EIDPYQAE 927
|
970 980 990
....*....|....*....|....*....|...
gi 1706746047 886 RRP---SRPVRLDLGGANVsLDPETRERLSAAL 915
Cdd:TIGR02813 928 KRPpaaTSPMNIKLNAANY-ISPATRKKMDDSL 959
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
9-474 |
1.16e-78 |
|
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: 261.88 E-value: 1.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 9 VAIVGMSVLFPGAPDLATYWHNLVSGVDAItevppGRWDAEeyyapggearadrvycrrggFvdelaevdvteFGIMPAA 88
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDV-----DLFDAA--------------------F-----------FGISPRE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 89 VPATEPdqlialrvaaaaladaggQgrlpadrhrvgvvlgrggyltpglvrldQRvrtasqlvrtlgeLLpdlgadrLEA 168
Cdd:smart00825 45 AEAMDP------------------Q----------------------------QR-------------LL-------LEV 58
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 169 VRQAFtdrlgpeapESSiGLVPnlaaSRLAGR-------LDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGV 241
Cdd:smart00825 59 AWEAL---------EDA-GIDP----ESLRGSrtgvfvgVSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGGV 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 242 HHCHDITFWSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPD 321
Cdd:smart00825 125 NLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPS 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 322 SGGQVRavrqaweaagldpsapgsiglleahgtatpagdgtelttlaevfgppstdasgdapdavIGSVKSMIGHTMPAA 401
Cdd:smart00825 205 GPAQLL-----------------------------------------------------------IGSVKSNIGHLEAAA 225
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1706746047 402 GVAGLIKAALAVHHQVLPPTLHCDD--PHPALARTRFTPIGAALPWRTDDRqpVRRAAVNAFGFGGINAHVVLEE 474
Cdd:smart00825 226 GVAGLIKVVLALKHGVIPPTLHFETpnPHIDLEESPLRVPTELTPWPPPGR--PRRAGVSSFGFGGTNAHVILEE 298
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
7-292 |
3.70e-50 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 178.21 E-value: 3.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 7 EPVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPPGRWDAEEYYAPGGEArADRVYCRRGGfVDELAEVDVTEFGIMP 86
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRI-AGKIYTKWGG-LDDIFDFDPLFFGISP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 87 AAVPATEPDQLIALRVAAAALADAGgqgrLPADR---HRVGVVLGRGGYLTPGLVRLDqrvrtasqlvrtlgellpdlGA 163
Cdd:pfam00109 79 REAERMDPQQRLLLEAAWEALEDAG----ITPDSldgSRTGVFIGSGIGDYAALLLLD--------------------ED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 164 DRLEAVRQAFTdrlgpeapessiGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVH- 242
Cdd:pfam00109 135 GGPRRGSPFAV------------GTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNl 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1706746047 243 HCHDITFwSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADA 292
Cdd:pfam00109 203 LLTPLGF-AGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
191-468 |
1.33e-49 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 182.58 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 191 NLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHCHDITFWSVFSQLGALS------PSER 264
Cdd:PTZ00050 145 NMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQRA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 265 IRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSApg 344
Cdd:PTZ00050 225 SRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANININ-- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 345 SIGLLEAHGTATPAGDGTELTTLAEVFGPpstdasGDAPDAVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHC 424
Cdd:PTZ00050 303 DVDYVNAHATSTPIGDKIELKAIKKVFGD------SGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINL 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1706746047 425 DDPHPALArTRFTPIGAALPwrtddRQPVRRAAVNAFGFGGINA 468
Cdd:PTZ00050 377 ENPDAECD-LNLVQGKTAHP-----LQSIDAVLSTSFGFGGVNT 414
|
|
| ACPS |
pfam01648 |
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ... |
1397-1485 |
4.77e-14 |
|
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Pssm-ID: 426364 [Multi-domain] Cd Length: 111 Bit Score: 69.94 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1397 PCGIDIEEVTD-------RPEGTLAVALTTAERELLTSLvhrpgGAPERLWFTRFWAAKEAVAKARGTGLGG--EPKRFE 1467
Cdd:pfam01648 1 GVGIDIEEIARirrpierLGERLAERIFTPEERALLASL-----PAEARRAFARLWTAKEAVFKALGPGLSKllDFDDIE 75
|
90
....*....|....*...
gi 1706746047 1468 ITSVDGDRLTVRTAGEEY 1485
Cdd:pfam01648 76 VLLDPDGRPTLRLLGEAA 93
|
|
| pantethn_trn |
TIGR00556 |
phosphopantetheine--protein transferase domain; This model models a domain active in ... |
1396-1508 |
2.30e-05 |
|
phosphopantetheine--protein transferase domain; This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics. [Protein fate, Protein modification and repair]
Pssm-ID: 273136 [Multi-domain] Cd Length: 128 Bit Score: 45.51 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1396 GPCGIDIEEVT------DRPEGTLAVALTTAERELLTSLvhrpGGAPERLWFTRFWAAKEAVAKARGTGLGGEP---KRF 1466
Cdd:TIGR00556 3 VGIGIDIVEIKriaeqiERSGTFAERFFTPSEIEDYCKL----SPKSQTESLAGRWAAKEAFIKALGKGISLGEllfTDI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1706746047 1467 EITSVDGDRLTVRTAGE-EYRVRHCALTTPRPSAGPDKEYVVA 1508
Cdd:TIGR00556 79 EIVKDLKGAPRVCLIGEaAKDAEKLGVCSVHVSISHDKEYAAA 121
|
|
| PRK10351 |
PRK10351 |
4'-phosphopantetheinyl transferase AcpT; |
1319-1497 |
4.08e-05 |
|
4'-phosphopantetheinyl transferase AcpT;
Pssm-ID: 182399 [Multi-domain] Cd Length: 187 Bit Score: 45.98 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1319 APRGRRQ--WLLGRiaakdavrnVMWDAGAGPVYPAEVrvgnDPAGRPFVTGGygrtlPELHVSIAHRGETAVAMARAEG 1396
Cdd:PRK10351 17 APQGPRRarWLAGR---------VLLSHALSPLPEIIY----GEQGKPAFAPE-----TPLWFNLSHSGDDIALLLSDEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1397 PCGIDIEEVTDRPE-GTLAVALTTAERELLTSLVHrPGGAPERLWftRFWAAKEAVAKARGTGLggepkrFEITSVDGdr 1475
Cdd:PRK10351 79 EVGCDIEVIRPRANwRSLANAVFSLGEHAEMDAVH-PEQQLEAFW--RIWTRKEAIVKQRGGSA------WQIVSVDS-- 147
|
170 180
....*....|....*....|....*....
gi 1706746047 1476 ltvrTAGEEYRVRHC-------ALTTPRP 1497
Cdd:PRK10351 148 ----TLPSALSVSHCqlenlslAVCTPTP 172
|
|
| AcpS |
COG0736 |
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]; |
1399-1483 |
6.63e-05 |
|
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
Pssm-ID: 440499 [Multi-domain] Cd Length: 122 Bit Score: 43.96 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1399 GIDIEEVtDRPEGTLAVA--------LTTAERELLTSLVHRPggapERLWfTRFwAAKEAVAKARGTGLGGE--PKRFEI 1468
Cdd:COG0736 3 GIDIVEI-ARIERALERHgerflervFTPAERAYCQSRKRPA----EFLA-GRF-AAKEAVSKALGTGIGKGvsWRDIEV 75
|
90
....*....|....*
gi 1706746047 1469 TSVDGDRLTVRTAGE 1483
Cdd:COG0736 76 LNDPSGKPTVRLSGR 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
4-1396 |
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: 599.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 4 PRAEPVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPPGRWDAEEYYAPGgEARADRVYCRRGGFVDELAEVDVTEFG 83
Cdd:COG3321 1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPD-PDAPGKTYVRWGGFLDDVDEFDALFFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 84 IMPAAVPATEPDQlialrvaaaaladaggqgRL---------------PA--DRHRVGVVLGRGGyltpglvrldqrvrt 146
Cdd:COG3321 80 ISPREAEAMDPQQ------------------RLllevawealedagydPEslAGSRTGVFVGASS--------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 147 asqlvrtlGELLPDLGADRLEAVRQAFTdrlgpeapessiGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVR 226
Cdd:COG3321 127 --------NDYALLLLADPEAIDAYALT------------GNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 227 ELGSGRCDVMLAGGVH-HCHDITFwSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITG 305
Cdd:COG3321 187 SLRSGECDLALAGGVNlMLTPESF-ILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 306 TGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFGppsTDASGDAPdA 385
Cdd:COG3321 266 SAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPA---TVDYVEAHGTGTPLGDPIEAAALTAAFG---QGRPADQP-C 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 386 VIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPA--LARTRFTPIGAALPWRTDDRqpVRRAAVNAFGF 463
Cdd:COG3321 339 AIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHidFENSPFYVNTELRPWPAGGG--PRRAGVSSFGF 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 464 GGINAHVVLEEVAVARRPAEVYEPEP-VLRLTAPTPEAMAALLDRsdsaiiTAGLDERAPATD---------------PV 527
Cdd:COG3321 417 GGTNAHVVLEEAPAAAPAAAAAARPPqLLVLSAKTEEALRALAAR------LAAFLEAHPDLDladvaytlatgrahfEH 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 528 RIAVVGPTAKRLALARKAVAKGKGWRG--RGDvwfvprpllGPGGGRLAFVFPG--------------LEAEFAPNSEDI 591
Cdd:COG3321 491 RLAVVASSREELAAKLRALAAGEAAPGvvTGA---------AAAAPKVAFLFPGqgsqyvgmgrelyeTEPVFRAALDEC 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 592 ARHFG--LPWS-RAVTDATVGDVGRQGTGV-----FELGRLLDTALRRLGVVPDALAGHSLGEWTAMAAAGIHPPEevda 663
Cdd:COG3321 562 DALLRphLGWSlREVLFPDEEESRLDRTEVaqpalFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLE---- 637
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 664 fladfdpDALSV------------PGLAFAAIGAPSEVVLSELDGRGDVVLSHDNAPNQSMICGPEPAVAALVEVFRARA 731
Cdd:COG3321 638 -------DALRLvaargrlmqalpGGGAMLAVGLSEEEVEALLAGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARG 710
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 732 VISQILPFRSGFHTPMLEPYLDPIRKAAEAYTLRPAALPVWSATTVAPYpDEPAAIRELFIRHLLEPVRFRPLVETMYAA 811
Cdd:COG3321 711 IRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWL-TGEALDADYWVRHLRQPVRFADAVEALLAD 789
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 812 GFRAFVQLGAGQ-LGSLIDDTLHGR-DHLVVPAHSPHRPGLPQLHRVASALWADGATPDLVPLLGGASTVT---PARTVR 886
Cdd:COG3321 790 GVRVFLEVGPGPvLTGLVRQCLAAAgDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRvplPTYPFQ 869
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 887 RPSRPVRLDLGGANVSLDPETRERLSAALARPRHTAPQEADALAAQGPLGAELSALLRDATALASDVVTAGRRGRGAPTL 966
Cdd:COG3321 870 REDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAA 949
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 967 PRTGAGRPPHPRTGGTPAKNGADLRTAEPTTPEPQPQPQPLEATLHVSVDTMPYLLDHCFFRQPAQADPADRWPVVPGTT 1046
Cdd:COG3321 950 AAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLA 1029
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1047 VIAHLMEFAERAAPGRRAVAVHDVRLHQWITATPAVDIPVRIVPEGPDRVTASLGPYARAVVELAQDRPRFTPPGPWTFP 1126
Cdd:COG3321 1030 AAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLL 1109
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1127 AEREEKPELTAAELYSRRWMFHGPRFQGLAELTAVGDRHVRGVLVTPPAPGALLDNVGQLLGYWIMARQPVRTTVFPVGM 1206
Cdd:COG3321 1110 ALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAAL 1189
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1207 KEIRFHGPHPAPGERLECLIRITSVTDATLEADMQLVHRGRVWAEFSGWQDRRFDSNPRIRKVDREPERYTLSRMQPGGW 1286
Cdd:COG3321 1190 AGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAA 1269
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1287 ALVHEEWPDLATRELIMRNILAGEERERYAVHAPRGRRQWLLGRIAAKDAVRNVMWDAGAGPVYPAEVRVGNDPAGRPFV 1366
Cdd:COG3321 1270 GLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAA 1349
|
1450 1460 1470
....*....|....*....|....*....|
gi 1706746047 1367 TGGYGRTLPELHVSIAHRGETAVAMARAEG 1396
Cdd:COG3321 1350 AAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
7-472 |
4.52e-144 |
|
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: 447.77 E-value: 4.52e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 7 EPVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPPGRWDAEEYYAPGGEAraDRVYCRRGGFVDELAEVDVTEFGIMP 86
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKP--GKTYTRRGGFLDDVDAFDAAFFGISP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 87 AAVPATEPDQlialrvaaaaladaggqgRL-----------------PADRHRVGVVLGrggyltpglvrldqrvrtasq 149
Cdd:cd00833 79 REAEAMDPQQ------------------RLllevawealedagyspeSLAGSRTGVFVG--------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 150 lvrTLGELLPDLGADRLEAVRqaftdrlgpeaPESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELG 229
Cdd:cd00833 120 ---ASSSDYLELLARDPDEID-----------AYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 230 SGRCDVMLAGGVHHCHDITFWSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVA 309
Cdd:cd00833 186 SGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 310 SDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFGPPSTDASGdapdAVIGS 389
Cdd:cd00833 266 QDGRTKGITAPSGEAQAALIRRAYARAGVDPS---DIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQP----LLIGS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 390 VKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPAL--ARTRFTPIGAALPWRTDDRqpVRRAAVNAFGFGGIN 467
Cdd:cd00833 339 VKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIdfEESPLRVPTEARPWPAPAG--PRRAGVSSFGFGGTN 416
|
....*
gi 1706746047 468 AHVVL 472
Cdd:cd00833 417 AHVIL 421
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
8-915 |
5.17e-123 |
|
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: 427.50 E-value: 5.17e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 8 PVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPPGRWDAEEYYApGGEARADRVYCRRGGFVDELaEVDVTEFGIMPA 87
Cdd:TIGR02813 8 PIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYD-SDKSEADKSYCKRGGFLPEV-DFNPMEFGLPPN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 88 AVPATEPDQLIALRVAAAALADAGgqgrLPA--DRHRVGVVLGRGG---YLTPGLVRLDQRVrtasqlvrtLGELLPDLG 162
Cdd:TIGR02813 86 ILELTDISQLLSLVVAKEVLNDAG----LPDgyDRDKIGITLGVGGgqkQSSSLNARLQYPV---------LKKVFKASG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 163 ---ADRlEAVRQAFTDRLGPEAPESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAG 239
Cdd:TIGR02813 153 vedEDS-EMLIKKFQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 240 GVHHCHDITFWSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMA 319
Cdd:TIGR02813 232 GVCTDNSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 320 PDSGGQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFgppsTDASGDAPDAVIGSVKSMIGHTMP 399
Cdd:TIGR02813 312 PRPEGQAKALKRAYDDAGFAPH---TCGLIEAHGTGTAAGDVAEFGGLVSVF----SQDNDQKQHIALGSVKSQIGHTKS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 400 AAGVAGLIKAALAVHHQVLPPTLHCDDPHPAL--ARTRFTPIGAALPW--RTDDRQpvRRAAVNAFGFGGINAHVVLEEV 475
Cdd:TIGR02813 385 TAGTAGMIKAVLALHHKVLPPTINVDQPNPKLdiENSPFYLNTETRPWmqREDGTP--RRAGISSFGFGGTNFHMVLEEY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 476 AVARRPAEVYEPEPV---LRLTAPTPEAM-AALLDRSDSAIITAGLDE------------RAPATDPVRIAVVGPTAKRL 539
Cdd:TIGR02813 463 SPKHQRDDQYRQRAVaqtLLFTAANEKALvSSLKDWKNKLSAKADDQPyafnalaventlRTIAVALARLGFVAKNADEL 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 540 ------ALARKAVAKGKGWRGRGDVWFVPRPLLGpGGGRLAFVFPGLEAEFAPNSEDIARHFglPWSRAVTDATVGDVGR 613
Cdd:TIGR02813 543 itmleqAITQLEAKSCEEWQLPSGISYRKSALVV-ESGKVAALFAGQGSQYLNMGRELACNF--PEVRQAAADMDSVFTQ 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 614 QGTG----------VF--ELGRLLDTALR---------------------RLGVVPDALAGHSLGEWTAMAAAGIhpPEE 660
Cdd:TIGR02813 620 AGKGalspvlypipVFndESRKAQEEALTntqhaqsaigtlsmgqyklftQAGFKADMTAGHSFGELSALCAAGV--ISD 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 661 VDAFLADF-----------DPDALSVPGLAFAAIGAPsEVVLSELDGRGDVVLSHDNAPNQSMICGPEPAVAALVEVFRA 729
Cdd:TIGR02813 698 DDYMMLAFsrgqamaaptgEADIGFMYAVILAVVGSP-TVIANCIKDFEGVSIANYNSPTQLVIAGVSTQIQIAAKALKE 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 730 RAVISQILPFRSGFHTPMLEPYLDPIRKAAEAYTLRPAALPVWSATTVAPYPDEPAAIRELFIRHLLEPVRFRPLVETMY 809
Cdd:TIGR02813 777 KGFKAIPLPVSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMY 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 810 AAGFRAFVQLGAGQ-LGSLIDDTLHGR-DHLVVPAHSPHRPGLP--QLHRVASALWADGATPDlvpllggasTVTPARTV 885
Cdd:TIGR02813 857 AAGARVFVEFGPKNiLQKLVENTLKDKeNELCAISINPNPKGDSdmQLRQAAVQLAVLGLELT---------EIDPYQAE 927
|
970 980 990
....*....|....*....|....*....|...
gi 1706746047 886 RRP---SRPVRLDLGGANVsLDPETRERLSAAL 915
Cdd:TIGR02813 928 KRPpaaTSPMNIKLNAANY-ISPATRKKMDDSL 959
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
9-474 |
1.16e-78 |
|
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: 261.88 E-value: 1.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 9 VAIVGMSVLFPGAPDLATYWHNLVSGVDAItevppGRWDAEeyyapggearadrvycrrggFvdelaevdvteFGIMPAA 88
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDV-----DLFDAA--------------------F-----------FGISPRE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 89 VPATEPdqlialrvaaaaladaggQgrlpadrhrvgvvlgrggyltpglvrldQRvrtasqlvrtlgeLLpdlgadrLEA 168
Cdd:smart00825 45 AEAMDP------------------Q----------------------------QR-------------LL-------LEV 58
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 169 VRQAFtdrlgpeapESSiGLVPnlaaSRLAGR-------LDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGV 241
Cdd:smart00825 59 AWEAL---------EDA-GIDP----ESLRGSrtgvfvgVSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGGV 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 242 HHCHDITFWSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPD 321
Cdd:smart00825 125 NLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPS 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 322 SGGQVRavrqaweaagldpsapgsiglleahgtatpagdgtelttlaevfgppstdasgdapdavIGSVKSMIGHTMPAA 401
Cdd:smart00825 205 GPAQLL-----------------------------------------------------------IGSVKSNIGHLEAAA 225
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1706746047 402 GVAGLIKAALAVHHQVLPPTLHCDD--PHPALARTRFTPIGAALPWRTDDRqpVRRAAVNAFGFGGINAHVVLEE 474
Cdd:smart00825 226 GVAGLIKVVLALKHGVIPPTLHFETpnPHIDLEESPLRVPTELTPWPPPGR--PRRAGVSSFGFGGTNAHVILEE 298
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
9-472 |
9.57e-75 |
|
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: 255.02 E-value: 9.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 9 VAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPpgRWDAEEYYAP-GGEARA-------DRVYCRRGGfvdelaevDVT 80
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRPIT--RFDASGLPVRiAGEVKDfdpeeylDRKELRRMD--------RFT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 81 EFGIMpAAVPATEpdqlialrvaaaaladaggQGRL---PADRHRVGVVLGRGGyltpglvrldqrvrtasqlvrtlgel 157
Cdd:COG0304 73 QYALA-AAREALA-------------------DAGLdldEVDPDRTGVIIGSGI-------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 158 lpdLGADRLEAVRQAFTDRlGPEA--PESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDV 235
Cdd:COG0304 107 ---GGLDTLEEAYRALLEK-GPRRvsPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 236 MLAGGVHHCHDITFWSVFSQLGALS-----PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVAS 310
Cdd:COG0304 183 MIAGGAEAAITPLGLAGFDALGALStrnddPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASS 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 311 DGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSApgsIGLLEAHGTATPAGDGTELTTLAEVFGppstdasGDAPDAVIGSV 390
Cdd:COG0304 263 DAYHITAPAPDGEGAARAMRAALKDAGLSPED---IDYINAHGTSTPLGDAAETKAIKRVFG-------DHAYKVPVSST 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 391 KSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPALArTRFTPIGAAlpwrtddRQPVRRAAVNAFGFGGINAHV 470
Cdd:COG0304 333 KSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECD-LDYVPNEAR-------EAKIDYALSNSFGFGGHNASL 404
|
..
gi 1706746047 471 VL 472
Cdd:COG0304 405 VF 406
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
8-472 |
4.06e-70 |
|
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: 241.67 E-value: 4.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 8 PVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPpgRWDAEEYyapggearadrvYCRRGGFVDELAEVD--------- 78
Cdd:cd00834 2 RVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPIT--RFDASGF------------PSRIAGEVPDFDPEDyldrkelrr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 79 VTEFGIMpaAVPATEP--DQLIALRVAAaaladaggqgrlpaDRHRVGVVLGRGgylTPGLVRLDqrvrtasqlvrtlge 156
Cdd:cd00834 68 MDRFAQF--ALAAAEEalADAGLDPEEL--------------DPERIGVVIGSG---IGGLATIE--------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 157 llpdlgadrlEAVRQAFTDRLGPEAPESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVM 236
Cdd:cd00834 114 ----------EAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 237 LAGGVH-HCHDITFWSvFSQLGALS-----PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVAS 310
Cdd:cd00834 184 IAGGAEaLITPLTLAG-FAALRALStrnddPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASS 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 311 DGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSApgsIGLLEAHGTATPAGDGTELTTLAEVFGPpstdasgDAPDAVIGSV 390
Cdd:cd00834 263 DAYHITAPDPDGEGAARAMRAALADAGLSPED---IDYINAHGTSTPLNDAAESKAIKRVFGE-------HAKKVPVSST 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 391 KSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPAlARTRFTPIGAAlpwrtddRQPVRRAAVNAFGFGGINAHV 470
Cdd:cd00834 333 KSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPE-CDLDYVPNEAR-------EAPIRYALSNSFGFGGHNASL 404
|
..
gi 1706746047 471 VL 472
Cdd:cd00834 405 VF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
187-472 |
4.71e-54 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 195.01 E-value: 4.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 187 GLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHChdITFWSV--FSQLGALS---- 260
Cdd:TIGR03150 134 MSIINMAAGQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAA--ITPLGIagFAAMKALStrnd 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 261 -PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLD 339
Cdd:TIGR03150 212 dPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGIN 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 340 PSapgSIGLLEAHGTATPAGDGTELTTLAEVFGppstdasGDAPDAVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLP 419
Cdd:TIGR03150 292 PE---DVDYINAHGTSTPLGDKAETKAIKKVFG-------DHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVP 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1706746047 420 PTLHCDDPHPALARTrFTPIGAalpwrtddRQ-PVRRAAVNAFGFGGINAHVVL 472
Cdd:TIGR03150 362 PTINLDNPDPECDLD-YVPNEA--------REaKIDYALSNSFGFGGTNASLVF 406
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
7-292 |
3.70e-50 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 178.21 E-value: 3.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 7 EPVAIVGMSVLFPGAPDLATYWHNLVSGVDAITEVPPGRWDAEEYYAPGGEArADRVYCRRGGfVDELAEVDVTEFGIMP 86
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRI-AGKIYTKWGG-LDDIFDFDPLFFGISP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 87 AAVPATEPDQLIALRVAAAALADAGgqgrLPADR---HRVGVVLGRGGYLTPGLVRLDqrvrtasqlvrtlgellpdlGA 163
Cdd:pfam00109 79 REAERMDPQQRLLLEAAWEALEDAG----ITPDSldgSRTGVFIGSGIGDYAALLLLD--------------------ED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 164 DRLEAVRQAFTdrlgpeapessiGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVH- 242
Cdd:pfam00109 135 GGPRRGSPFAV------------GTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNl 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1706746047 243 HCHDITFwSVFSQLGALSPSERIRPFDRGADGVLIGEGTGVVVLKRLADA 292
Cdd:pfam00109 203 LLTPLGF-AGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
191-468 |
1.33e-49 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 182.58 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 191 NLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHCHDITFWSVFSQLGALS------PSER 264
Cdd:PTZ00050 145 NMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQRA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 265 IRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSApg 344
Cdd:PTZ00050 225 SRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANININ-- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 345 SIGLLEAHGTATPAGDGTELTTLAEVFGPpstdasGDAPDAVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHC 424
Cdd:PTZ00050 303 DVDYVNAHATSTPIGDKIELKAIKKVFGD------SGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINL 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1706746047 425 DDPHPALArTRFTPIGAALPwrtddRQPVRRAAVNAFGFGGINA 468
Cdd:PTZ00050 377 ENPDAECD-LNLVQGKTAHP-----LQSIDAVLSTSFGFGGVNT 414
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
167-472 |
2.41e-49 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 181.73 E-value: 2.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 167 EAVRQafTDRLGPE--APESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHC 244
Cdd:PRK06333 126 EAVRT--LDSRGPRrlSPFTIPSFLTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 245 HDITFWSVFSQLGALS------PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLM 318
Cdd:PRK06333 204 IDRVSLAGFAAARALStrfndaPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 319 APDSGGQVRAVRQAWEAAGLdpsAPGSIGLLEAHGTATPAGDGTELTTLAEVFGPPSTDAsgdapdavIGSVKSMIGHTM 398
Cdd:PRK06333 284 PEDGEGARRAMLIALRQAGI---PPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSGLA--------VSSTKSATGHLL 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706746047 399 PAAGVAGLIKAALAVHHQVLPPTLHCDDPHPALARTRFTPiGAALPWrtddrqPVRRAAVNAFGFGGINAHVVL 472
Cdd:PRK06333 353 GAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVA-NKARPM------DMDYALSNGFGFGGVNASILF 419
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
187-476 |
1.39e-48 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 179.21 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 187 GLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHChdITFWSV--FSQLGALS---- 260
Cdd:PRK07314 135 MAIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAA--ITPLGIagFAAARALStrnd 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 261 -PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLD 339
Cdd:PRK07314 213 dPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGIN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 340 PSApgsIGLLEAHGTATPAGDGTELTTLAEVFGppstdasGDAPDAVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLP 419
Cdd:PRK07314 293 PED---IDYINAHGTSTPAGDKAETQAIKRVFG-------EHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIP 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706746047 420 PTLHCDDPHPALA------RTRFTPIGAALpwrtddrqpvrraaVNAFGFGGINAHVVLEEVA 476
Cdd:PRK07314 363 PTINLDNPDEECDldyvpnEARERKIDYAL--------------SNSFGFGGTNASLVFKRYE 411
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
188-472 |
4.81e-46 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 172.67 E-value: 4.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 188 LVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHCHDITFWSVFSQLGALS------P 261
Cdd:PLN02836 158 ILINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStkfnscP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 262 SERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPS 341
Cdd:PLN02836 238 TEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPN 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 342 apgSIGLLEAHGTATPAGDGTELTTLAEVFGPPSTDASgdapdAVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPT 421
Cdd:PLN02836 318 ---QVDYVNAHATSTPLGDAVEARAIKTVFSEHATSGG-----LAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPT 389
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1706746047 422 LHCDDPHPALaRTRFTPIGAAlpwrtdDRQPVRRAAVNAFGFGGINAHVVL 472
Cdd:PLN02836 390 LNLERPDPIF-DDGFVPLTAS------KAMLIRAALSNSFGFGGTNASLLF 433
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
188-472 |
7.35e-44 |
|
"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: 165.30 E-value: 7.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 188 LVPNLAASRLAGRLDL-RGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHH-CHDITFWsvFSQLGALS----- 260
Cdd:cd00828 135 LSPNTVAGWVNILLLSsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDpLEEGLSG--FANMGALStaeee 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 261 PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPdSGGQVRAVRQAWEAAGLDP 340
Cdd:cd00828 213 PEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 341 SApgsIGLLEAHGTATPAGDGTELTTLAEVFGPpstdasGDAPDAVIgSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPP 420
Cdd:cd00828 292 DD---LDVISAHGTSTPANDVAESRAIAEVAGA------LGAPLPVT-AQKALFGHSKGAAGALQLIGALQSLEHGLIPP 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1706746047 421 TLHCDDPHPALARTRFTpiGAALPWRTDDRQpvrrAAVNAFGFGGINAHVVL 472
Cdd:cd00828 362 TANLDDVDPDVEHLSVV--GLSRDLNLKVRA----ALVNAFGFGGSNAALVL 407
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
182-472 |
1.64e-43 |
|
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: 162.03 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 182 PESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHCHDITFWSVFSQLGALSP 261
Cdd:cd00825 64 PYVVTKAMFPGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 262 SERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLDps 341
Cdd:cd00825 144 EKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLT-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 342 aPGSIGLLEAHGTATPAGDGTELTTLAEVFGPPSTdasgdapdaVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPT 421
Cdd:cd00825 222 -VWDIDYLVAHGTGTPIGDVKELKLLRSEFGDKSP---------AVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPS 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1706746047 422 LHCDDPHPALARTrftpigaalPWRTDDRQPvRRAAVNAFGFGGINAHVVL 472
Cdd:cd00825 292 IHIEELDEAGLNI---------VTETTPREL-RTALLNGFGLGGTNATLVL 332
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
201-473 |
7.24e-42 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 159.43 E-value: 7.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 201 LDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVhhCHDITFWSV--FSQLGALS-------PSERIRPFDRG 271
Cdd:PRK07103 154 FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGA--LMDLSYWECqaLRSLGAMGsdrfadePEAACRPFDQD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 272 ADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGrtTSLMAPDSGGQVRAVRQAWEAAGLdpsAPGSIGLLEA 351
Cdd:PRK07103 232 RDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA--NRGPDPSLEGEMRVIRAALRRAGL---GPEDIDYVNP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 352 HGTATPAGDGTELTTLaevfgppstDASGdAPDAVIGSVKSMIGHTMPAAGVAGLIKAALavhhQVLPPTLHcddPHPAL 431
Cdd:PRK07103 307 HGTGSPLGDETELAAL---------FASG-LAHAWINATKSLTGHGLSAAGIVELIATLL----QMRAGFLH---PSRNL 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1706746047 432 ARtrftPIGAALPWRTDDRQP--VRRAAVNAFGFGGINAHVVLE 473
Cdd:PRK07103 370 DE----PIDERFRWVGSTAESarIRYALSLSFGFGGINTALVLE 409
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
300-425 |
9.94e-40 |
|
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: 143.48 E-value: 9.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 300 YAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPsapGSIGLLEAHGTATPAGDGTELTTLAEVFGPPSTDAS 379
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDP---EDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKQP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1706746047 380 gdapdAVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCD 425
Cdd:pfam02801 78 -----LAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
162-475 |
4.08e-39 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 151.69 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 162 GADRLEAVRQAFTDRlGPEapESSIGLVPNLAASRLAGRLD----LRGPAYTVDAACASSLIAVDHAVRELGSGRCDVML 237
Cdd:PRK08722 111 GLGLIEAGHQALVEK-GPR--KVSPFFVPSTIVNMIAGNLSimrgLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 238 AGGVHHCHDITFWSVFSQLGALS-----PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDG 312
Cdd:PRK08722 188 AGGAEKASTPLGMAGFGAAKALStrndePQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 313 RTTSLMAPDSGGQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFGPPSTDasgdapDAVIGSVKS 392
Cdd:PRK08722 268 YHMTSPSEDGSGGALAMEAAMRDAGVTGE---QIGYVNAHGTSTPAGDVAEIKGIKRALGEAGSK------QVLVSSTKS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 393 MIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPALARTrftpigaALPWRTDDRQPVRRAAVNAFGFGGINAHVVL 472
Cdd:PRK08722 339 MTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDID-------LVPHTARKVESMEYAICNSFGFGGTNGSLIF 411
|
...
gi 1706746047 473 EEV 475
Cdd:PRK08722 412 KKM 414
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
176-472 |
4.74e-39 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 151.36 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 176 RLGPEApessiglVPNLAASR----LAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGvhhCHDITfWS 251
Cdd:PRK07967 127 RVGPYA-------VTKAMASTvsacLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGG---GEELD-WE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 252 V---FSQLGALS------PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGrtTSLMAPDS 322
Cdd:PRK07967 196 MsclFDAMGALStkyndtPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDG--YDMVAPSG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 323 GGQVRAVRQAweAAGLDpsapGSIGLLEAHGTATPAGDGTELTTLAEVFG---PPstdasgdapdavIGSVKSMIGHTMP 399
Cdd:PRK07967 274 EGAVRCMQMA--LATVD----TPIDYINTHGTSTPVGDVKELGAIREVFGdksPA------------ISATKSLTGHSLG 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706746047 400 AAGVAGLIKAALAVHHQVLPPTLHCDDPHPALArtrftpiGAALPWRTDDRQPVRRAAVNAFGFGGINAHVVL 472
Cdd:PRK07967 336 AAGVQEAIYSLLMMEHGFIAPSANIEELDPQAA-------GMPIVTETTDNAELTTVMSNSFGFGGTNATLVF 401
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
197-472 |
8.77e-39 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 149.99 E-value: 8.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 197 LAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHCHDITFWSvFSQLGALSPsERIRPFDRGADGVL 276
Cdd:PRK09185 143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNG-FNSLESLSP-QPCRPFSANRDGIN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 277 IGEGTGVVVLKRLADAErdgdriyAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLDPSApgsIGLLEAHGTAT 356
Cdd:PRK09185 221 IGEAAAFFLLEREDDAA-------VALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPAD---IGYINLHGTAT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 357 PAGDGTELTTLAEVFGpPSTDASgdapdavigSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPALartrf 436
Cdd:PRK09185 291 PLNDAMESRAVAAVFG-DGVPCS---------STKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPAL----- 355
|
250 260 270
....*....|....*....|....*....|....*..
gi 1706746047 437 tpigAALPWRTD-DRQPVRRAAVNAFGFGGINAHVVL 472
Cdd:PRK09185 356 ----PPLYLVENaQALAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
168-473 |
6.39e-36 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 140.25 E-value: 6.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 168 AVRQafTDRLGPE--APESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHCH 245
Cdd:PRK14691 45 AVRT--SDSRGPKrlSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 246 DITFWSVFSQLGALS------PSERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMA 319
Cdd:PRK14691 123 DTVSLAGFAAARALSthfnstPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 320 PDSGGQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFGPPSTDAsgdapdavIGSVKSMIGHTMP 399
Cdd:PRK14691 203 EDGDGAYRAMKIALRQAGITPE---QVQHLNAHATSTPVGDLGEINAIKHLFGESNALA--------ITSTKSATGHLLG 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706746047 400 AAGVAGLIKAALAVHHQVLPPTLHCDDPHPAlARTRFTPIGAALPwrtddrQPVRRAAVNAFGFGGINAHVVLE 473
Cdd:PRK14691 272 AAGGLETIFTVLALRDQIVPATLNLENPDPA-AKGLNIIAGNAQP------HDMTYALSNGFGFAGVNASILLK 338
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
194-482 |
1.79e-35 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 140.92 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 194 ASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGvhhchdiTFWSV-------FSQLGALS-----P 261
Cdd:PRK06501 155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIA-------TDGSVsaealirFSLLSALStqndpP 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 262 SERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDG--RTTSlmAPDSGGQVRAVRQAWEAAGLD 339
Cdd:PRK06501 228 EKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhRTRS--SPDGSPAIGAIRAALADAGLT 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 340 PSApgsIGLLEAHGTATPAGDGTELTTLAEVFGppstDASGDAPdavIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLP 419
Cdd:PRK06501 306 PEQ---IDYINAHGTSTPENDKMEYLGLSAVFG----ERLASIP---VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLP 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706746047 420 PTLHCDDPHPALartrftPIGaALPWRTDDrQPVRRAAVNAFGFGGINAHVVLeevavARRPA 482
Cdd:PRK06501 376 PTINYDNPDPAI------PLD-VVPNVARD-ARVTAVLSNSFGFGGQNASLVL-----TAEPA 425
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
169-472 |
1.84e-34 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 137.11 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 169 VRQAFTDRLGPEA---PESSIGLVPNLAASRLAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHch 245
Cdd:PRK05952 98 ARQMYQGDDSPDEeldLENWLDTLPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEA-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 246 DITFWSV--FSQLGALSPsERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDSG 323
Cdd:PRK05952 176 PITPLTLagFQQMGALAK-TGAYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 324 GQVRAVRQAWEAAGLDPSapgSIGLLEAHGTATPAGDGTELTTLAEVFGppstdasgdaPDAVIGSVKSMIGHTMPAAGV 403
Cdd:PRK05952 255 SAIAAIQQCLARSGLTPE---DIDYIHAHGTATRLNDQREANLIQALFP----------HRVAVSSTKGATGHTLGASGA 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706746047 404 AGLIKAALAVHHQVLPPTLHCDDPHPALartRFTpigaalpwRTDDRQPVRRAAVNAFGFGGINAHVVL 472
Cdd:PRK05952 322 LGVAFSLLALRHQQLPPCVGLQEPEFDL---NFV--------RQAQQSPLQNVLCLSFGFGGQNAAIAL 379
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
628-822 |
1.32e-33 |
|
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: 132.56 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 628 ALRRLGVVPDALAGHSLGEWTAMAAAGihppeevdAFlaDFDpDALS------------VP----GLAfAAIGAPSEVVL 691
Cdd:COG0331 75 ALEEEGIRPDAVAGHSLGEYSALVAAG--------AL--SFE-DALRlvrlrgrlmqeaVPagpgGMA-AVLGLDDEEVE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 692 S---ELDGRGDVVLSHDNAPNQSMICGPEPAVAALVEVFRAR-AVISQILPFRSGFHTPMLEPYLDPIRKAAEAYTLRPA 767
Cdd:COG0331 143 AlcaEAAQGEVVEIANYNSPGQIVISGEKEAVEAAAELAKEAgAKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADP 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1706746047 768 ALPVWSATTVAPYPDePAAIRELFIRHLLEPVRFRPLVETMYAAGFRAFVQLGAG 822
Cdd:COG0331 223 KIPVVSNVDAAPVTD-PEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPG 276
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
202-467 |
5.74e-33 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 133.19 E-value: 5.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 202 DLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHChDITFWSVFSQLGALS-----PSERIRPFDRGADGVL 276
Cdd:PRK09116 152 GLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEEL-CPTEAAVFDTLFATStrndaPELTPRPFDANRDGLV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 277 IGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSlmAPDSGGQVRAVRQAWEAAGLDPSApgsIGLLEAHGTAT 356
Cdd:PRK09116 231 IGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVT--QPQAETMQIAMELALKDAGLAPED---IGYVNAHGTAT 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 357 PAGDGTELTTLAEVFGPpstdasgDAPdavIGSVKSMIGHTMpaaGVAGLIKAALAV---HHQVLPPTLHCDDPHPALAR 433
Cdd:PRK09116 306 DRGDIAESQATAAVFGA-------RMP---ISSLKSYFGHTL---GACGALEAWMSIemmNEGWFAPTLNLTQVDPACGA 372
|
250 260 270
....*....|....*....|....*....|....
gi 1706746047 434 TRFTPIGAalpwRTDDRQPVrraAVNAFGFGGIN 467
Cdd:PRK09116 373 LDYIMGEA----REIDTEYV---MSNNFAFGGIN 399
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
203-475 |
9.28e-31 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 126.77 E-value: 9.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 203 LRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVhhchDITFWSV----FSQLGALS-----PSERIRPFDRGAD 273
Cdd:PRK08439 151 LKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGA----ESAICPVgiggFAAMKALStrnddPKKASRPFDKDRD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 274 GVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDsgGQVRAVRQAWEAAGLDPsapgsIGLLEAHG 353
Cdd:PRK08439 227 GFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNPK-----IDYINAHG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 354 TATPAGDGTELTTLAEVFG-----PPstdasgdapdavIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLH----- 423
Cdd:PRK08439 300 TSTPYNDKNETAALKELFGskekvPP------------VSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINqetpd 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1706746047 424 --CD-DPHPALARtrftpigaalpwrtddRQPVRRAAVNAFGFGGINAHVVLEEV 475
Cdd:PRK08439 368 peCDlDYIPNVAR----------------KAELNVVMSNSFGFGGTNGVVIFKKV 406
|
|
| Sfp |
COG2091 |
Phosphopantetheinyl transferase [Coenzyme transport and metabolism]; |
1303-1466 |
2.90e-28 |
|
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
Pssm-ID: 441694 Cd Length: 177 Bit Score: 112.75 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1303 MRNILAGEERERYA-VHAPRGRRQWLLGRIAAKDAVrnvmwdAGAGPVYPAEVRVGNDPAGRPFVTGgygrtlPELHVSI 1381
Cdd:COG2091 25 LLALLSEDERARAArFRSEKRRRRFLAGRALLRELL------ARLLGLPPADLEFAYDPHGKPYLAD------PGLHFSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1382 AHRGETAVAMARAEGPCGIDIEEVTDRPEGTLA-VALTTAERELLTSLvhrpGGAPERLWFTRFWAAKEAVAKARGTGLG 1460
Cdd:COG2091 93 SHSGGLAAVAVSRGGPVGVDIERIRPRIDLALArRFFSPEERAWLAAL----PQDDRLEAFTRLWTLKEALLKATGTGLS 168
|
....*.
gi 1706746047 1461 GEPKRF 1466
Cdd:COG2091 169 LPLRAL 174
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
589-842 |
4.30e-28 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 115.96 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 589 EDIARHFGLPWSRAVTDATVGDVGRQGTGV-------FE--LGRLLdtalRRLGVVPDALAGHSLGEWTAMAAAGIhppe 659
Cdd:smart00827 31 DAALQPLLGWSLLDVLLGEDGAASLLDTEVaqpalfaVQvaLARLL----RSWGVRPDAVVGHSSGEIAAAYVAGV---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 660 evdafladFD-PDALSV------------PGLAFAAIGAPSEVVLSELDGRGD-VVLSHDNAPNQSMICGPEPAVAALVE 725
Cdd:smart00827 103 --------LSlEDAARLvaargrlmqalpGGGAMLAVGLSEEEVEPLLAGVPDrVSVAAVNSPSSVVLSGDEDAVDELAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 726 VFRARAVISQILPFRSGFHTPMLEPYLDPIRKAAEAYTLRPAALPVWSATTVAPYPDEPAAIRELFIRHLLEPVRFRPLV 805
Cdd:smart00827 175 RLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELDDADYWVRNLREPVRFADAV 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1706746047 806 ETMYAA-GFRAFVQLGAGQ-LGSLIDDTL-HGRDHLVVPA 842
Cdd:smart00827 255 RALLAEgGVTVFLEVGPHPvLTGPIKQTLaAAGSAVVLPS 294
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
191-472 |
8.65e-28 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 120.08 E-value: 8.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 191 NLAASRLAGRLDLRGPAYTVDAACASS----LIAVDHAVRelgsGRCDVMLAGGVHHCHDITFWSVFSQLGALS-----P 261
Cdd:PLN02787 268 NMGSAMLAMDLGWMGPNYSISTACATSnfciLNAANHIIR----GEADVMLCGGSDAAIIPIGLGGFVACRALSqrnddP 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 262 SERIRPFDRGADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPDSGGQVRAVRQAWEAAGLdps 341
Cdd:PLN02787 344 TKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGV--- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 342 APGSIGLLEAHGTATPAGDGTELTTLAEVFgppstdasGDAPDAVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPT 421
Cdd:PLN02787 421 SKEDVNYINAHATSTKAGDLKEYQALMRCF--------GQNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPN 492
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1706746047 422 LHCDDPHPALARTRFtpIGAalpwrTDDRQPVRRAAVNAFGFGGINAHVVL 472
Cdd:PLN02787 493 INLENPESGVDTKVL--VGP-----KKERLDIKVALSNSFGFGGHNSSILF 536
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
193-472 |
1.88e-27 |
|
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: 112.92 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 193 AASRLAGRLDLR-GPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHChditfwsvfsqlgalspserirpfdrg 271
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF--------------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 272 adgvLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMaPDSGGQVRAVRQAWEAAGLDPSapgSIGLLEA 351
Cdd:cd00327 99 ----VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPA-VSGEGLARAARKALEGAGLTPS---DIDYVEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 352 HGTATPAGDGTELTTLAEVFGPPSTDasgdapdavIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTlhcddphpal 431
Cdd:cd00327 171 HGTGTPIGDAVELALGLDPDGVRSPA---------VSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1706746047 432 artrftpigaalpwrtddRQPVRRAAVNAFGFGGINAHVVL 472
Cdd:cd00327 232 ------------------PREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
122-467 |
7.37e-26 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 112.13 E-value: 7.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 122 RVGVVLGRGGYLTPGLVRLDQR-----VRTASQLVRTLGELLPDLGADRLEAVRQAFTDRLGPEAPESSIGLvpnlaasr 196
Cdd:PRK07910 85 RMSTVLGRRVWENAGSPEVDTNrlmvsIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGL-------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 197 lagRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHHCHDITFWSVFSQLGAL------SPSERIRPFDR 270
Cdd:PRK07910 157 ---ERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVmstnndDPAGACRPFDK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 271 GADGVLIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGrtTSLMAPDSGGQ--VRAVRQAWEAAGLdpsAPGSIGL 348
Cdd:PRK07910 234 DRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDG--FHMVAPDPNGEraGHAMTRAIELAGL---TPGDIDH 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 349 LEAHGTATPAGDgtelttLAEvfGPPSTDASGDAPDAVIGSvKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPH 428
Cdd:PRK07910 309 VNAHATGTSVGD------VAE--GKAINNALGGHRPAVYAP-KSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLD 379
|
330 340 350
....*....|....*....|....*....|....*....
gi 1706746047 429 PALArtrfTPIGAALPWRTDdrqpVRRAAVNAFGFGGIN 467
Cdd:PRK07910 380 PEID----LDVVAGEPRPGN----YRYAINNSFGFGGHN 410
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
200-472 |
2.93e-24 |
|
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: 107.06 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 200 RLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCdVMLAGGVHHCHDITFWSVFSQLGALSPSER----IRPFDRGADGV 275
Cdd:cd00832 147 RHGMRGPSGVVVAEQAGGLDALAQARRLVRRGTP-LVVSGGVDSALCPWGWVAQLSSGRLSTSDDparaYLPFDAAAAGY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 276 LIGEGTGVVVLKRLADAERDGDRIYAAITGTGVASDGRTTSLMAPdsgGQVRAVRQAWEAAGLdpsAPGSIGLLEAHGTA 355
Cdd:cd00832 226 VPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPP---GLARAIRLALADAGL---TPEDVDVVFADAAG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 356 TPAGDGTELTTLAEVFGP---PSTdasgdAPdavigsvKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLHCDDPHPALa 432
Cdd:cd00832 300 VPELDRAEAAALAAVFGPrgvPVT-----AP-------KTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAY- 366
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1706746047 433 rtrftpiGAALPWRTDDRQPVRRAAVNAFGFGGINAHVVL 472
Cdd:cd00832 367 -------GLDLVTGRPRPAALRTALVLARGRGGFNSALVV 399
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
633-822 |
8.60e-19 |
|
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: 88.68 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 633 GVVPDALAGHSLGEWTAMAAAGihppeevdAFlaDFDpDAL------------SVP---GLAFAAIGAPSEVVLSELD-- 695
Cdd:TIGR00128 81 GLKPDFAAGHSLGEYSALVAAG--------AL--DFE-TALklvkkrgelmqeAVPeggGAMAAVIGLDEEQLAQACEea 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 696 GRGDVVLSHDNAPNQSMICGPEPAVAALVEVFRARAViSQILPFR-SG-FHTPMLEPYLDPIRKAAEAYTLRPAALPVWS 773
Cdd:TIGR00128 150 TENDVDLANFNSPGQVVISGTKDGVEAAAALFKEMGA-KRAVPLEvSGaFHSRFMKPAAEKFAETLEACQFNDPTVPVIS 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1706746047 774 ATTVAPYpDEPAAIRELFIRHLLEPVRFRPLVETMYAAGFRAFVQLGAG 822
Cdd:TIGR00128 229 NVDAKPY-TNGDRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPG 276
|
|
| PS-DH |
pfam14765 |
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ... |
1012-1262 |
4.27e-17 |
|
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: 83.58 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1012 HVSVDTMPYLLDHCFFRQPaqadpadrwpVVPGTTVIAHLMEFAERAAPGRRAVAVHDVRLHQWITATP--AVDIPVRIV 1089
Cdd:pfam14765 21 RLRLADLPWLRDHRVGGTV----------VLPGAGYLEMALEAARQLFGGSGAVALRDVSILKALVLPEddPVEVQTSLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1090 PEGPDRVT------ASLGP-------YARAVVELAQDRPRFTPPGPWTFPAEREE--KPELTAAELY---SRRWMFHGPR 1151
Cdd:pfam14765 91 PEEDGADSwwefeiFSRAGggwewtlHATGTVRLAPGEPAAPVDLESLPARCAQPadPRSVSSAEFYerlAARGLFYGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1152 FQGLAELTAvGDRHVRGVLVTPPAPG----------ALLDNVGQLLGYWIMARQPV-RTTVFPVGMKEIRFHGPHPaPGE 1220
Cdd:pfam14765 171 FQGLRRIWR-GDGEALAEARLPEAAAggespyllhpALLDAALQLLGAALPAEAEHaDQAYLPVGIERLRIYRSLP-PGE 248
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1706746047 1221 RLECLIRITSVTDATLEADMQLVHR-GRVWAEFSGWQDRRFDS 1262
Cdd:pfam14765 249 PLWVHARLERRGGRTIVGDLTLVDEdGRVVARIEGLRLRRVER 291
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
637-823 |
1.84e-16 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 82.50 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 637 DALAGHSLGEWTAMAAAG----------IHPPEEVDAFLADFDPDA-LSVPGLAFAAIGAPSEVVLSELDGRGDVVLSHD 705
Cdd:PLN02752 126 DVCAGLSLGEYTALVFAGalsfedglklVKLRGEAMQAAADAGPSGmVSVIGLDSDKVQELCAAANEEVGEDDVVQIANY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 706 NAPNQSMICGPEP---AVAALVEVFRARAVIsqILPFRSGFHTPMLEPYLDPIRKAAEAYTLRPAALPVWSATTVAPYPD 782
Cdd:PLN02752 206 LCPGNYAVSGGKKgidAVEAKAKSFKARMTV--RLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNVDAQPHSD 283
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1706746047 783 ePAAIRELFIRHLLEPVRFRPLVETMYAAGFRAFVQLGAGQ 823
Cdd:PLN02752 284 -PATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGK 323
|
|
| ACPS |
pfam01648 |
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ... |
1397-1485 |
4.77e-14 |
|
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Pssm-ID: 426364 [Multi-domain] Cd Length: 111 Bit Score: 69.94 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1397 PCGIDIEEVTD-------RPEGTLAVALTTAERELLTSLvhrpgGAPERLWFTRFWAAKEAVAKARGTGLGG--EPKRFE 1467
Cdd:pfam01648 1 GVGIDIEEIARirrpierLGERLAERIFTPEERALLASL-----PAEARRAFARLWTAKEAVFKALGPGLSKllDFDDIE 75
|
90
....*....|....*...
gi 1706746047 1468 ITSVDGDRLTVRTAGEEY 1485
Cdd:pfam01648 76 VLLDPDGRPTLRLLGEAA 93
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
629-819 |
1.40e-13 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 73.66 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 629 LRRLGVVPDALAGHSLGEWTAMAAAGIHPPEE--VDAFLADFDPDALSVPGlAFAAIGAPSEVVlsELDGRGDVVLSHDN 706
Cdd:pfam00698 77 LQSYGVRPDAVVGHSLGEYAAAVVAGALSPEEalLAAVLRSRLMMQLAGPG-GMAAVELSAEEV--EQRWPDDVVGAVVN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 707 APNQSMICGPEPAVAALVEVFRARAVISQILPFRSGFHTPMLEPYLDPIRKAAEAYTLRPAALPVWSATTVAPYpDEPAA 786
Cdd:pfam00698 154 SPRSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPS-DQRTL 232
|
170 180 190
....*....|....*....|....*....|...
gi 1706746047 787 IRELFIRHLLEPVRFRPLVETMYAAGFRAFVQL 819
Cdd:pfam00698 233 SAEYWVRNLRSPVRFAEAILSAAEPGPLVFIEI 265
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
429-507 |
6.91e-12 |
|
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: 63.72 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 429 PALARTRFTPIGAALPWrtddrqPVRRAAVNAFGFGGINAHVVLEEVAVARRPAEVYEPEPVL-RLTAPTPEAMAALLDR 507
Cdd:pfam16197 6 PALLDGRLKVVTEPTPW------PGGIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLvLLSGRTEEAVKALLEK 79
|
|
| EntD |
COG2977 |
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ... |
1307-1454 |
2.78e-09 |
|
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442216 [Multi-domain] Cd Length: 205 Bit Score: 58.77 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1307 LAGEERERYAVHAPRGRRQWLLGRIAAKDAVRnvmwDAGagpVYPAEVRVGND-----PAGrpfVTGgygrtlpelhvSI 1381
Cdd:COG2977 12 LGPPEPAALARAVPKRRAEFLAGRLCARRALA----ELG---VPPAPILIGEDraplwPAG---VVG-----------SI 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706746047 1382 AHRGETAVAMARAEGPC---GIDIEEVTD--RPEGTLAVALTTAERELLTSLVHRPGGaperLWFTRFWAAKEAVAKA 1454
Cdd:COG2977 71 SHSDGYAAAVVAPASDVrglGIDIEPLLDepLAEELLPSILTPAERALLAALSPLPFA----HALTLLFSAKESLYKA 144
|
|
| acpS |
PRK00070 |
4'-phosphopantetheinyl transferase; Provisional |
1303-1397 |
2.89e-06 |
|
4'-phosphopantetheinyl transferase; Provisional
Pssm-ID: 234610 [Multi-domain] Cd Length: 126 Bit Score: 47.82 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1303 MRNILAGEERERYAVHAPRGRRqwLLGRIAAKDAV---------RNVMWdagagpvypAEVRVGNDPAGRPFV--TGGYG 1371
Cdd:PRK00070 27 AERVLTPKERAKFKSGKRPAEF--LAGRFAAKEAFskalgtgigKGVSF---------RDIEVLNDELGKPIVrlSGEAA 95
|
90 100 110
....*....|....*....|....*....|.
gi 1706746047 1372 RTLPEL-----HVSIAHRGETAVAMARAEGP 1397
Cdd:PRK00070 96 ERLEKLggariHLSISHDGDYAVAFVILESL 126
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
185-243 |
1.02e-05 |
|
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: 49.53 E-value: 1.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706746047 185 SIGLVPNLA--ASRLAGrLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHH 243
Cdd:TIGR01930 53 QAGEQQNIArqAALLAG-LPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVES 112
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
190-241 |
1.18e-05 |
|
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: 49.29 E-value: 1.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1706746047 190 PNLA--ASRLAGrLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGV 241
Cdd:COG0183 63 QNPArqAALLAG-LPESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGV 115
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
187-241 |
1.72e-05 |
|
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: 49.01 E-value: 1.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1706746047 187 GLVPNLA--ASRLAGrLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGV 241
Cdd:cd00751 56 GEGQNPArqAALLAG-LPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGV 111
|
|
| pantethn_trn |
TIGR00556 |
phosphopantetheine--protein transferase domain; This model models a domain active in ... |
1396-1508 |
2.30e-05 |
|
phosphopantetheine--protein transferase domain; This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics. [Protein fate, Protein modification and repair]
Pssm-ID: 273136 [Multi-domain] Cd Length: 128 Bit Score: 45.51 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1396 GPCGIDIEEVT------DRPEGTLAVALTTAERELLTSLvhrpGGAPERLWFTRFWAAKEAVAKARGTGLGGEP---KRF 1466
Cdd:TIGR00556 3 VGIGIDIVEIKriaeqiERSGTFAERFFTPSEIEDYCKL----SPKSQTESLAGRWAAKEAFIKALGKGISLGEllfTDI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1706746047 1467 EITSVDGDRLTVRTAGE-EYRVRHCALTTPRPSAGPDKEYVVA 1508
Cdd:TIGR00556 79 EIVKDLKGAPRVCLIGEaAKDAEKLGVCSVHVSISHDKEYAAA 121
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
152-341 |
2.41e-05 |
|
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: 48.41 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 152 RTLGELLPDLGAdrlEAVRQAFTD-RLGPEAPESSI------GLVPNLAASRLAGRLDLRG-PAYTVDAACASSLIAVDH 223
Cdd:cd00829 10 RRSDRSPLELAA---EAARAALDDaGLEPADIDAVVvgnaagGRFQSFPGALIAEYLGLLGkPATRVEAAGASGSAAVRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 224 AVRELGSGRCDVMLAGGV-HHCHDITFWSVFSQLGALSPSERIRPFDRGA------------------------------ 272
Cdd:cd00829 87 AAAAIASGLADVVLVVGAeKMSDVPTGDEAGGRASDLEWEGPEPPGGLTPpalyalaarrymhrygttredlakvavknh 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 273 ---------------------------------DGVLIGEGTGVVVLKRLADAERDGDRiYAAITGTGVASDGRTTSLMA 319
Cdd:cd00829 167 rnaarnpyaqfrkpitvedvlnsrmiadplrllDCCPVSDGAAAVVLASEERARELTDR-PVWILGVGAASDTPSLSERD 245
|
250 260
....*....|....*....|....
gi 1706746047 320 PDSG--GQVRAVRQAWEAAGLDPS 341
Cdd:cd00829 246 DFLSldAARLAARRAYKMAGITPD 269
|
|
| PRK10351 |
PRK10351 |
4'-phosphopantetheinyl transferase AcpT; |
1319-1497 |
4.08e-05 |
|
4'-phosphopantetheinyl transferase AcpT;
Pssm-ID: 182399 [Multi-domain] Cd Length: 187 Bit Score: 45.98 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1319 APRGRRQ--WLLGRiaakdavrnVMWDAGAGPVYPAEVrvgnDPAGRPFVTGGygrtlPELHVSIAHRGETAVAMARAEG 1396
Cdd:PRK10351 17 APQGPRRarWLAGR---------VLLSHALSPLPEIIY----GEQGKPAFAPE-----TPLWFNLSHSGDDIALLLSDEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1397 PCGIDIEEVTDRPE-GTLAVALTTAERELLTSLVHrPGGAPERLWftRFWAAKEAVAKARGTGLggepkrFEITSVDGdr 1475
Cdd:PRK10351 79 EVGCDIEVIRPRANwRSLANAVFSLGEHAEMDAVH-PEQQLEAFW--RIWTRKEAIVKQRGGSA------WQIVSVDS-- 147
|
170 180
....*....|....*....|....*....
gi 1706746047 1476 ltvrTAGEEYRVRHC-------ALTTPRP 1497
Cdd:PRK10351 148 ----TLPSALSVSHCqlenlslAVCTPTP 172
|
|
| AcpS |
COG0736 |
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]; |
1399-1483 |
6.63e-05 |
|
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
Pssm-ID: 440499 [Multi-domain] Cd Length: 122 Bit Score: 43.96 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1399 GIDIEEVtDRPEGTLAVA--------LTTAERELLTSLVHRPggapERLWfTRFwAAKEAVAKARGTGLGGE--PKRFEI 1468
Cdd:COG0736 3 GIDIVEI-ARIERALERHgerflervFTPAERAYCQSRKRPA----EFLA-GRF-AAKEAVSKALGTGIGKGvsWRDIEV 75
|
90
....*....|....*
gi 1706746047 1469 TSVDGDRLTVRTAGE 1483
Cdd:COG0736 76 LNDPSGKPTVRLSGR 90
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
197-243 |
9.05e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 46.64 E-value: 9.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1706746047 197 LAGRLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHH 243
Cdd:PRK06445 78 FLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEH 124
|
|
| AcpS |
COG0736 |
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]; |
1306-1396 |
1.21e-04 |
|
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
Pssm-ID: 440499 [Multi-domain] Cd Length: 122 Bit Score: 43.19 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1306 ILAGEERERYAVHAPRGRRqwLLGRIAAKDAVRNVMwdaGAG---PVYPAEVRVGNDPAGRPFV--TGGYGRTLPEL--- 1377
Cdd:COG0736 27 VFTPAERAYCQSRKRPAEF--LAGRFAAKEAVSKAL---GTGigkGVSWRDIEVLNDPSGKPTVrlSGRAAELAAELgit 101
|
90 100
....*....|....*....|.
gi 1706746047 1378 --HVSIAHRGETAVAMARAEG 1396
Cdd:COG0736 102 riHLSISHERDYAVAFVILEA 122
|
|
| acpS |
PRK14663 |
holo-[acyl-carrier-protein] synthase; |
1329-1392 |
1.47e-04 |
|
holo-[acyl-carrier-protein] synthase;
Pssm-ID: 237781 [Multi-domain] Cd Length: 116 Bit Score: 42.90 E-value: 1.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1706746047 1329 GRIAAKDAVRNVMWDAGAGPVYPAEVRVGNDPAGRPFVTGGYGRTLPE---LHVSIAHRGETAVAMA 1392
Cdd:PRK14663 45 GRFAAKEAVVKALGTGFSQGVHWKSFAILNDAAGRPFVKVIDDGCLPPgcvIKISISHDRHSAVATA 111
|
|
| acpS |
PRK00070 |
4'-phosphopantetheinyl transferase; Provisional |
1399-1483 |
6.00e-04 |
|
4'-phosphopantetheinyl transferase; Provisional
Pssm-ID: 234610 [Multi-domain] Cd Length: 126 Bit Score: 41.27 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 1399 GID------IEEVTDRPEGTLA--VaLTTAERELLTSLVHRPggaperlwftRF----WAAKEAVAKARGTGLGGEP--K 1464
Cdd:PRK00070 6 GIDiveierIEKALERTGDRFAerV-LTPKERAKFKSGKRPA----------EFlagrFAAKEAFSKALGTGIGKGVsfR 74
|
90
....*....|....*....
gi 1706746047 1465 RFEITSVDGDRLTVRTAGE 1483
Cdd:PRK00070 75 DIEVLNDELGKPIVRLSGE 93
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
179-241 |
1.15e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 43.08 E-value: 1.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706746047 179 PEAPESSIGLVpnlAASRLAgrLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGV 241
Cdd:PRK08170 59 PSPDEANIARV---VALRLG--CGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGV 116
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
183-241 |
2.70e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 41.92 E-value: 2.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1706746047 183 ESSIGLVPNLAASRLAGrLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGV 241
Cdd:PRK06366 58 QAGVGQNPAGQAAYHAG-LPFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGM 115
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
193-243 |
3.04e-03 |
|
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: 41.13 E-value: 3.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1706746047 193 AASRLAGrLDLRGPAYTVDAACASSLIAVDHAVRELGSGRCDVMLAGGVHH 243
Cdd:pfam00108 65 QAALKAG-IPDSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVES 114
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
215-429 |
5.99e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 40.71 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 215 ASSLIAVDHAVRELGSGRCDVMLAGGVHHCHDITFWSVFSQLGALSPSERIRPFDRG---ADGVLIGEGTGVVVLKRLAD 291
Cdd:PRK06519 176 SAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKGGWAPVWSRGgedGGGFILGSGGAFLVLESREH 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706746047 292 AERDGDRIYAAITGtgVASDgrttslMAPDSGGQVRA-VRQAWEAAGLDPsAPGSI--GLLEAHGTATpagdgTELTTLA 368
Cdd:PRK06519 256 AEARGARPYARISG--VESD------RARRAPGDLEAsLERLLKPAGGLA-APTAVisGATGAHPATA-----EEKAALE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706746047 369 evfgppstdasgDAPDAVIGSVKSMIGHTMPAAGVAGLIKAALAVHHQVLPPTLhcdDPHP 429
Cdd:PRK06519 322 ------------AALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPF---DASG 367
|
|
| |
