|
Name |
Accession |
Description |
Interval |
E-value |
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
499-1071 |
0e+00 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 611.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 499 HWAAQeiTQNKALYTWINEGGAVGCQRTYAELDSNASCVAHKLLTSRKPtikpGDRVLLVHVPGLDFIDAFFGCLRAKVI 578
Cdd:cd05931 1 RRAAA--RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 579 PIPVLPPDPlqrgGQALTKIENIAKLCNAVAILSTVGYHAAVRAGLVknlisftgksvkSTGQWPNLPWLHTDSWikssk 658
Cdd:cd05931 75 AVPLPPPTP----GRHAERLAAILADAGPRVVLTTAAALAAVRAFAA------------SRPAAGTPRLLVVDLL----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 659 VLPASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAM 738
Cdd:cd05931 134 PDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 739 ACGGSAILFSPLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEAdkAKARNYDLSSMIFFMIAAEPVRQKTLKRF 818
Cdd:cd05931 214 YSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRD--EDLEGLDLSSWRVALNGAEPVRPATLRRF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 819 VELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKPILV-------------------DWQGRICCGYVDPndaDVDIRI 879
Cdd:cd05931 292 AEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRPLP---DQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 880 VDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRnKLQNYPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAG 959
Cdd:cd05931 369 VDPETGREL-PDGEVGEIWVRGPSVASGYWGRPEATAETFG-ALAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 960 RNIYSADVEKTVESSSELLRPGCCAVIGVPEEvlsakgislpdasDEVGLVVIAEL--RDSKLVNKDIIKQIESRVAEEH 1037
Cdd:cd05931 447 RNHYPQDIEATAEEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREH 513
|
570 580 590
....*....|....*....|....*....|....
gi 1917948728 1038 GVTVASVKLIRPRTISKTTSGKIKRFECLKQFVD 1071
Cdd:cd05931 514 GVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
1720-2046 |
6.70e-125 |
|
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.
Pssm-ID: 163707 Cd Length: 328 Bit Score: 396.80 E-value: 6.70e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1720 EEMDPKYKKIVGNLAANLAATTLKVKSRYFHRIGVSGKGYLKLYDDIQgLPEHDIFGPGKRYTVIVRHSNSLSADDDARL 1799
Cdd:cd08151 1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1800 DARGAALRILS---DDSPLLDLTLKTGKAFYARTISDFATWLVCGLAAREEHVKRV-PHVRDAVWTSLRQA-DSFADLHY 1874
Cdd:cd08151 80 DGRGAALRFLNagdDDAGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLRRApDSYTDLHY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1875 YSNTCRLFRFKDRQEMYVKFKLRPSDENIEEDIGKVEPSGILPPETGAIPRDANDTRPLLFLAEDFHNRVKSPsGVRYIF 1954
Cdd:cd08151 160 YSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1955 QLQVRPIPQDeaARDIALDCTKPWDESQFPYIDVGEVIINENLTKEGSEKLEVNPfLRCHEVDVIRATSSSQ-SASIDHG 2033
Cdd:cd08151 239 QIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGHL 315
|
330
....*....|...
gi 1917948728 2034 RSLIYEICQHLRN 2046
Cdd:cd08151 316 RSLVYEISQRLRK 328
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
487-1079 |
3.51e-96 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 325.92 E-value: 3.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 487 FPNLPTLDCYLKHWAaqEITQNKALYTWIN---EGGAVGCQRTYAELDSNASCVAHKLltsrKPTIKPGDRVLLVHVPGL 563
Cdd:PRK07769 17 FPPNTNLVRHVERWA--KVRGDKLAYRFLDfstERDGVARDLTWSQFGARNRAVGARL----QQVTKPGDRVAILAPQNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 564 DFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIENiaklCNAVAILSTVGYHAAVRAgLVKNLISFTGKSVKSTGQWP 643
Cdd:PRK07769 91 DYLIAFFGALYAGRIAVPLFDPAEPGHVGRLHAVLDD----CTPSAILTTTDSAEGVRK-FFRARPAKERPRVIAVDAVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 644 NLpwlhtdswIKSSKVLPASNIafqsesqpDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLP 723
Cdd:PRK07769 166 DE--------VGATWVPPEANE--------DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 724 QYHDMGLIGGLFTAMaCGGSAILFSPLTFIRNPLMWLQTIS----DYKATHSAGPNFAFELVIRRlEADKAKARNYDLSS 799
Cdd:PRK07769 230 FFHDMGLITVLLPAL-LGHYITFMSPAAFVRRPGRWIRELArkpgGTGGTFSAAPNFAFEHAAAR-GLPKDGEPPLDLSN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 800 MIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKP--ILVDWQ----GRIC--------- 864
Cdd:PRK07769 308 VKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPtvIYVDRDelnaGRFVevpadapna 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 865 -----CGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQNY----------PGR 929
Cdd:PRK07769 388 vaqvsAGKVGVSEWAV---IVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRlseshaegapDDA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 930 KYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGVPEEVLSAK-------GISL-P 1001
Cdd:PRK07769 464 LWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVvfddshaGLKFdP 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1002 DASDEvGLVVIAELR--DSKLVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGNL----- 1074
Cdd:PRK07769 544 EDTSE-QLVIVAERApgAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSLrsgyg 622
|
....*.
gi 1917948728 1075 -NTVPD 1079
Cdd:PRK07769 623 qPAFPD 628
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
526-1069 |
7.82e-95 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 319.97 E-value: 7.82e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSRKPtikpGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPdplqRGGQALTKIENIAKLC 605
Cdd:PRK05850 37 TWSQLYRRTLNVAEELRRHGST----GDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVP----QGGAHDERVSAVLRDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTvgyhAAVRAGLVKNLISFTGKSVKSTGQwpnLPWLHTDSWIKS-SKVLPASNIAFqsesqpddlcfLQFTSG 684
Cdd:PRK05850 109 SPSVVLTT----SAVVDDVTEYVAPQPGQSAPPVIE---VDLLDLDSPRGSdARPRDLPSTAY-----------LQYTSG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 685 STSDAKGVMITHGGLIHNV-KLMRRRYRST-----SNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLM 758
Cdd:PRK05850 171 STRTPAGVMVSHRNVIANFeQLMSDYFGDTggvppPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRPAR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 759 WLQTISDYKATHSAGPNFAFELVIRRL-EADKAkarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYG 837
Cdd:PRK05850 251 WMQLLASNPHAFSAAPNFAFELAVRKTsDDDMA---GLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 838 LAENCVFVSCAYGKKKPILVDW--------QGRIC--------CGYVDPNDADVdiRIVDADTGLEVdEDGKEGEIWISS 901
Cdd:PRK05850 328 LAEATVYVATREPGQPPESVRFdyeklsagHAKRCetgggtplVSYGSPRSPTV--RIVDPDTCIEC-PAGTVGEIWVHG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 902 PSAGIGYWGKEELSQKTFRNKLQN----YPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVEsssEL 977
Cdd:PRK05850 405 DNVAAGYWQKPEETERTFGATLVDpspgTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQ---EI 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 978 LRpGCCAVIGVPEevlsakgislpDASDEvgLVVIAELR------DSKLVNKDIIK-QIESRVAEEHGVTVASVKLIRPR 1050
Cdd:PRK05850 482 TG-GRVAAISVPD-----------DGTEK--LVAIIELKkrgdsdEEAMDRLRTVKrEVTSAISKSHGLSVADLVLVAPG 547
|
570
....*....|....*....
gi 1917948728 1051 TISKTTSGKIKRFECLKQF 1069
Cdd:PRK05850 548 SIPITTSGKIRRAACVEQY 566
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
507-1200 |
1.42e-92 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 337.53 E-value: 1.42e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 507 QNKALYT-------WINEGGAVGCQRTYAELDSNASCVAHKLLTSrkptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIP 579
Cdd:PRK05691 16 QRRAAQTpdrlalrFLADDPGEGVVLSYRDLDLRARTIAAALQAR----ASFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 580 IPVLPPDPLQRGGQAltkieniaKLCNAVA-----ILSTVgyhaavrAGLVKNLISFtgksvkSTGQWPNLP-WLHTDSw 653
Cdd:PRK05691 92 VPAYPPESARRHHQE--------RLLSIIAdaeprLLLTV-------ADLRDSLLQM------EELAAANAPeLLCVDT- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 654 iksskVLPASNIAFQSES-QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT--VLVSWLPQYHDMGL 730
Cdd:PRK05691 150 -----LDPALAEAWQEPAlQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddVIVSWLPLYHDMGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 731 IGGLFTAMACGGSAILFSPLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLeADKAKARnYDLSSMIFFMIAAEPV 810
Cdd:PRK05691 225 IGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERV-SESALER-LDLSRWRVAYSGSEPI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 811 RQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAY-GKKKPIL-VDWQG-------------RICCGYVDPNDAdv 875
Cdd:PRK05691 303 RQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRrGQGIPALeLDAEAlarnraepgtgsvLMSCGRSQPGHA-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 876 dIRIVDADTgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklQNYPGRKYTRTGDLGWVIQGNLFITGRIKDLI 955
Cdd:PRK05691 381 -VLIVDPQS-LEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGRTWLRTGDLGFLRDGELFVTGRLKDML 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 956 IVAGRNIYSADVEKTVESSSELLRPGCCAVIGVPEEVLSAKGISLpDASDEVGLVVIAElrdsklvnkDIIKQIESRVAE 1035
Cdd:PRK05691 455 IVRGHNLYPQDIEKTVEREVEVVRKGRVAAFAVNHQGEEGIGIAA-EISRSVQKILPPQ---------ALIKSIRQAVAE 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1036 EHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGNLntvpDPIVTKRSLTrsfttgtcregktprSHLAKSSLAPSP 1115
Cdd:PRK05691 525 ACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----DSYALFPALQ---------------AVEAAQTAASGD 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1116 KLSNRNIVEFLKQLISEQtgisiqnISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANFAENLLM 1195
Cdd:PRK05691 586 ELQARIAAIWCEQLKVEQ-------VAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLA 658
|
....*
gi 1917948728 1196 KSQPH 1200
Cdd:PRK05691 659 GGGAA 663
|
|
| FAAL_FadD32 |
NF038339 |
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ... |
479-1074 |
1.91e-92 |
|
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.
Pssm-ID: 468483 [Multi-domain] Cd Length: 625 Bit Score: 314.74 E-value: 1.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 479 LSETSGVVFPNLPTLDCYLKHWAAQEitQNKALYTWIN---EGGAVGCQRTYAELDSNASCVAHKLltsrKPTIKPGDRV 555
Cdd:NF038339 6 LDENGNIRFPDGATLVDHVERNARER--ADTLAYRFIDysrERDGEARDLTWAQFGARLRAVAARL----QQVTKPGDRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 556 LLVHVPGLDFIDAFFGCLRAKVIPIPVLPPD-PLQRGgqaltKIENIAKLCNAVAILSTVGYHAAVRAgLVKNLISFTGK 634
Cdd:NF038339 80 AILAPQGLDYVVSFFAAIYAGNIAVPLFDPDePGHTD-----RLHAVLGDCKPSAILTATSSAEGVRK-FFRSLPAKERP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 635 SVKSTGQWPnlpwlhtDSwIKSSKVLPASNIafqsesqpDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS 714
Cdd:NF038339 154 RVIAVDAVP-------DS-VGSTWVRPDADL--------DDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 715 NTVLVSWLPQYHDMGLIGGLFTAMacGGSAILF-SPLTFIRNPLMW---LQTISDYKATHSAGPNFAFELVIRR-LEADk 789
Cdd:NF038339 218 NSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWireLAAVSDGAGTFAAAPNFAFEHAAARgLPKE- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 790 akARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKP--ILVDW----QGRI 863
Cdd:NF038339 295 --GEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAkvIYVDReelnAGRI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 864 --------------CCGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQNY--- 926
Cdd:NF038339 373 vevdpdapnavaqvSCGYVARSQWAV---IVDPETGTEL-PDGQVGEIWLHGNNIGTGYWGRPEETEETFHNKLKSRlee 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 927 --------PGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGV-----PEEVL 993
Cdd:NF038339 449 gshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVpanqlPAEVF 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 994 SAKGISL---PDASDEvGLVVIAElR---DSKLVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLK 1067
Cdd:NF038339 529 ENSHSGLkydADDSSE-QLVIVAE-RapgAGKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACKA 606
|
....*..
gi 1917948728 1068 QFVDGNL 1074
Cdd:NF038339 607 AYIDGTL 613
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
522-1076 |
5.54e-86 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 289.79 E-value: 5.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENI 601
Cdd:COG0318 22 GRRLTYAELDARARRLAAAL---RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEE-------LAYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 602 AKLCNAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpddlCFLQF 681
Cdd:COG0318 92 LEDSGARALVT----------------------------------------------------------------ALILY 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTfirnplm 758
Cdd:COG0318 108 TSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLlprFDPER------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 759 WLQTISDYKATHSAG-PNFAFELvirrleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLsqeVMAPGYG 837
Cdd:COG0318 181 VLELIERERVTVLFGvPTMLARL------LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEER---FGV---RIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 838 LAENCVFVSCAygkkkPILVDWQGRICCGYVDPNdadVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQK 917
Cdd:COG0318 249 LTETSPVVTVN-----PEDPGERRPGSVGRPLPG---VEVRIVDED-GREL-PPGEVGEIVVRGPNVMKGYWNDPEATAE 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 918 TFRNklqnypGrkYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVLsak 996
Cdd:COG0318 319 AFRD------G--WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVVGVPDEKW--- 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 997 gislpdasDEVGLVVIAELRDSKLVNKDIIKQIESRVAeEHGVtvasvklirPRTIS------KTTSGKIKRFECLKQFV 1070
Cdd:COG0318 385 --------GERVVAFVVLRPGAELDAEELRAFLRERLA-RYKV---------PRRVEfvdelpRTASGKIDRRALRERYA 446
|
....*.
gi 1917948728 1071 DGNLNT 1076
Cdd:COG0318 447 AGALEA 452
|
|
| FadD32_Coryne |
NF040633 |
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ... |
550-1071 |
1.74e-85 |
|
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.
Pssm-ID: 468603 [Multi-domain] Cd Length: 613 Bit Score: 293.87 E-value: 1.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 550 KPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLppDPLQRG-GQALTkieniAKL--CNAVAILSTVGYHAAVRAGLvk 626
Cdd:NF040633 84 KPGDRVAILANNSPEYIFGFLGALYAGMVPVPLY--DPNEPGhADHLR-----AVLadSGPTVVLTNKTSAPAVRAHF-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 627 nlisftgkSVKSTGQWP------NLPWLHTDSWIKSSKVLPASNIAFQSESQP-DDLCFLQFTSGSTSDAKGVMITHGGL 699
Cdd:NF040633 155 --------ADLPAAERPrilsvdSLPDSLAESWVNPMATIEGQPLLAPAGTDPsDDTAFLQYTSGSTRTPAGVVLTNRSI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 700 IHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMACGGSAILFSPLTFIRNPLMWLQTIS---DYKATHSAGPNF 776
Cdd:NF040633 227 VTNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSrreDDVNVYTVVPNF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 777 AFELVIRRleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKPiL 856
Cdd:NF040633 306 ALELAARY--ANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERP-L 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 857 VDWQGR--ICCGYVDPNDADVD----------------IRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKT 918
Cdd:NF040633 383 FTYFDReaLAEGRAVEVAEDSEnavpfasngqvvrpqvLAIVDPETGQEL-PDGTVGEIWVHGDNMAAGYLDREEETAET 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 919 FRNKL----------QNYPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGV 988
Cdd:NF040633 462 FRNTLgerlaensraEGAPEDNWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAV 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 989 PeevlsakgislpdASDEVGLVVIAELRDSKLVNKD--IIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECL 1066
Cdd:NF040633 542 P-------------GDDVEKLVILAERDDEADESGDaeAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNA 608
|
....*
gi 1917948728 1067 KQFVD 1071
Cdd:NF040633 609 KAYLE 613
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
479-1074 |
1.68e-82 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 285.10 E-value: 1.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 479 LSETSGVVFPNLPTLDCYLKHWAAqeITQNKALYTWIN-EGGAVGC--QRTYAELDSNASCVAHKLltsrKPTIKPGDRV 555
Cdd:PRK12476 22 LDADGNIALPPGTTLISLIERNIA--NVGDTVAYRYLDhSHSAAGCavELTWTQLGVRLRAVGARL----QQVAGPGDRV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 556 LLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDpLQrgGQAlTKIENIAKLCNAVAILSTVGYHAAVRAGLVKnlisftgks 635
Cdd:PRK12476 96 AILAPQGIDYVAGFFAAIKAGTIAVPLFAPE-LP--GHA-ERLDTALRDAEPTVVLTTTAAAEAVEGFLRN--------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 636 vkstgqwpnLPWLHTDSWIKSSKVLPASNIAFQ-SESQPDDLCFLQFTSGSTSDAKGVMITHGG-------LIHNVKLMR 707
Cdd:PRK12476 163 ---------LPRLRRPRVIAIDAIPDSAGESFVpVELDTDDVSHLQYTSGSTRPPVGVEITHRAvgtnlvqMILSIDLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 708 RryrstsNTVLVSWLPQYHDMGLIGGLFTAMaCGGSAILFSPLTFIRNPLMWLQTISD---YKATHSAGPNFAFELVIRR 784
Cdd:PRK12476 234 R------NTHGVSWLPLYHDMGLSMIGFPAV-YGGHSTLMSPTAFVRRPQRWIKALSEgsrTGRVVTAAPNFAYEWAAQR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 785 -LEADKAkarNYDLSSMIfFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKKKP--ILVDWQ- 860
Cdd:PRK12476 307 gLPAEGD---DIDLSNVV-LIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPsvVYLDREq 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 861 ---GR--------------ICCGYVDPNDADVdirIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKL 923
Cdd:PRK12476 383 lgaGRavrvaadapnavahVSCGQVARSQWAV---IVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 924 QNY-----------PGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVIGVPeev 992
Cdd:PRK12476 459 QSRlaegshadgaaDDGTWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVP--- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 993 lsakgislpdASDEVGLVVIAElRDSKLVNKD---IIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQF 1069
Cdd:PRK12476 536 ----------AEDNERLVIVAE-RAAGTSRADpapAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQY 604
|
....*
gi 1917948728 1070 VDGNL 1074
Cdd:PRK12476 605 LDGRL 609
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
527-1072 |
1.23e-81 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 281.51 E-value: 1.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 527 YAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlpPDPLQRGGQA--LTKIENIAKL 604
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL---GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPMGFGGREsyIAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 605 CNAVAILSTVGyhaavraglvknLISFTGKSVKSTgqwpNLPWLHTDSWIKSskvLPASNIAFQsESQPDDLCFLQFTSG 684
Cdd:PRK09192 127 AQPAAIITPDE------------LLPWVNEATHGN----PLLHVLSHAWFKA---LPEADVALP-RPTPDDIAYLQYSSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 685 STSDAKGVMITHGGLIHNVK-------LMRRRYRStsntvlVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPL 757
Cdd:PRK09192 187 STRFPRGVIITHRALMANLRaishdglKVRPGDRC------VSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 758 MWLQTISDYKATHSAGPNFAFELVIRRL-EADKAkarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGY 836
Cdd:PRK09192 261 QWLDLISRNRGTISYSPPFGYELCARRVnSKDLA---ELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 837 GLAENCVFVSCA----------------YGKKKPILVDWQGR-----ICCGYVDPnDADVDIRivdadtglevDEDGKE- 894
Cdd:PRK09192 338 GLAEATLAVSFSplgsgivveevdrdrlEYQGKAVAPGAETRrvrtfVNCGKALP-GHEIEIR----------NEAGMPl 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 895 -----GEIWISSPSAGIGYWGKEElSQKTFR--NKLQnypgrkytrTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADV 967
Cdd:PRK09192 407 pervvGHICVRGPSLMSGYFRDEE-SQDVLAadGWLD---------TGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 968 EKTVESSSElLRPGCCAVIGVPEEvlsakgislpdasDEVGLVVIAELRDSKLVNK-DIIKQIESRVAEEHGVTVaSVKL 1046
Cdd:PRK09192 477 EWIAEQEPE-LRSGDAAAFSIAQE-------------NGEKIVLLVQCRISDEERRgQLIHALAALVRSEFGVEA-AVEL 541
|
570 580
....*....|....*....|....*.
gi 1917948728 1047 IRPRTISKTTSGKIKRFECLKQFVDG 1072
Cdd:PRK09192 542 VPPHSLPRTSSGKLSRAKAKKRYLSG 567
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
525-1072 |
1.69e-76 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 265.30 E-value: 1.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 525 RTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIENIAKL 604
Cdd:cd05906 40 QSYQDLLEDARRLAAGL---RQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 605 CNAVAILSTVGYHAAVRaglvknlisftgksvKSTGQWPNLPWlhTDSWIKSSKVLPASNIAFQSesQPDDLCFLQFTSG 684
Cdd:cd05906 117 LGSPVVLTDAELVAEFA---------------GLETLSGLPGI--RVLSIEELLDTAADHDLPQS--RPDDLALLMLTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 685 STSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLMWLQTIS 764
Cdd:cd05906 178 STGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLID 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 765 DYKATHSAGPNFAFELVIRRLEADKAkaRNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENC-- 842
Cdd:cd05906 258 RYRVTITWAPNFAFALLNDLLEEIED--GTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCsg 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 843 --VFVSCAYGKKKPILVdwqgRICCGYVDPNdadVDIRIVDADTGLEvdEDGKEGEIWISSPSAGIGYWGKEELSQKTFR 920
Cdd:cd05906 336 viYSRSFPTYDHSQALE----FVSLGRPIPG---VSMRIVDDEGQLL--PEGEVGRLQVRGPVVTKGYYNNPEANAEAFT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 921 NKlqnypgrKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCAVigvpeevlsakgiSL 1000
Cdd:cd05906 407 ED-------GWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAF-------------AV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 1001 PDASDEVGLVVIAELRDSKLVNK--DIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDG 1072
Cdd:cd05906 467 RDPGAETEELAIFFVPEYDLQDAlsETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| FAAL_FadD21 |
NF038337 |
fatty-acid--AMP ligase FAAL21/FadD21; |
526-1069 |
2.34e-76 |
|
fatty-acid--AMP ligase FAAL21/FadD21;
Pssm-ID: 439631 [Multi-domain] Cd Length: 579 Bit Score: 266.36 E-value: 2.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltSRKPTIkpGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPlqrgGQALTKIENIAKLC 605
Cdd:NF038337 40 TWAQLYRRTLNVAHEV--RRHGTT--GDRAVILAPQGLPYIVAFLGAMQAGLIAVPLSVPQP----GSHDERVSAVLADT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTVGYHAAVraglvknlisftGKSVKSTGQWPNLPWLHTDSWiksskVLPASNIAFQSESQPDDLCFLQFTSGS 685
Cdd:NF038337 112 SPSVVLTTSAAAAAV------------AEYLHRPDTGAVPAVIEIDSL-----DLDGPNSPSIRISDAPSIAYLQYTSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSN------TVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLMW 759
Cdd:NF038337 175 TRLPAGVMVSHRNLQVNFQQLMAAYFPDTNgvaprdTTIVSWLPFYHDMGLVLGVIAPILGGYRSELTSPVAFLQRPARW 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 760 LQTISDYKATHSAGPNFAFELVIRRL-EADKAkarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGL 838
Cdd:NF038337 255 IHAMANGSPVFSAAPNFAFELAVRKTtDADLA---GLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFREDMMQPSYGL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 839 AENCVFVSCAYGKKKPILVDWQ-GRICCGYVDPNDADVD-------------IRIVDADTGLEVdEDGKEGEIWISSPSA 904
Cdd:NF038337 332 AEATVYVASRAEGGAPEVVHFEpEKLSEGSAQRCEARTGspllsygtptsptVRIVDPDTCIEC-PAGTVGEIWVHGDNV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 905 GIGYWGKEELSQKTFRNKLQN----YPGRKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESsselLRP 980
Cdd:NF038337 411 AEGYWQKPEETRRTFGGVLANpspgTPEGPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIESTVQE----ITG 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 981 GCCAVIGVPeevlsakgislpdaSDEV-GLVVIAELR-----DSKLVNK-DIIK-QIESRVAEEHGVTVASVKLIRPRTI 1052
Cdd:NF038337 487 GRVAAISVP--------------VDETeKLVTIIELKkrgdsDEEAMRKlDAVKnNVTAAISRSHGLNVADLVLVPPGSI 552
|
570
....*....|....*..
gi 1917948728 1053 SKTTSGKIKRFECLKQF 1069
Cdd:NF038337 553 PTTTSGKIRRAACVEQY 569
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
670-1062 |
1.84e-75 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 262.62 E-value: 1.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLVSWLPQYHDMGLIGGLFTAMACGGSAILFS 748
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETdVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 749 PLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEAdKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLS 828
Cdd:PRK07768 228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRR-QAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 829 QEVMAPGYGLAENCVFVSCAygkkkpilvdwqgRICCGY-VDPNDADV---DIRIVDAD--------------TGLE--- 887
Cdd:PRK07768 307 PEAILPAYGMAEATLAVSFS-------------PCGAGLvVDEVDADLlaaLRRAVPATkgntrrlatlgpplPGLEvrv 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 888 VDEDGKE------GEIWISSPSAGIGYwgkeeLSQKTFRnKLQNYPGrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGR 960
Cdd:PRK07768 374 VDEDGQVlpprgvGVIELRGESVTPGY-----LTMDGFI-PAQDADG--WLDTGDLGYLTEeGEVVVCGRVKDVIIMAGR 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 961 NIYSADVEKTVeSSSELLRPGCCAVIGVPeevlsakgisLPDASDEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVT 1040
Cdd:PRK07768 446 NIYPTDIERAA-ARVEGVRPGNAVAVRLD----------AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVR 514
|
410 420
....*....|....*....|..
gi 1917948728 1041 VASVKLIRPRTISKTTSGKIKR 1062
Cdd:PRK07768 515 PRNVVVLGPGSIPKTPSGKLRR 536
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
526-958 |
1.99e-69 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 240.68 E-value: 1.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHkLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:pfam00501 23 TYRELDERANRLAA-GLRALG--VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE-------LAYILEDS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLHTDSWIKSSKVLPASNIafqsesQPDDLCFLQFTSGS 685
Cdd:pfam00501 93 GAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP------DPDDLAYIIYTSGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRS----TSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFiRNPLMWLQ 761
Cdd:pfam00501 167 TGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 762 TISDYKATHSAGPNFAFELVirrleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVMAPGYGLAEN 841
Cdd:pfam00501 246 LIERYKVTVLYGVPTLLNML-----LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG------ALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 842 CVFVSCAYgkkkPILVDWQGRICCGYVDPNdadVDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRN 921
Cdd:pfam00501 315 TGVVTTPL----PLDEDLRSLGSVGRPLPG---TEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPELTAEAFDE 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 1917948728 922 KlqnypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIVA 958
Cdd:pfam00501 387 D-------GWYRTGDLGrRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
675-1061 |
8.71e-65 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 224.47 E-value: 8.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 675 DLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdMGLIGGLFTAMACGGSAILFSPltfiR 754
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPK----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 755 NPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKakarnYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVMAP 834
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAG-----YDLSSLRALVSGGAPLPPELLERFEEAPGI------KLVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 GYGLAENCVFVSCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDADTGLevDEDGKEGEIWISSPSAGIGYWGKEEL 914
Cdd:cd04433 145 GYGLTETGGTVATGPPDDDARKPGSVGRPV--------PGVEVRIVDPDGGE--LPPGEIGELVVRGPSVMKGYWNNPEA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 915 SQKTFRNklqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEevl 993
Cdd:cd04433 215 TAAVDED--------GWYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE---AAVVGVPD--- 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728 994 sakgislPDASDEVGLVViaELRDSKLVNKDIIKQIesrVAEEHGVTVASVKLIRPRTISKTTSGKIK 1061
Cdd:cd04433 281 -------PEWGERVVAVV--VLRPGADLDAEELRAH---VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
526-1072 |
2.76e-62 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 222.75 E-value: 2.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlPPDPLQRGGQALTKIENIAklc 605
Cdd:cd05908 17 SYRHLREEALGYLGAL---QELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV-SIGSNEEHKLKLNKVWNTL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 navailstvgyhaavraglvknlisftgksvkstgqwpNLPWLhtdswIKSSKVLpasniafqsESQPDDLCFLQFTSGS 685
Cdd:cd05908 90 --------------------------------------KNPYL-----ITEEEVL---------CELADELAFIQFSSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTFIRNPLMWLQTISD 765
Cdd:cd05908 118 TGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 766 YKATHSAGPNFAFELVIRRLEADKAKarNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFV 845
Cdd:cd05908 198 HKATIVSSPNFGYKYFLKTLKPEKAN--DWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASVGA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 846 SCA-----------------YGKKKPiLVDWQGRICCGYVDPNDA--DVDIRIVDADTglEVDEDGKEGEIWISSPSAGI 906
Cdd:cd05908 276 SLPkaqspfktitlgrrhvtHGEPEP-EVDKKDSECLTFVEVGKPidETDIRICDEDN--KILPDGYIGHIQIRGKNVTP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 907 GYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESssellrpgccaVI 986
Cdd:cd05908 353 GYYNNPEATAKVFTDD-------GWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEE-----------LE 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 987 GVpeevlsakgislpdasdEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVTVA-------------SVKLIRP-RTI 1052
Cdd:cd05908 415 GV-----------------ELGRVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGkkikkhlnkrggwQINEVLPiRRI 477
|
570 580
....*....|....*....|
gi 1917948728 1053 SKTTSGKIKRFECLKQFVDG 1072
Cdd:cd05908 478 PKTTSGKVKRYELAQRYQSG 497
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
511-1078 |
2.00e-55 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 204.50 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 511 LYTWINEGGAVGCQRTYAELDSNASCVAHKLLTsrKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQR 590
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQK--KVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 591 GGQALTkIENIAKLCNAVAILstvgyhaavRAGLVKNLISFT-GKSVKSTGqWPNLPWLHTdswIKSSKVLPASNIAFQS 669
Cdd:cd05905 79 LGFLLG-TCKVRVALTVEACL---------KGLPKKLLKSKTaAEIAKKKG-WPKILDFVK---IPKSKRSKLKKWGPHP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSP 749
Cdd:cd05905 145 PTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 750 LTFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKA--KARNYDLSSMIFFMIAAE-PVRQKTLKRFVELTRPFG 826
Cdd:cd05905 225 ELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLAslKNRDVNLSSLRMCMVPCEnRPRISSCDSFLKLFQTLG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 827 LSQEVMAPGYGlaenCVFVScaygkkkpiLVDWQG----RICCGYVDPN------------DA-------DVDIRIVDAD 883
Cdd:cd05905 305 LSPRAVSTEFG----TRVNP---------FICWQGtsgpEPSRVYLDMRalrhgvvrlderDKpnslplqDSGKVLPGAQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 884 TGLeVDEDGKE-------GEIWISSPSAGIGYWG--KEELSQKTFRNKLQNYPGRK---YTRTGDLGWVIQGN------- 944
Cdd:cd05905 372 VAI-VNPETKGlckdgeiGEIWVNSPANASGYFLldGETNDTFKVFPSTRLSTGITnnsYARTGLLGFLRPTKctdlnve 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 945 ----LFITGRIKDLIIVAGRNIYSADVEKTVEsSSELLRPGCCavigvpeeVLSAKGIslpdasdevgLVVIAELRD-SK 1019
Cdd:cd05905 451 ehdlLFVVGSIDETLEVRGLRHHPSDIEATVM-RVHPYRGRCA--------VFSITGL----------VVVVAEQPPgSE 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 1020 LVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKRFECLKQFVDGNLNTVP 1078
Cdd:cd05905 512 EEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIY 570
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
527-1073 |
4.75e-50 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 187.28 E-value: 4.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 527 YAELDSNASCVAHKLLTSRKPTIkpgdrVLLVHVPGLDFIDAFFGCLRA----KVIPIPVLPPDPLQRGGQALTKIENIA 602
Cdd:PRK05851 34 WPEVHGRAENVAARLLDRDRPGA-----VGLVGEPTVELVAAIQGAWLAgaavSILPGPVRGADDGRWADATLTRFAGIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 klcnAVAILSTVGYHAAVRA---GLVKNLISFTGKSVKSTGQWPnlpwlhtdswiksskvLPASNIAFqsesqpddlcfL 679
Cdd:PRK05851 109 ----VRTVLSHGSHLERLRAvdsSVTVHDLATAAHTNRSASLTP----------------PDSGGPAV-----------L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 680 QFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLVSWLPQYHDMGLIGgLFTAmACGGSAILFSPLT-FIRNPL 757
Cdd:PRK05851 158 QGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLYHDMGLAF-LLTA-ALAGAPLWLAPTTaFSASPF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 758 MWLQTISDYKATHSAGPNFAFELV---IRRLeadkakaRNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAP 834
Cdd:PRK05851 236 RWLSWLSDSRATLTAAPNFAYNLIgkyARRV-------SDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAAP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 GYGLAENcvfvSCAYGKKKP---------ILVDWQGRICCGYVDPNDADVDIRIVDADTGLEVDEDGKeGEIWISSPSAG 905
Cdd:PRK05851 309 SYGLAES----TCAVTVPVPgiglrvdevTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGVAGREI-GEIEIRGASMM 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 906 IGYWGKEELSqktfrnklqnyPGrKYTRTGDLGWVIQGNLFITGRIKDLIIVAGRNIYSADVEKtVESSSELLRPGCCAV 985
Cdd:PRK05851 384 SGYLGQAPID-----------PD-DWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIER-VAAQVRGVREGAVVA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 986 IGVPEevlsakgislpdASDEVGLVVIAELR--DSKLVNKDIIKqiesRVAEEHGVTVASVKLIRPRTISKTTSGKIKRF 1063
Cdd:PRK05851 451 VGTGE------------GSARPGLVIAAEFRgpDEAGARSEVVQ----RVASECGVVPSDVVFVAPGSLPRTSSGKLRRL 514
|
570
....*....|
gi 1917948728 1064 ECLKQFVDGN 1073
Cdd:PRK05851 515 AVKRSLEAAD 524
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
526-1062 |
2.65e-49 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 183.53 E-value: 2.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppDPLQRGgqalTKIENIAKLC 605
Cdd:cd05936 26 TYRELDALAEAFAAGLQNL---GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL---NPLYTP----RELEHILNDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTVGYHAAVRAGlvknlisftgksvKSTGQWPNLPwlhtdswiksskvlpasniafqsesqPDDLCFLQFTSGS 685
Cdd:cd05936 96 GAKALIVAVSFTDLLAAG-------------APLGERVALT--------------------------PEDVAVLQYTSGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRY--RSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirnplmwL 760
Cdd:cd05936 137 TGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLiprFRPIGV-------L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 761 QTISDYKATHSAGPNFAFELVIRRLEADKakarnYDLSSMIFFMIAAEPVRQKTLKRFVELTRpfglsqevmAP---GYG 837
Cdd:cd05936 210 KEIRKHRVTIFPGVPTMYIALLNAPEFKK-----RDFSSLRLCISGGAPLPVEVAERFEELTG---------VPiveGYG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 838 LAENCVFVSC--AYGKKKPilvdwqgriccGYVDPNDADVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELS 915
Cdd:cd05936 276 LTETSPVVAVnpLDGPRKP-----------GSIGIPLPGTEVKIVDDD-GEEL-PPGEVGELWVRGPQVMKGYWNRPEET 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 916 QKTFRNklqnypGrkYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVessseLLRPGC--CAVIGVPEev 992
Cdd:cd05936 343 AEAFVD------G--WLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVL-----YEHPAVaeAAVVGVPD-- 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728 993 lsakgislPDASDEV-GLVVIAElrDSKLVNKDIIKQiesrvAEEHgvtVASVKliRPRTIS------KTTSGKIKR 1062
Cdd:cd05936 408 --------PYSGEAVkAFVVLKE--GASLTEEEIIAF-----CREQ---LAGYK--VPRQVEfrdelpKSAVGKILR 464
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
526-1060 |
5.17e-43 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 165.46 E-value: 5.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVI--PI-PVLPPDPLQRggqaLTKIENiA 602
Cdd:cd05911 12 TYAQLRTLSRRLAAGL---RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIfsAAnPIYTADELAH----QLKISK-P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 K-LCNAVAILSTVgYHAAVRAGLVKNLISFTGK--SVKSTGQWPNLPWLHTDSWIKSSKVLPasniafqsesqPDDLCFL 679
Cdd:cd05911 84 KvIFTDPDGLEKV-KEAAKELGPKDKIIVLDDKpdGVLSIEDLLSPTLGEEDEDLPPPLKDG-----------KDDTAAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 680 QFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRST--SNTVLVSWLPQYHDMGLIgGLFTAMACGGSAIL---FSPLTFir 754
Cdd:cd05911 152 LYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLF-TTLASLLNGATVIImpkFDSELF-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 755 nplmwLQTISDYKATHSAGPNFAFELVIRRLEADKakarnYDLSSMIFFMIAAEPVrqktLKRFVELTRPFGLSQEVMaP 834
Cdd:cd05911 229 -----LDLIEKYKITFLYLVPPIAAALAKSPLLDK-----YDLSSLRVILSGGAPL----SKELQELLAKRFPNATIK-Q 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 GYGLAENCVFVSCAygkkkPILVDWQGriCCGYVDPNdadVDIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYWGKEEL 914
Cdd:cd05911 294 GYGMTETGGILTVN-----PDGDDKPG--SVGRLLPN---VEAKIVDDDGK-DSLGPNEPGEICVRGPQVMKGYYNNPEA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 915 SQKTFRNKlqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvesssELLR--PGC--CAVIGVP 989
Cdd:cd05911 363 TKETFDED-------GWLHTGDIGYFdEDGYLYIVDRKKELIKYKGFQVAPAELE-------AVLLehPGVadAAVIGIP 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728 990 EEVlsakgislpdaSDEV--GLVVIAElrDSKLVNKDIIKQIESRVAEEH----GVTVASvklirprTISKTTSGKI 1060
Cdd:cd05911 429 DEV-----------SGELprAYVVRKP--GEKLTEKEVKDYVAKKVASYKqlrgGVVFVD-------EIPKSASGKI 485
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
525-1060 |
4.41e-42 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 161.62 E-value: 4.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 525 RTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppdplqrgGQALTKIEN--IA 602
Cdd:cd17631 21 LTYAELDERVNRLAHAL---RALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL---------NFRLTPPEVayIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 KLCNAVAILstvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpDDLCFLQFT 682
Cdd:cd17631 89 ADSGAKVLF--------------------------------------------------------------DDLALLMYT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 683 SGSTSDAKGVMITHGGLIHNV--KLMRRRYRSTSNTVLVswLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirnpl 757
Cdd:cd17631 107 SGTTGRPKGAMLTHRNLLWNAvnALAALDLGPDDVLLVV--APLFHIGGLGVFTLPTLLRGGTVVIlrkFDPETV----- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 758 mwLQTISDYKATHSAGPNFAFELVIRRLEADKakarnYDLSSMIFFMIAAEPVRQKTLKRFVEltrpFGLsqeVMAPGYG 837
Cdd:cd17631 180 --LDLIERHRVTSFFLVPTMIQALLQHPRFAT-----TDLSSLRAVIYGGAPMPERLLRALQA----RGV---KFVQGYG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 838 LAEnCVFVSCAYGKKkpilvDWQGRI-CCGYVDPNdadVDIRIVDADtGLEVDeDGKEGEIWISSPSAGIGYWGKEELSQ 916
Cdd:cd17631 246 MTE-TSPGVTFLSPE-----DHRRKLgSAGRPVFF---VEVRIVDPD-GREVP-PGEVGEIVVRGPHVMAGYWNRPEATA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 917 KTFRNklqnypGrkYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEvlsa 995
Cdd:cd17631 315 AAFRD------G--WFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAE---VAVIGVPDE---- 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 996 KGIslpdasdEVGLVVIAELRDSKLVNKDIIKQIESRvaeehgvtVASVKliRPRTI------SKTTSGKI 1060
Cdd:cd17631 380 KWG-------EAVVAVVVPRPGAELDEDELIAHCRER--------LARYK--IPKSVefvdalPRNATGKI 433
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
510-1072 |
6.70e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 161.05 E-value: 6.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 510 ALYtWINEGGAVGcQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLvHVP-GLDFIDAFFGCLRAKVIPIPV---LPP 585
Cdd:COG0365 27 ALI-WEGEDGEER-TLTYAELRREVNRFANAL---RALGVKKGDRVAI-YLPnIPEAVIAMLACARIGAVHSPVfpgFGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 586 DPLqrggqaLTKIENiaklCNAVAILSTVGYH------------AAVRAGL--VKNLISF--TGKSVkstgQWPNLPWLH 649
Cdd:COG0365 101 EAL------ADRIED----AEAKVLITADGGLrggkvidlkekvDEALEELpsLEHVIVVgrTGADV----PMEGDLDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 650 TdswiksskVLPASNIAFQSES-QPDDLCFLQFTSGSTSDAKGVMITHGG-LIHNVKLMRR--------RYRSTSNtvlV 719
Cdd:COG0365 167 E--------LLAAASAEFEPEPtDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYvldlkpgdVFWCTAD---I 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 720 SWLpqyhdMGLIGGLFTAMACGGSAILF--SPLTfiRNPLMWLQTISDYKATH-SAGPNFafelvIRRLE-ADKAKARNY 795
Cdd:COG0365 236 GWA-----TGHSYIVYGPLLNGATVVLYegRPDF--PDPGRLWELIEKYGVTVfFTAPTA-----IRALMkAGDEPLKKY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 796 DLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLsqeVMAPGYGLAE-NCVFVSCAYGKK-KPilvdwqGRICC---GYvdp 870
Cdd:COG0365 304 DLSSLRLLGSAGEPLNPEVWEWWYEA---VGV---PIVDGWGQTEtGGIFISNLPGLPvKP------GSMGKpvpGY--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 871 ndadvDIRIVDaDTGLEVdEDGKEGEIWISSPSAG--IGYWGKEELSQKTFRNKlqnYPGrkYTRTGDLGWVIQ-GNLFI 947
Cdd:COG0365 369 -----DVAVVD-EDGNPV-PPGEEGELVIKGPWPGmfRGYWNDPERYRETYFGR---FPG--WYRTGDGARRDEdGYFWI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 948 TGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsaKGISLpdasdeVGLVViaeLRDSKLVNKDIIK 1027
Cdd:COG0365 437 LGRSDDVINVSGHRIGTAEIESALVSHPAVAE---AAVVGVPDEI---RGQVV------KAFVV---LKPGVEPSDELAK 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 1028 QIESRVAEEhgvtVASVKliRPRTIS------KTTSGKIKRFEcLKQFVDG 1072
Cdd:COG0365 502 ELQAHVREE----LGPYA--YPREIEfvdelpKTRSGKIMRRL-LRKIAEG 545
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
526-1062 |
7.54e-41 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 159.40 E-value: 7.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPpdplqrggqALTKIE---NIA 602
Cdd:cd05926 16 TYADLAELVDDLARQL---AALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNP---------AYKKAEfefYLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 KLCNAVAILSTVGYHAAVRA-----GLVKNL--ISFTGKSVKSTGQWPNLPWLHTdswiksskvlpasNIAFQSESQPDD 675
Cdd:cd05926 84 DLGSKLVLTPKGELGPASRAasklgLAILELalDVGVLIRAPSAESLSNLLADKK-------------NAKSEGVPLPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 676 LCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS--NTVLVswLPQYHDMGLIGGLFTAMACGGSAIL---FSPL 750
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPddRTLVV--MPLFHVHGLVASLLSTLAAGGSVVLpprFSAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 TFirnplmWlQTISDYKAT-HSAGPNFaFELVIRRLEADKAKArnydLSSMIFFMIAAEPVRQKTLKRfveltrpfgLSQ 829
Cdd:cd05926 229 TF------W-PDVRDYNATwYTAVPTI-HQILLNRPEPNPESP----PPKLRFIRSCSASLPPAVLEA---------LEA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 830 EVMAP---GYGLAENCVFVSC---AYGKKKPILVdwqGRiccgyvdPNdaDVDIRIVDADTglEVDEDGKEGEIWISSPS 903
Cdd:cd05926 288 TFGAPvleAYGMTEAAHQMTSnplPPGPRKPGSV---GK-------PV--GVEVRILDEDG--EILPPGVVGEICLRGPN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 904 AGIGYWGKEELSQK-TFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR-P 980
Cdd:cd05926 354 VTRGYLNNPEANAEaAFKD--------GWFRTGDLGYLDAdGYLFLTGRIKELINRGGEKISPLEVDGV------LLShP 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 981 GC--CAVIGVPEEVLsakgislpdaSDEVGLVVIAELrDSKLVNKDIIKQIESRVAEehgVTVASvKLIRPRTISKTTSG 1058
Cdd:cd05926 420 AVleAVAFGVPDEKY----------GEEVAAAVVLRE-GASVTEEELRAFCRKHLAA---FKVPK-KVYFVDELPKTATG 484
|
....
gi 1917948728 1059 KIKR 1062
Cdd:cd05926 485 KIQR 488
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
524-1072 |
1.57e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 159.20 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDplqrggqaltKIEN 600
Cdd:PRK06187 31 RTTYAELDERVNRLANALRAL---GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPInirLKPE----------EIAY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 601 IAKLCNAVAIL---STVGYHAAVRAGL--VKNLISFTGKSVKSTGQwpnlPWLHTDSWIKSskvlpASNIAFQSESQPDD 675
Cdd:PRK06187 98 ILNDAEDRVVLvdsEFVPLLAAILPQLptVRTVIVEGDGPAAPLAP----EVGEYEELLAA-----ASDTFDFPDIDEND 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 676 LCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLigGL-FTAMACGGSAILfsPLTFIR 754
Cdd:PRK06187 169 AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW--GLpYLALMAGAKQVI--PRRFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 755 NPLmwLQTISDYKATHSAGPNFAFELVIRRLEAdkakaRNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLSqevMAP 834
Cdd:PRK06187 245 ENL--LDLIETERVTFFFAVPTIWQMLLKAPRA-----YFVDFSSLRLVIYGGAALPPALLREFKEK---FGID---LVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 GYGLAENCVFVSCAY-------GKKKPILvdwQGRICCGyvdpndadVDIRIVDADtGLEVDEDGKE-GEIWISSPSAGI 906
Cdd:PRK06187 312 GYGMTETSPVVSVLPpedqlpgQWTKRRS---AGRPLPG--------VEARIVDDD-GDELPPDGGEvGEIIVRGPWLMQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 907 GYWGKEELSQKTFRNklqnypGrkYTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC- 982
Cdd:PRK06187 380 GYWNRPEATAETIDG------G--WLHTGDVG-YIdeDGYLYITDRIKDVIISGGENIYPRELE------DALYGhPAVa 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 983 -CAVIGVPEEvlsakgislpdASDEVGLVVIaELRDSKLVN-KDIIKQIESRVAeehgvtvasvKLIRPRTIS------K 1054
Cdd:PRK06187 445 eVAVIGVPDE-----------KWGERPVAVV-VLKPGATLDaKELRAFLRGRLA----------KFKLPKRIAfvdelpR 502
|
570
....*....|....*...
gi 1917948728 1055 TTSGKIKRFECLKQFVDG 1072
Cdd:PRK06187 503 TSVGKILKRVLREQYAEG 520
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
487-1062 |
7.05e-37 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 147.77 E-value: 7.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 487 FPNLPTLDCYLkHWAAQEITQNKALytwINegGAVGCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFI 566
Cdd:cd05904 1 LPTDLPLDSVS-FLFASAHPSRPAL---ID--AATGRALTYAELERRVRRLAAGL---AKRGGRKGDVVLLLSPNSIEFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 567 DAFFGCLRAKVIPIPVLP---PDPLQRggQAltkieniaKLCNAVAILSTvgyhaavrAGLVKNLISFtGKSVKSTGQWP 643
Cdd:cd05904 72 VAFLAVLSLGAVVTTANPlstPAEIAK--QV--------KDSGAKLAFTT--------AELAEKLASL-ALPVVLLDSAE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 644 NLPWLHTDSWIKSSKVLPasniaFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS---NTVLVS 720
Cdd:cd05904 133 FDSLSFSDLLFEADEAEP-----PVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSdseDVFLCV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 721 wLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFIRNplmwlqtISDYKATH-SAGPNFAFELVirrleaDKAKARNYD 796
Cdd:cd05904 208 -LPMFHIYGLSSFALGLLRLGATVVVmprFDLEELLAA-------IERYKVTHlPVVPPIVLALV------KSPIVDKYD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 797 LSSMIFFMIAAEPVRQKTLKRFVEltrPFGLSQEVMapGYGLAE-NCVFVSCAYGKKKPILVDwqgriCCGYVDPNdadV 875
Cdd:cd05904 274 LSSLRQIMSGAAPLGKELIEAFRA---KFPNVDLGQ--GYGMTEsTGVVAMCFAPEKDRAKYG-----SVGRLVPN---V 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 876 DIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDL 954
Cdd:cd05904 341 EAKIVDPETG-ESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE-------GWLHTGDLCYIDEdGYLFIVDRLKEL 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 955 IIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEvlsaKGISLPdasdeVGLVVIAelRDSKLVNKDIIKQIESRva 1034
Cdd:cd05904 413 IKYKGFQVAPAELEALLLSHPEILD---AAVIPYPDE----EAGEVP-----MAFVVRK--PGSSLTEDEIMDFVAKQ-- 476
|
570 580 590
....*....|....*....|....*....|..
gi 1917948728 1035 eehgvtVASVKLIRPRT----ISKTTSGKIKR 1062
Cdd:cd05904 477 ------VAPYKKVRKVAfvdaIPKSPSGKILR 502
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
526-1062 |
1.55e-36 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 144.93 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltSRKpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPpdplqrggqaltkieniaklc 605
Cdd:cd05935 3 TYLELLEVVKKLASFL--SNK-GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 navailstvgyhaavraglvkNLISFtgksvkstgqwpNLPWLHTDSWIKSSKVLpasniafqseSQPDDLCFLQFTSGS 685
Cdd:cd05935 59 ---------------------MLKER------------ELEYILNDSGAKVAVVG----------SELDDLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSplTFIRNPLmwLQTISD 765
Cdd:cd05935 96 TGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA--RWDRETA--LELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 766 YKATHS-AGPNFAFELVirrleaDKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSqevmapGYGLAEncvf 844
Cdd:cd05935 172 YKVTFWtNIPTMLVDLL------ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVE------GYGLTE---- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 845 vSCAYGKKKPILVdwQGRICCGYVdpnDADVDIRIVDADTGLEVDeDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklQ 924
Cdd:cd05935 236 -TMSQTHTNPPLR--PKLQCLGIP---*FGVDARVIDIETGRELP-PNEVGEIVVRGPQIFKGYWNRPEETEESF----I 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 925 NYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEvlsakgislpDA 1003
Cdd:cd05935 305 EIKGRRFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E---VCVISVPDE----------RV 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 1004 SDEV-GLVVIAELRDSKLVNKDIIKQIESRvaeehgvtVASVKliRPRTIS------KTTSGKIKR 1062
Cdd:cd05935 372 GEEVkAFIVLRPEYRGKVTEEDIIEWAREQ--------MAAYK--YPREVEfvdelpRSASGKILW 427
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
526-968 |
1.19e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 141.64 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltSRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAK--VIPI-PVLPPDPLqrggqaltkiENIA 602
Cdd:PRK08314 37 SYRELLEEAERLAGYL--QQECGVRKGDRVLLYMQNSPQFVIAYYAILRANavVVPVnPMNREEEL----------AHYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 KLCNAVAILSTVGYHAAVRAGL----VKNLI--SFTGkSVKSTGQWPNLPWLHT---------DSWIKSSKVLPASNIAF 667
Cdd:PRK08314 105 TDSGARVAIVGSELAPKVAPAVgnlrLRHVIvaQYSD-YLPAEPEIAVPAWLRAepplqalapGGVVAWKEALAAGLAPP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 668 QSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILF 747
Cdd:PRK08314 184 PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 SpltfirnplMW-----LQTISDYKATH-----------SAGPNFAfelvirrleadkakarNYDLSSMIFfmI----AA 807
Cdd:PRK08314 264 P---------RWdreaaARLIERYRVTHwtniptmvvdfLASPGLA----------------ERDLSSLRY--IggggAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 808 EP--VRQKTLKRFveltrpfGLS-QEvmapGYGLAENCVFVscaygkkkpilvdwqgriccgYVDPNDA----------- 873
Cdd:PRK08314 317 MPeaVAERLKELT-------GLDyVE----GYGLTETMAQT---------------------HSNPPDRpklqclgiptf 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 874 DVDIRIVDADTGLEVDeDGKEGEIWISSPSAGIGYWGKEELSQKTFrnklQNYPGRKYTRTGDLGWV-IQGNLFITGRIK 952
Cdd:PRK08314 365 GVDARVIDPETLEELP-PGEVGEIVVHGPQVFKGYWNRPEATAEAF----IEIDGKRFFRTGDLGRMdEEGYFFITDRLK 439
|
490
....*....|....*.
gi 1917948728 953 DLIIVAGRNIYSADVE 968
Cdd:PRK08314 440 RMINASGFKVWPAEVE 455
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
673-1064 |
4.00e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 132.79 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLftaMAC--GGSAILFSPL 750
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGV---LACltHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 TFirNPLMWLQTISDYKATHSAGPNFAFelvIRRLEADKAKarNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLSQE 830
Cdd:cd05917 78 SF--DPLAVLEAIEKEKCTALHGVPTMF---IAELEHPDFD--KFDLSSLRTGIMAGAPCPPELMKRVIEV---MNMKDV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 831 VMApgYGLAENCVfVSCAYGKKKPILVdwqgRI-CCGYVDPndaDVDIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYW 909
Cdd:cd05917 148 TIA--YGMTETSP-VSTQTRTDDSIEK----RVnTVGRIMP---HTEAKIVDPEGG-IVPPVGVPGELCIRGYSVMKGYW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 910 GKEELSQKTFRNKlqnypgrKYTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIG 987
Cdd:cd05917 217 NDPEKTAEAIDGD-------GWLHTGDLA-VMdeDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSD---VQVVG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 988 VPEEVLsakgislpdaSDEVGLVVIaeLRD-SKLVNKDIIKQIESRVAeEHGVtvasvklirPRTI------SKTTSGKI 1060
Cdd:cd05917 286 VPDERY----------GEEVCAWIR--LKEgAELTEEDIKAYCKGKIA-HYKV---------PRYVffvdefPLTVSGKI 343
|
....
gi 1917948728 1061 KRFE 1064
Cdd:cd05917 344 QKFK 347
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
526-951 |
1.27e-32 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 132.77 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSRKptIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKL 604
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKAGAAYVPLDPAYPAER-------LAFILED 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 605 CNAVAILSTVGyHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLhtdswiksskvlpasniafQSESQPDDLCFLQFTSG 684
Cdd:TIGR01733 71 AGARLLLTDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPP-------------------DAPSGPDDLAYVIYTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 685 STSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgGLFTAMACGGSAILFSPLTFIRNPLMWLQTIS 764
Cdd:TIGR01733 131 STGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 765 DYKATHSAGPNFAFELVirrleadkAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAENCVF 844
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALL--------AAALPPALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLYGPTETTVW 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 845 VSCAYgkKKPILVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRN--K 922
Cdd:TIGR01733 277 STATL--VDPDDAPRESPVPIGRPLAN---TRLYVLDDD--LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPdpF 349
|
410 420 430
....*....|....*....|....*....|
gi 1917948728 923 LQNYPGRKYtRTGDLG-WVIQGNLFITGRI 951
Cdd:TIGR01733 350 AGGDGARLY-RTGDLVrYLPDGNLEFLGRI 378
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
525-1063 |
2.36e-32 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 134.03 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 525 RTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPLQrggQALTkiENI 601
Cdd:cd05959 30 LTYAELEAEARRVAGAL---RALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVntlLTPDDYA---YYLE--DSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 602 AK-LCNAVAILSTVGYHAAVRAGLVKNLISFTGKsvkstGQWPNLPWLhTDSWIKSSKVLPASNiafqseSQPDDLCFLQ 680
Cdd:cd05959 102 ARvVVVSGELAPVLAAALTKSEHTLVVLIVSGGA-----GPEAGALLL-AELVAAEAEQLKPAA------THADDPAFWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 681 FTSGSTSDAKGVMITHGGLIHNVKLMRRR-YRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFS--PltfirNPL 757
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPerP-----TPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 758 MWLQTISDYKATHSAG-PNFAFELvirrLEADKAKARnyDLSSMIFFMIAAEPVRQKTLKRFvelTRPFGLSqevMAPGY 836
Cdd:cd05959 245 AVFKRIRRYRPTVFFGvPTLYAAM----LAAPNLPSR--DLSSLRLCVSAGEALPAEVGERW---KARFGLD---ILDGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 837 GLAENC-VFVSCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELS 915
Cdd:cd05959 313 GSTEMLhIFLSNRPGRVRY---GTTGKPVPGY--------EVELRD-EDGGDV-ADGEPGELYVRGPSSATMYWNNRDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 916 QKTFRNKLqNYPGRKYTRTGDlgwviqGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsa 995
Cdd:cd05959 380 RDTFQGEW-TRTGDKYVRDDD------GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLE---AAVVGVEDED--- 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728 996 kGISLPDAsdevgLVVIA-ELRDSKLVNKDIIKQIESRvaeehgvtVASVKliRPRTI------SKTTSGKIKRF 1063
Cdd:cd05959 447 -GLTKPKA-----FVVLRpGYEDSEALEEELKEFVKDR--------LAPYK--YPRWIvfvdelPKTATGKIQRF 505
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
522-1009 |
3.57e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 134.74 E-value: 3.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLV--HVPglDFIDAFFGCLRAKVIPI---PVLPPDPLQ------- 589
Cdd:PRK05605 55 GATTTYAELGKQVRRAAAGL---RALGVRPGDRVAIVlpNCP--QHIVAFYAVLRLGAVVVehnPLYTAHELEhpfedhg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 590 --------RGGQALTKIENIAKLCNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPN-LPWlhtdSWIKSSKVL 660
Cdd:PRK05605 130 arvaivwdKVAPTVERLRRTTPLETIVSVNMIAAMPLLQRLALRLPIPALRKARAALTGPAPGtVPW----ETLVDAAIG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 661 PASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVkLMRRRY----RSTSNTVLVSwLPQYHDMGLIGGLFT 736
Cdd:PRK05605 206 GDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAWvpglGDGPERVLAA-LPMFHAYGLTLCLTL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 737 AMACGGSAILF-SPltfiRNPLMwLQTISDYKATHSAG-PNfafelVIRRLeADKAKARNYDLSSMIFFMIAAEPVRQKT 814
Cdd:PRK05605 284 AVSIGGELVLLpAP----DIDLI-LDAMKKHPPTWLPGvPP-----LYEKI-AEAAEERGVDLSGVRNAFSGAMALPVST 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 815 LKRFVELTRpfGLSQEvmapGYGLAENCVFVSCaygkkKPILVDWQGriccGYVDPNDADVDIRIVDADTGLEVDEDGKE 894
Cdd:PRK05605 353 VELWEKLTG--GLLVE----GYGLTETSPIIVG-----NPMSDDRRP----GYVGVPFPDTEVRIVDPEDPDETMPDGEE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 895 GEIWISSPSAGIGYWGKEELSQKTFrnklqnYPGrkYTRTGDLGwVIQGNLFIT--GRIKDLIIVAGRNIYSADVEktve 972
Cdd:PRK05605 418 GELLVRGPQVFKGYWNRPEETAKSF------LDG--WFRTGDVV-VMEEDGFIRivDRIKELIITGGFNVYPAEVE---- 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1917948728 973 sssELLR--PGC--CAVIGVP-----EEVLSAkgISLPDAS--DEVGL 1009
Cdd:PRK05605 485 ---EVLRehPGVedAAVVGLPredgsEEVVAA--VVLEPGAalDPEGL 527
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
525-1064 |
4.51e-32 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 132.12 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 525 RTYAELDSNASCVAHKLLTSRkptIKPGDRVLlVHVPG-LDFIDAFFGCLRAKVIPIPVLPpdplqrggqALTKIEniak 603
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALG---VGPGDVVA-FQLPNwWEFAVLYLACLRIGAVTNPILP---------FFREHE---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 604 lcnAVAILStvgyHAAVRAGLVknlisftgksvkstgqwpnlpwlhTDSWIKsskvlpasniaFQSESQPDDLCFLQFTS 683
Cdd:cd05903 65 ---LAFILR----RAKAKVFVV------------------------PERFRQ-----------FDPAAMPDAVALLLFTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSpltfIRNPLMWLQTI 763
Cdd:cd05903 103 GTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD----IWDPDKALALM 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 764 SDYKATHSAG-PNFAFELVIRRLEADKakarnyDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLsqeVMAPGYGLAENC 842
Cdd:cd05903 179 REHGVTFMMGaTPFLTDLLNAVEEAGE------PLSRLRTFVCGGATVPRSLARRAAEL---LGA---KVCSAYGSTECP 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 843 vfvsCAYGKKKPILVDwqgRICC--GYVDPNdadVDIRIVDaDTGLEVDEdGKEGEIWISSPSAGIGYWGKEELsqkTFR 920
Cdd:cd05903 247 ----GAVTSITPAPED---RRLYtdGRPLPG---VEIKVVD-DTGATLAP-GVEGELLSRGPSVFLGYLDRPDL---TAD 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 921 nklqNYPGRKYtRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC--CAVIGVPEE----- 991
Cdd:cd05903 312 ----AAPEGWF-RTGDLArLDEDGYLRITGRSKDIIIRGGENIPVLEVE------DLLLGhPGVieAAVVALPDErlger 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 992 ---VLSAKGISLPDASDevglvvIAELRDSKLVNKDIIKqiesrvaeEHGVTVASVklirPRtiskTTSGKIKRFE 1064
Cdd:cd05903 381 acaVVVTKSGALLTFDE------LVAYLDRQGVAKQYWP--------ERLVHVDDL----PR----TPSGKVQKFR 434
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
526-1062 |
1.19e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 132.34 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP-------PDPLQRGGqaltki 598
Cdd:PRK07656 32 TYAELNARVRRAAAALAAL---GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTrytadeaAYILARGD------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 599 eniAKLCNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQwPNLPWlhtDSWIKsskvlPASNIAFQSESQPDDLCF 678
Cdd:PRK07656 103 ---AKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTE-KMKTF---TDFLA-----AGDPAERAPEVDPDDVAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 679 LQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirn 755
Cdd:PRK07656 171 ILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPlpvFDPDEV--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 756 plmwLQTISDYKATHSAGP----NFAFelvirrleaDKAKARNYDLSSMIFFMI--AAEPVRqkTLKRFVELtrpFGLsq 829
Cdd:PRK07656 248 ----FRLIETERITVLPGPptmyNSLL---------QHPDRSAEDLSSLRLAVTgaASMPVA--LLERFESE---LGV-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 830 EVMAPGYGLAENCVFVS-CAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGY 908
Cdd:PRK07656 308 DIVLTGYGLSEASGVTTfNRLDDDRKTVAGTIGTAI--------AGVENKIVNEL-GEEV-PVGEVGELLVRGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 909 WGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR-PGC--CA 984
Cdd:PRK07656 378 YDDPEATAAAIDAD-------GWLHTGDLGRLDEeGYLYIVDRKKDMFIVGGFNVYPAEVEEV------LYEhPAVaeAA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 985 VIGVPEEVLSakgislpdasdEVGLVVIAELRDSKLVNKDIIKQIESRVAeehgvtvasvKLIRPRTIS------KTTSG 1058
Cdd:PRK07656 445 VIGVPDERLG-----------EVGKAYVVLKPGAELTEEELIAYCREHLA----------KYKVPRSIEfldelpKNATG 503
|
....
gi 1917948728 1059 KIKR 1062
Cdd:PRK07656 504 KVLK 507
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
673-1064 |
1.81e-30 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 127.33 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACG-------GSAI 745
Cdd:cd05907 86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGariyfasSAET 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 746 L------FSPLTFIRNPLMWlQTISDyKATHSAGPNFafelviRRLEADKAKarnydLSSMIFFMIAAEPVRQKTLKRFv 819
Cdd:cd05907 166 LlddlseVRPTVFLAVPRVW-EKVYA-AIKVKAVPGL------KRKLFDLAV-----GGRLRFAASGGAPLPAELLHFF- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 820 eltRPFGLsqeVMAPGYGLAENCVFVSCAygkkkpilVDWQGRI-CCGYVDPndaDVDIRIVDadtglevdedgkEGEIW 898
Cdd:cd05907 232 ---RALGI---PVYEGYGLTETSAVVTLN--------PPGDNRIgTVGKPLP---GVEVRIAD------------DGEIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 899 ISSPSAGIGYWGKEElsqKTFRNKLQNypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS-- 974
Cdd:cd05907 283 VRGPNVMLGYYKNPE---ATAEALDAD----GWLHTGDLGEIdEDGFLHITGRKKDLIITSgGKNISPEPIENALKASpl 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 975 -SELL-----RPGCCAVIGVPEEVLSA----KGISLPDASDevglvviaelrdsKLVNKDIIKQIESRVAEE-HGVT-VA 1042
Cdd:cd05907 356 iSQAVvigdgRPFLVALIVPDPEALEAwaeeHGIAYTDVAE-------------LAANPAVRAEIEAAVEAAnARLSrYE 422
|
410 420
....*....|....*....|....*....
gi 1917948728 1043 SVK----LIRPRTIS---KTTSGKIKRFE 1064
Cdd:cd05907 423 QIKkfllLPEPFTIEngeLTPTLKLKRPV 451
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
526-993 |
1.27e-29 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 126.41 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLtsrKPTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPdplQRGgqalTKIENIAKL 604
Cdd:COG1021 52 SYAELDRRADRLAAGLL---ALGLRPGDRVV-VQLPnVAEFVIVFFALFRAGAIPVFALPA---HRR----AEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 605 CNAVAILST--------VGYHAAVRAGL--VKNLISftgksVKSTGQWPNLpwlhtDSWIKSskvlPASniAFQSESQPD 674
Cdd:COG1021 121 SEAVAYIIPdrhrgfdyRALARELQAEVpsLRHVLV-----VGDAGEFTSL-----DALLAA----PAD--LSEPRPDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 675 DLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIG-GLFTAMACGGSAIL---FSPL 750
Cdd:COG1021 185 DVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTVVLapdPSPD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 TFIrnPLmwlqtISDYKATHSA-GPnfafELVIRRLEAdkAKARNYDLSSMIFFMI-----AAEPVRQktlkrfvelTRP 824
Cdd:COG1021 265 TAF--PL-----IERERVTVTAlVP----PLALLWLDA--AERSRYDLSSLRVLQVggaklSPELARR---------VRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 825 -FGLS-QEVmapgYGLAE---NCVfvscaygkkKP-----ILVDWQGR-ICcgyvdPNDadvDIRIVDaDTGLEVdEDGK 893
Cdd:COG1021 323 aLGCTlQQV----FGMAEglvNYT---------RLddpeeVILTTQGRpIS-----PDD---EVRIVD-EDGNPV-PPGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 894 EGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypGrkYTRTGDLgwVIQ---GNLFITGRIKDLIIVAGRNIYSADVEkt 970
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFTPD-----G--FYRTGDL--VRRtpdGYLVVEGRAKDQINRGGEKIAAEEVE-- 448
|
490 500
....*....|....*....|....*.
gi 1917948728 971 vessSELLR-PGC--CAVIGVPEEVL 993
Cdd:COG1021 449 ----NLLLAhPAVhdAAVVAMPDEYL 470
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
522-951 |
3.61e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 123.41 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRV-LLVHvPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIEN 600
Cdd:cd05930 10 DQSLTYAELDARANRLARYL---RERGVGPGDLVaVLLE-RSLEMVVAILAVLKAGAAYVPLDPSYPAER-------LAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 601 IAKLCNAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQ 680
Cdd:cd05930 79 ILEDSGAKLVLT-----------------------------------------------------------DPDDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 681 FTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTfIRNPLMWL 760
Cdd:cd05930 100 YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVLPEEV-RKDPEALA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 761 QTISDYKATHSAGPNFAFELVIRRLEADkakarnyDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAE 840
Cdd:cd05930 178 DLLAEEGITVLHLTPSLLRLLLQELELA-------ALPSLRLVLVGGEALPPDLVRRWREL-----LPGARLVNLYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 841 NCVFVSCAYGKKKPILVDwqgRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFR 920
Cdd:cd05930 246 ATVDATYYRVPPDDEEDG---RVPIGRPIPN---TRVYVLDEN--LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFV 317
|
410 420 430
....*....|....*....|....*....|..
gi 1917948728 921 NkLQNYPGRKYTRTGDLG-WVIQGNLFITGRI 951
Cdd:cd05930 318 P-NPFGPGERMYRTGDLVrWLPDGNLEFLGRI 348
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
526-1064 |
6.16e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 122.40 E-value: 6.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPpdplQRGGQALTkieniaklc 605
Cdd:cd05934 5 TYAELLRESARIAAALAAL---GIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT----ALRGDELA--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 navAILSTVGYHAAVRaglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpdDLCFLQFTSGS 685
Cdd:cd05934 69 ---YIIDHSGAQLVVV-----------------------------------------------------DPASILYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirnplmWLQt 762
Cdd:cd05934 93 TGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLlprFSASRF------WSD- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 763 ISDYKAT--HSAGPNFAFELVIRRLEADKA-KARnydlssmiffMIAAEPVRQKTLKRFVEltRpFGLsqeVMAPGYGLA 839
Cdd:cd05934 166 VRRYGATvtNYLGAMLSYLLAQPPSPDDRAhRLR----------AAYGAPNPPELHEEFEE--R-FGV---RLLEGYGMT 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 840 ENCVFVSCAYGKKKPILvdwqgriCCGYVDPndaDVDIRIVDADtGLEVdEDGKEGEIWI-SSPSAGI--GYWGKEELSQ 916
Cdd:cd05934 230 ETIVGVIGPRDEPRRPG-------SIGRPAP---GYEVRIVDDD-GQEL-PAGEPGELVIrGLRGWGFfkGYYNMPEATA 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 917 KTFRNklqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsa 995
Cdd:cd05934 298 EAMRN--------GWFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVRE---AAVVAVPDEV--- 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 996 kgislpdASDEVGLVVIaeLRD-SKLVNKDIIKQIESRVAeehgvtvasvKLIRPRTIS------KTTSGKIKRFE 1064
Cdd:cd05934 364 -------GEDEVKAVVV--LRPgETLDPEELFAFCEGQLA----------YFKVPRYIRfvddlpKTPTEKVAKAQ 420
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
526-993 |
4.38e-28 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 120.09 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLqrggqaltkieniaklc 605
Cdd:cd05941 13 TYADLVARAARLANRLLALGK--DLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPL----------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 navailstvgyhaavraglvknlisftgksvkstgqwPNLPWLHTDSwiKSSKVLpasniafqsesqpdDLCFLQFTSGS 685
Cdd:cd05941 74 -------------------------------------AELEYVITDS--EPSLVL--------------DPALILYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLT----------- 751
Cdd:cd05941 101 TGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFlpkFDPKEvaisrlmpsit 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 752 -FIRNPLMWLQTISDYKAtHSAGPNFAFELVIRRLEadkakarnydlssmifFMI---AAEPVrqKTLKRFVELTRPFGL 827
Cdd:cd05941 181 vFMGVPTIYTRLLQYYEA-HFTDPQFARAAAAERLR----------------LMVsgsAALPV--PTLEEWEAITGHTLL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 828 SQevmapgYGLAENCVFVSCAY-GKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVDEdGKEGEIWISSPSAGI 906
Cdd:cd05941 242 ER------YGMTEIGMALSNPLdGERRP-----------GTVGMPLPGVQARIVDEETGEPLPR-GEVGEIQVRGPSVFK 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 907 GYWGKEELSQKTFRnklqnypGRKYTRTGDLGWV-IQGNLFITGRIKDLII-VAGRNIYSADVEKTVESssellRPGC-- 982
Cdd:cd05941 304 EYWNKPEATKEEFT-------DDGWFKTGDLGVVdEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLA-----HPGVse 371
|
490
....*....|.
gi 1917948728 983 CAVIGVPEEVL 993
Cdd:cd05941 372 CAVIGVPDPDW 382
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
549-1064 |
4.16e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 119.00 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 549 IKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP---PDPLQR-----GGQALTKIENIAKLCNAVA--------ILS 612
Cdd:PRK08974 71 LKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPlytPRELEHqlndsGAKAIVIVSNFAHTLEKVVfktpvkhvILT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 613 TVGYHAAVRAGlvkNLISFTGKSVKSTGQWPNLPwlHTDSWIKS-SK------VLPasniafqsESQPDDLCFLQFTSGS 685
Cdd:PRK08974 151 RMGDQLSTAKG---TLVNFVVKYIKRLVPKYHLP--DAISFRSAlHKgrrmqyVKP--------ELVPEDLAFLQYTGGT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVK--------LMRRRYRstsntVLVSWLPQYHDMGLIGGLFTAMACGGSAILfspltfIRNPL 757
Cdd:PRK08974 218 TGVAKGAMLTHRNMLANLEqakaaygpLLHPGKE-----LVVTALPLYHIFALTVNCLLFIELGGQNLL------ITNPR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 758 ---MWLQTISDYKATHSAGPNFAFELVIRRLEADKAkarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSqevmap 834
Cdd:PRK08974 287 dipGFVKELKKYPFTAITGVNTLFNALLNNEEFQEL-----DFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLE------ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 GYGLAENCVFVSCAygkkkPI-LVDWQGRIccGYVDPNdadVDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEE 913
Cdd:PRK08974 356 GYGLTECSPLVSVN-----PYdLDYYSGSI--GLPVPS---TEIKLVD-DDGNEV-PPGEPGELWVKGPQVMLGYWQRPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 914 LSQKTFRNklqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEV 992
Cdd:PRK08974 424 ATDEVIKD--------GWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE---VAAVGVPSEV 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 993 lsakgislpdaSDE-VGLVVIAelRDSKLVNKDIIKQiesrvAEEH--GVTVAsvKLIRPRT-ISKTTSGKIKRFE 1064
Cdd:PRK08974 493 -----------SGEaVKIFVVK--KDPSLTEEELITH-----CRRHltGYKVP--KLVEFRDeLPKSNVGKILRRE 548
|
|
| NRPS_term_dom |
TIGR02353 |
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
1269-1702 |
9.70e-27 |
|
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.
Pssm-ID: 274093 [Multi-domain] Cd Length: 695 Bit Score: 119.09 E-value: 9.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1269 GLPWLHQAsvvlLAPLSWILCIALTSISIAFFGNSFLRINYA------LTPEV-SVWSVDFVKWWALYKAQEVSSKVLav 1341
Cdd:TIGR02353 24 GYNWLYEA----LDDVSWLYLRAVALVFAVPVGRLGFAIAAKwllvgrWKPGTyPIWGSTYLRFWTVKRLVDAAPTVL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1342 hLRGTVFLKHWFEMLGARIGSSVLLDTV--DITDpsLVSIGDGAVIAEGALLQSHEVRNSILRLQPIRIGRNCSVGPYAV 1419
Cdd:TIGR02353 98 -LSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGYRAERGRLHTGPVTLGRDAFIGTRST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1420 VQKGSVLREGAEVPALQKSEGGKS-----------ALKMAKAENILK-VSPGTL-KTVQQFMGIYVVGFLsslsaatvyl 1486
Cdd:TIGR02353 175 LDIDTSIGDGAQLGHGSALQGGQSipdgerwhgspAQKTGADYRKVQpARPYTVrRRLYVAGALFVVFVL---------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1487 lymslsqkvpsLELLAFLCISGAlhwvpFTIVAYATMFTKAPPNPFEFAISLAIAYFAHGLVLSLLTSIFTHLLAG---K 1563
Cdd:TIGR02353 245 -----------LPPLAFLFAIPV-----AITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLLAAVRLLLNlvlK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1564 EKKTQTHikTWFGHQL----AIACHVRFAKLLSG-TEAFCMYLRLLGAKVGRYCSIRAINpIADPRMVSIGAGVHLGDFS 1638
Cdd:TIGR02353 309 PGRYYVH--SGFYYQAwtvqQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPDLTDIGEETFIADGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 1639 RIITGFYSQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGS 1702
Cdd:TIGR02353 386 LMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGS 449
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
524-992 |
1.68e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 116.57 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppdplqrgGQALTK--IENI 601
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLDL---GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV---------NFMLTGeeLAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 602 AKLCNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLHTDSWIKSskvlpASNIAFQSESQPDDLCFLQF 681
Cdd:PRK08316 104 LDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEA-----GSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 682 TSGSTSDAKGVMITHGGLIHNvklmrrrYRST-------SNTVLVSWLPQYHDMGLIGGLFTAMACGG-SAILFSPltfi 753
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAE-------YVSCivagdmsADDIPLHALPLYHCAQLDVFLGPYLYVGAtNVILDAP---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 754 rNPLMWLQTISDYKATHSagpnFAFELV----IRRLEADKakarnYDLSSM--IFF--MIAAEPVRQKTLKRF--VELTR 823
Cdd:PRK08316 248 -DPELILRTIEAERITSF----FAPPTVwislLRHPDFDT-----RDLSSLrkGYYgaSIMPVEVLKELRERLpgLRFYN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 824 PFGlsQEVMAPgygLAEncvfV-----------SCAygkkKPILvdwqgriccgyvdpndaDVDIRIVDADtGLEVdEDG 892
Cdd:PRK08316 318 CYG--QTEIAP---LAT----VlgpeehlrrpgSAG----RPVL-----------------NVETRVVDDD-GNDV-APG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 893 KEGEIWISSPSAGIGYWGKEELSQKTFRNklqnypgrKYTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PRK08316 366 EVGEIVHRSPQLMLGYWDDPEKTAEAFRG--------GWFHSGDLG-VMdeEGYITVVDRKKDMIKTGGENVASREVEEA 436
|
490 500
....*....|....*....|....*
gi 1917948728 971 V---ESSSELlrpgccAVIGVPEEV 992
Cdd:PRK08316 437 LythPAVAEV------AVIGLPDPK 455
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
526-1064 |
1.91e-26 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 116.66 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAhKLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP---PDPLQR-----GGQALTK 597
Cdd:PRK07059 50 TYGELDELSRALA-AWLQSRG--LAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPlytPRELEHqlkdsGAEAIVV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 598 IENIAKLCNAVaILSTVGYHAAVRA-----GLVKNLISFTGKSVKSTGQWPNLPwlhtdSWIKSSKVLPA-SNIAFQSES 671
Cdd:PRK07059 127 LENFATTVQQV-LAKTAVKHVVVASmgdllGFKGHIVNFVVRRVKKMVPAWSLP-----GHVRFNDALAEgARQTFKPVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 672 Q-PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLM-------RRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGS 743
Cdd:PRK07059 201 LgPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMeawlqpaFEKKPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 744 AILfspltfIRNPL---MWLQTISDYKATHSAGPNFAFELVIRRLEADKAkarnyDLSSMIFF----MIAAEPVRqktlK 816
Cdd:PRK07059 281 NIL------IPNPRdipGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKL-----DFSKLIVAngggMAVQRPVA----E 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 817 RFVELTRPFglsqevMAPGYGLAENCVFVSCaygkkKPILVD-WQGRIccGYVDPNdADVDIRivdadtglevDEDGKE- 894
Cdd:PRK07059 346 RWLEMTGCP------ITEGYGLSETSPVATC-----NPVDATeFSGTI--GLPLPS-TEVSIR----------DDDGNDl 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 895 -----GEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK07059 402 plgepGEICIRGPQVMAGYWNRPDETAKVMTAD-------GFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 969 KTVESSSELLRpgcCAVIGVPEEvlsakgislpDASDEVGLVVIAelRDSKLVNKDIIKQIESRvaeehgvtVASVKliR 1048
Cdd:PRK07059 475 EVVASHPGVLE---VAAVGVPDE----------HSGEAVKLFVVK--KDPALTEEDVKAFCKER--------LTNYK--R 529
|
570 580
....*....|....*....|..
gi 1917948728 1049 PRTIS------KTTSGKIKRFE 1064
Cdd:PRK07059 530 PKFVEfrtelpKTNVGKILRRE 551
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
526-1027 |
2.55e-26 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 114.71 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd17653 24 TYGELDAASNALANRL---LQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSAR-------IQAILRTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqseSQPDDLCFLQFTSGS 685
Cdd:cd17653 94 GATLLLTT---------------------------------------------------------DSPDDLAYIIFTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRST-SNTVLvswlpQYHDMGL---IGGLFTAMACGGSAILfspltfiRNPLMWLQ 761
Cdd:cd17653 117 TGIPKGVMVPHRGVLNYVSQPPARLDVGpGSRVA-----QVLSIAFdacIGEIFSTLCNGGTLVL-------ADPSDPFA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 762 TISDYKATHSAGPNFAFELvirrleadkaKARNYDLSSMIFFmiAAEPVRQKTLKRFVEltrpfglsQEVMAPGYGLAEn 841
Cdd:cd17653 185 HVARTVDALMSTPSILSTL----------SPQDFPNLKTIFL--GGEAVPPSLLDRWSP--------GRRLYNAYGPTE- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 842 CVfVSCAYGKKKPIlvdwqGRICCGYVDPNdadVDIRIVDADTgLEVDEdGKEGEIWISSPSAGIGYWGKEELSQKTFRN 921
Cdd:cd17653 244 CT-ISSTMTELLPG-----QPVTIGKPIPN---STCYILDADL-QPVPE-GVVGEICISGVQVARGYLGNPALTASKFVP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 922 kLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPgccAVIGVPEEVLSAkgISL 1000
Cdd:cd17653 313 -DPFWPGSRMYRTGDYGrWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQ---AAAIVVNGRLVA--FVT 386
|
490 500
....*....|....*....|....*...
gi 1917948728 1001 PDASDEVGL-VVIAELRDSKLVNKDIIK 1027
Cdd:cd17653 387 PETVDVDGLrSELAKHLPSYAVPDRIIA 414
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
526-1064 |
2.69e-26 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 114.48 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPI---PVLPPDPLqrggqaltkiENIA 602
Cdd:cd05919 12 TYGQLHDGANRLGSAL---RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVvinPLLHPDDY----------AYIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 KLCNAVAIlstvgyhaaVRAGlvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesqpDDLCFLQFT 682
Cdd:cd05919 79 RDCEARLV---------VTSA--------------------------------------------------DDIAYLLYS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 683 SGSTSDAKGVMITHGGLIHNVKLMRRRY-RSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLtfiRNPLMWLQ 761
Cdd:cd05919 100 SGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW---PTAERVLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 762 TISDYKATHSAG-PNFafelvIRRLEADKAKARNyDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLSqevMAPGYGLAE 840
Cdd:cd05919 177 TLARFRPTVLYGvPTF-----YANLLDSCAGSPD-ALRSLRLCVSAGEALPRGLGERWMEH---FGGP---ILDGIGATE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 841 NC-VFVSCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTF 919
Cdd:cd05919 245 VGhIFLSNRPGAWRL---GSTGRPVPGY--------EIRLVD-EEGHTI-PPGEEGDLLVRGPSAAVGYWNNPEKSRATF 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 920 RNKLQnYPGRKYTRTGDlGWVIQgnlfiTGRIKDLIIVAGRNIYSADVEKTVesssellrpgcCAVIGVPEEVLsakgIS 999
Cdd:cd05919 312 NGGWY-RTGDKFCRDAD-GWYTH-----AGRADDMLKVGGQWVSPVEVESLI-----------IQHPAVAEAAV----VA 369
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 1000 LPDASDEVGLVVIAELRDSKLVNKDIIKQIESRVAEehgvTVASVKliRPRTIS------KTTSGKIKRFE 1064
Cdd:cd05919 370 VPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLE----RLSAHK--VPRRIAfvdelpRTATGKLQRFK 434
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
671-1063 |
3.51e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 114.85 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 671 SQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILfspL 750
Cdd:cd05914 86 SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVF---L 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 TFIRNPLMWLQtiSDYKATHSAG---PNFAFELVIRRLEADKAKARN-YDLSSMIFFMIAAEPVRQKTLKRFVELTRPF- 825
Cdd:cd05914 163 DKIPSAKIIAL--AFAQVTPTLGvpvPLVIEKIFKMDIIPKLTLKKFkFKLAKKINNRKIRKLAFKKVHEAFGGNIKEFv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 826 ----GLSQEV----------MAPGYGLAENCVFVScaYGKKKPILVDwqgriCCGYVDPNdadVDIRIVDADTGLEvded 891
Cdd:cd05914 241 iggaKINPDVeeflrtigfpYTIGYGMTETAPIIS--YSPPNRIRLG-----SAGKVIDG---VEVRIDSPDPATG---- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 892 gkEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIV-AGRNIYSADVEK 969
Cdd:cd05914 307 --EGEIIVRGPNVMKGYYKNPEATAEAFDKD-------GWFHTGDLGkIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 970 TVESSSELLRpgccAVIGVPEEVLSAKGISLPDASDEvglvviaelrdSKLVNKDIIKQIESRVAEEHGVTVASVK---- 1045
Cdd:cd05914 378 KINNMPFVLE----SLVVVQEKKLVALAYIDPDFLDV-----------KALKQRNIIDAIKWEVRDKVNQKVPNYKkisk 442
|
410
....*....|....*....
gi 1917948728 1046 -LIRPRTISKTTSGKIKRF 1063
Cdd:cd05914 443 vKIVKEEFEKTPKGKIKRF 461
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
665-991 |
1.18e-25 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 113.58 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 665 IAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSA 744
Cdd:cd05909 138 IFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 745 IL-FSPLtfirNPLMWLQTISDYKATHSAG-PNFaFELVIRRleadkakARNYDLSSMIFFMIAAEPVRQKTLKRFVELt 822
Cdd:cd05909 218 VFhPNPL----DYKKIPELIYDKKATILLGtPTF-LRGYARA-------AHPEDFSSLRLVVAGAEKLKDTLRQEFQEK- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 823 rpFGLsqeVMAPGYGLAENCVFVSCaygkKKPILVDWQGriCCGYVDPNdadVDIRIVDADTGLEVDEdGKEGEIWISSP 902
Cdd:cd05909 285 --FGI---RILEGYGTTECSPVISV----NTPQSPNKEG--TVGRPLPG---MEVKIVSVETHEEVPI-GEGGLLLVRGP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 903 SAGIGYWGKEELSQKTFrnklqnypGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvESSSELLRP- 980
Cdd:cd05909 350 NVMLGYLNEPELTSFAF--------GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIE---DILSEILPEd 418
|
330
....*....|.
gi 1917948728 981 GCCAVIGVPEE 991
Cdd:cd05909 419 NEVAVVSVPDG 429
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
526-951 |
1.32e-25 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 116.49 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAK---VipiPVLPPDPLQRggqaltkIENIA 602
Cdd:COG1020 503 TYAELNARANRLAHHL---RALGVGPGDLVGVCLERSLEMVVALLAVLKAGaayV---PLDPAYPAER-------LAYML 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 KLCNAVAILSTvgyhAAVRAGLvknlisftgksvkstgQWPNLPWLHTDSWIKSSkvLPASNIAfqSESQPDDLCFLQFT 682
Cdd:COG1020 570 EDAGARLVLTQ----SALAARL----------------PELGVPVLALDALALAA--EPATNPP--VPVTPDDLAYVIYT 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 683 SGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTfIRNPLMWLQT 762
Cdd:COG1020 626 SGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEA-RRDPAALAEL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 763 ISDYKATHSagpNF---AFELVirrLEADKAkarnyDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLA 839
Cdd:COG1020 704 LARHRVTVL---NLtpsLLRAL---LDAAPE-----ALPSLRLVLVGGEALPPELVRRWRAR-----LPGARLVNLYGPT 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 840 ENCVFVSCAygkkkPILVD--WQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQK 917
Cdd:COG1020 768 ETTVDSTYY-----EVTPPdaDGGSVPIGRPIAN---TRVYVLDAH--LQPVPVGVPGELYIGGAGLARGYLNRPELTAE 837
|
410 420 430
....*....|....*....|....*....|....*
gi 1917948728 918 TFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRI 951
Cdd:COG1020 838 RFVADPFGFPGARLYRTGDLArWLPDGNLEFLGRA 872
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
522-1064 |
2.91e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 112.92 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 522 GCQRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLvHVPGL-DFIDAFFGCLRAKVIPIPVLPpdplQRGGQALTKIEN 600
Cdd:PRK06087 47 GASYTYSALDHAASRLANWLLAK---GIEPGDRVAF-QLPGWcEFTIIYLACLKVGAVSVPLLP----SWREAELVWVLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 601 iakLCNAVAILSTVGYHAAVRAGLVKNLISftgksvkstgQWPNL-PWLHTDSWIKSSKVLPASNIAFQSES-------Q 672
Cdd:PRK06087 119 ---KCQAKMFFAPTLFKQTRPVDLILPLQN----------QLPQLqQIVGVDKLAPATSSLSLSQIIADYEPlttaittH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSpltf 752
Cdd:PRK06087 186 GDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD---- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 753 IRNPLMWLQTISDYKATHSAGPN-FAFELvIRRLEADKakarnYDLSSMIFFMIAAEPVRqktlKRFVELTRPFGLsqeV 831
Cdd:PRK06087 262 IFTPDACLALLEQQRCTCMLGATpFIYDL-LNLLEKQP-----ADLSALRFFLCGGTTIP----KKVARECQQRGI---K 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 832 MAPGYGLAENCVFVSCAYGKKKPILVDWQGRICCGyvdpndadVDIRIVDADTGlEVDEdGKEGEIWISSPSAGIGYWGK 911
Cdd:PRK06087 329 LLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAG--------VEIKVVDEARK-TLPP-GCEGEEASRGPNVFMGYLDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 912 EELSQKTFRNKlqnypGRKYtrTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVessSELLRPGCCAVIGVPE 990
Cdd:PRK06087 399 PELTARALDEE-----GWYY--SGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDIL---LQHPKIHDACVVAMPD 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 991 EVLSAKGISLPDASDEVGLVVIAELRdSKLVNKDIIKqiesRVAEEHGVTVASvklirprtISKTTSGKIKRFE 1064
Cdd:PRK06087 469 ERLGERSCAYVVLKAPHHSLTLEEVV-AFFSRKRVAK----YKYPEHIVVIDK--------LPRTASGKIQKFL 529
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
1747-2045 |
3.61e-24 |
|
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity.
Pssm-ID: 163706 Cd Length: 283 Bit Score: 104.95 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1747 RYFHRIGVSGKGYLKLYDDIQGLPEHDIFGPGKRYTVIVRHSNSLSADDDARlDARGAALRI-LSDDSPLLDLTLKTGKA 1825
Cdd:cd08150 3 RGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGAGIDDTKP-DIRGFAIKFtGVADAGTLDFVLNNTPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1826 FYARTISDFATWLV---------CGLAAREEHVKRVPH-VRDAVWTSLRQADSFADLHYYSNTCRLFRFKDRQEMYVKFK 1895
Cdd:cd08150 82 FFIRNTSDYEDFVAefarsargePPLDFIAWYVEKRPEdLPNLLGARSQVPDSYAAARYFSQVTFAFINGAGKYRVVRSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1896 LRPSDENIEEDIGKVEpsgilppetgaiprdandTRPLLFLAEDFHNRV-KSPsgVRYIFQLQVRPiPQDEAARDialDC 1974
Cdd:cd08150 162 DNPVDGIPSLEDHELE------------------ARPPDYLREELTERLqRGP--VVYDFRIQLND-DTDATTID---NP 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 1975 TKPWDESQfPYIDVGEVIINENLTKEGSEKLEVNPFLRCHEVDVIRATSssqsaSIDHGRSLIYEICQHLR 2045
Cdd:cd08150 218 TILWPTEH-PVEAVAKITIPPPTFTAAQEAFAFNPFTPWHGLLETNDLG-----PILEVRRRVYTSSQGLR 282
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
520-991 |
4.09e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 109.47 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 520 AVGCQRTYAELDSNASCVAHKLltSRKPTIKPGDRVLlVHVPG-LDFIDAFFGCLRAKVIpipVLPPDPL---------- 588
Cdd:PRK05677 45 NLGKTLTYGELYKLSGAFAAWL--QQHTDLKPGDRIA-VQLPNvLQYPVAVFGAMRAGLI---VVNTNPLytaremehqf 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 589 -QRGGQALTKIENIAKLCNAV--------AILSTVG-YHAAVRAGLVKNLISFTGKSVkstgqwpnlPWLHTDSWIKSSK 658
Cdd:PRK05677 119 nDSGAKALVCLANMAHLAEKVlpktgvkhVIVTEVAdMLPPLKRLLINAVVKHVKKMV---------PAYHLPQAVKFND 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 659 VLPA-SNIAFQSES-QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSN---TVLVSWLPQYHDMGLIGG 733
Cdd:PRK05677 190 ALAKgAGQPVTEANpQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNegcEILIAPLPLYHIYAFTFH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 734 LFTAMACGGSAILfspltfIRNPL---MWLQTISDYKATHSAGPNFAFELVIRRleadkAKARNYDLSSMIFFMIAAEPV 810
Cdd:PRK05677 270 CMAMMLIGNHNIL------ISNPRdlpAMVKELGKWKFSGFVGLNTLFVALCNN-----EAFRKLDFSALKLTLSGGMAL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 811 RQKTLKRFVELTrpfGLSqevMAPGYGLAENCVFVScaygkkkpilVDWQGRICCGYVDPNDADVDIRIVDaDTGLEVDE 890
Cdd:PRK05677 339 QLATAERWKEVT---GCA---ICEGYGMTETSPVVS----------VNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 891 dGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGwVIQ--GNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK05677 402 -GEVGELCVKGPQVMKGYWQRPEATDEILDSD-------GWLKTGDIA-LIQedGYMRIVDRKKDMILVSGFNVYPNELE 472
|
490 500
....*....|....*....|...
gi 1917948728 969 KTVESSSELLRpgcCAVIGVPEE 991
Cdd:PRK05677 473 DVLAALPGVLQ---CAAIGVPDE 492
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
551-1062 |
6.20e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 107.91 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 551 PGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVL-PPDPlqrgGQALTKIENIAKLCNAVAILSTVGYHAAVRAGLVKNLI 629
Cdd:cd05922 17 RGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvPLNP----TLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 630 SFTgksvkstgqwpnlpWLHTDSWIKSSKVLPASniafqsESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRR 709
Cdd:cd05922 93 PGT--------------VLDADGIRAARASAPAH------EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 710 YRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILFS----PLTFIRnplmwlqTISDYKATHSAGPNFAFELvIRRL 785
Cdd:cd05922 153 LGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNdgvlDDAFWE-------DLREHGATGLAGVPSTYAM-LTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 786 EADKAKarnydLSSMIFFMIAAEPVRQKTLKRFVELTRpfGLSQEVMapgYGLAEncVFVSCAY-----GKKKPilvdwq 860
Cdd:cd05922 224 GFDPAK-----LPSLRYLTQAGGRLPQETIARLRELLP--GAQVYVM---YGQTE--ATRRMTYlpperILEKP------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 861 GRICCGYvdPNDAdvdIRIVDADTGLEvdEDGKEGEIWISSPSAGIGYWGKEELSQKtfrnklqnyPGRKYTR--TGDLG 938
Cdd:cd05922 286 GSIGLAI--PGGE---FEILDDDGTPT--PPGEPGEIVHRGPNVMKGYWNDPPYRRK---------EGRGGGVlhTGDLA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 939 WVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlrpGCCAVIGVPeevlsakgislPDASDEVGLVVIAelrD 1017
Cdd:cd05922 350 RRDEdGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI---IEAAAVGLP-----------DPLGEKLALFVTA---P 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1917948728 1018 SKLVNKDIIkqiesRVAEEHGVTVASVKLIRP-RTISKTTSGKIKR 1062
Cdd:cd05922 413 DKIDPKDVL-----RSLAERLPPYKVPATVRVvDELPLTASGKVDY 453
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
526-989 |
1.10e-23 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 106.95 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaLTKIENIAKlc 605
Cdd:cd05945 18 TYRELKERADALAAALASL---GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER----IREILDAAK-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 navailstvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlPASNIAFqsesqPDDLCFLQFTSGS 685
Cdd:cd05945 89 -------------------------------------------------------PALLIAD-----GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILFsPLTFIRNPLMWLQTISD 765
Cdd:cd05945 109 TGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPV-PRDATADPKQLFRFLAE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 766 YKAT--HSAgPNFAfELVIRRlEADKAKArnydLSSMIFFMIAAEPVRQKTLKRFVELtrpfglsqevmAPG------YG 837
Cdd:cd05945 187 HGITvwVST-PSFA-AMCLLS-PTFTPES----LPSLRHFLFCGEVLPHKTARALQQR-----------FPDariyntYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 838 LAENCvfVSCAYGKKKPILVDWQGRICCGYVDPndaDVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQK 917
Cdd:cd05945 249 PTEAT--VAVTYIEVTPEVLDGYDRLPIGYAKP---GAKLVILDED-GRPV-PPGEKGELVISGPSVSKGYLNNPEKTAA 321
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728 918 TFRnklqNYPGRKYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlrpGCCAVIGVP 989
Cdd:cd05945 322 AFF----PDEGQRAYRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV---KEAVVVPKY 387
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
672-1035 |
1.32e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 108.26 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 672 QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMACGGS-AILFSPL 750
Cdd:COG1022 181 KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY-ALAAGATvAFAESPD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 TFIRN------------PLMW---LQTISDyKATHSAGP-----NFAFELVIRRLEA----------DKAKARNYDLssM 800
Cdd:COG1022 260 TLAEDlrevkptfmlavPRVWekvYAGIQA-KAEEAGGLkrklfRWALAVGRRYARArlagkspsllLRLKHALADK--L 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 801 IFfmiaaEPVRQKT---LKRFV--------ELTRPF---GLsqeVMAPGYGLAENCVFVSC-AYGKKKPILVdwqGRICC 865
Cdd:COG1022 337 VF-----SKLREALggrLRFAVsggaalgpELARFFralGI---PVLEGYGLTETSPVITVnRPGDNRIGTV---GPPLP 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 866 GyvdpndadVDIRIvdadtglevdedGKEGEIWISSPSAGIGYWGKEELSQKTFrnklqnypgrkyT-----RTGDLGWV 940
Cdd:COG1022 406 G--------VEVKI------------AEDGEILVRGPNVMKGYYKNPEATAEAF------------DadgwlHTGDIGEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 941 I-QGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS---SELL-----RPGCCAVIgVP-----EEVLSAKGISLPDASD 1005
Cdd:COG1022 454 DeDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASpliEQAVvvgdgRPFLAALI-VPdfealGEWAEENGLPYTSYAE 532
|
410 420 430
....*....|....*....|....*....|
gi 1917948728 1006 EVGlvviaelrdsklvNKDIIKQIESRVAE 1035
Cdd:COG1022 533 LAQ-------------DPEVRALIQEEVDR 549
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
526-1062 |
2.46e-23 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 105.61 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVipiPVLPPDPLQRGGQALTKIENIAKlc 605
Cdd:TIGR01923 1 TWQDLDCEAAHLAKAL---KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGA---EIAMLNTRLTENERTNQLEDLDV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 navailstvgyhaavraGLVKNLISFTGKSVKSTgqwpNLPWLHTDSwiksskvlpASNIAFQSESQPDDLCFLQFTSGS 685
Cdd:TIGR01923 73 -----------------QLLLTDSLLEEKDFQAD----SLDRIEAAG---------RYETSLSASFNMDQIATLMFTSGT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILFSPLTFIrnplmwLQTISD 765
Cdd:TIGR01923 123 TGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFNQL------LEMIAN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 766 YKATH-SAGPNfafeLVIRRLEADkakARNYDLSSmifFMIAAEPVRQKTLKRFVELTRPFGLsqevmapGYGLAENCVF 844
Cdd:TIGR01923 196 ERVTHiSLVPT----QLNRLLDEG---GHNENLRK---ILLGGSAIPAPLIEEAQQYGLPIYL-------SYGMTETCSQ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 845 VsCAygkkKPILVDwQGRICCGYVDPNdadVDIRIvdadtglEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNklq 924
Cdd:TIGR01923 259 V-TT----ATPEML-HARPDVGRPLAG---REIKI-------KVDNKEGHGEIMVKGANLMKGYLYQGELTPAFEQQ--- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 925 nypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEevlsakgislpda 1003
Cdd:TIGR01923 320 -----GWFNTGDIGeLDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQE---AVVVPKPD------------- 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 1004 sDEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVTVASVKLirpRTISKTTSGKIKR 1062
Cdd:TIGR01923 379 -AEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKL---DELPYNASGKILR 433
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
496-991 |
5.85e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 105.89 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 496 YLKHWAaQEITQNKALYTWineggavGCQRTYAELDSNASCVAhKLLTSRKptIKPGDRV--LLVHVPglDFIDAFFGCL 573
Cdd:PRK06178 38 YLRAWA-RERPQRPAIIFY-------GHVITYAELDELSDRFA-ALLRQRG--VGAGDRVavFLPNCP--QFHIVFFGIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 574 RAKVIPIPVlppDPLQRGGQALTKIeNIAKLCNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQwPNLPW------ 647
Cdd:PRK06178 105 KLGAVHVPV---SPLFREHELSYEL-NDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAE-PTLPLpdslra 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 648 --LHTDSWIKSSKVLPASNIAFQSES-QPDDLCFLQFTSGSTSDAKGVMITHGGLI------HNVKLmrrryRSTSNTVL 718
Cdd:PRK06178 180 prLAAAGAIDLLPALRACTAPVPLPPpALDALAALNYTGGTTGMPKGCEHTQRDMVytaaaaYAVAV-----VGGEDSVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 719 VSWLPQY----HDMGLIGGLFtamaCGGSAILFS---PLTFirnplmwLQTISDYKATHSAGP-NFAFELVirrleaDKA 790
Cdd:PRK06178 255 LSFLPEFwiagENFGLLFPLF----SGATLVLLArwdAVAF-------MAAVERYRVTRTVMLvDNAVELM------DHP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 791 KARNYDLSSM-----IFFMIAAEPV-RQktlkRFVELTrpfglsqevmapGYGLAEncvfvsCAYGKKKPILVDwqgRIC 864
Cdd:PRK06178 318 RFAEYDLSSLrqvrvVSFVKKLNPDyRQ----RWRALT------------GSVLAE------AAWGMTETHTCD---TFT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 865 CGYVDpNDADV--------------DIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNklqnypgrK 930
Cdd:PRK06178 373 AGFQD-DDFDLlsqpvfvglpvpgtEFKICDFETG-ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD--------G 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728 931 YTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEE 991
Cdd:PRK06178 443 WLHTGDIG-KIdeQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLG---SAVVGRPDP 501
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
524-993 |
2.14e-22 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 103.56 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLltsRKPTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPpdplqrgGQALTKIENIA 602
Cdd:cd05920 40 RLTYRELDRRADRLAAGL---RGLGIRPGDRVV-VQLPnVAEFVVLFFALLRLGAVPVLALP-------SHRRSELSAFC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 KLCNAVAilstvgYHAAVRAGLVKNLisftgksvkstgqwpnlpwlhtdswiksskvlpasNIAFQS-ESQPDdLCFLQF 681
Cdd:cd05920 109 AHAEAVA------YIVPDRHAGFDHR-----------------------------------ALARELaESIPE-VALFLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIG-GLFTAMACGGSAILFSPLTfirnPLMWL 760
Cdd:cd05920 147 SGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPS----PDAAF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 761 QTISDYKATHSAgpnfafeLV--IRRLEADKAKARNYDLSSMIFFMIAAEPVrQKTLKRFVELTRPFGLsQEVmapgYGL 838
Cdd:cd05920 223 PLIEREGVTVTA-------LVpaLVSLWLDAAASRRADLSSLRLLQVGGARL-SPALARRVPPVLGCTL-QQV----FGM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 839 AENCVFVScAYGKKKPILVDWQGRiccgyvdPNDADVDIRIVDADtGLEVDEdGKEGEIWISSPSAGIGYWGKEELSQKT 918
Cdd:cd05920 290 AEGLLNYT-RLDDPDEVIIHTQGR-------PMSPDDEIRVVDEE-GNPVPP-GEEGELLTRGPYTIRGYYRAPEHNARA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 919 FrnklqNYPGrkYTRTGDLgwvIQ----GNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC--CAVIGVPEE 991
Cdd:cd05920 360 F-----TPDG--FYRTGDL---VRrtpdGYLVVEGRIKDQINRGGEKIAAEEVE------NLLLRhPAVhdAAVVAMPDE 423
|
..
gi 1917948728 992 VL 993
Cdd:cd05920 424 LL 425
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
526-1064 |
7.60e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 102.65 E-value: 7.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP---PDPLQR-----GGQALTK 597
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQ--LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPlytPRELKHqlidsGASVLVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 598 IENiakLCNAVA-ILSTVGYHAAVRAGL-------VKNLISFTGKSVKSTgqwpnLPWLHTDSWIK--------SSKVLP 661
Cdd:PRK08751 130 IDN---FGTTVQqVIADTPVKQVITTGLgdmlgfpKAALVNFVVKYVKKL-----VPEYRINGAIRfrealalgRKHSMP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 662 ASNIAfqsesqPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTS-----NTVLVSWLPQYHDMGLIGGLFT 736
Cdd:PRK08751 202 TLQIE------PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGkleegCEVVITALPLYHIFALTANGLV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 737 AMACGGSAILFS-PltfiRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKAkarnyDLSSMIFFMIAAEPVRQKTL 815
Cdd:PRK08751 276 FMKIGGCNHLISnP----RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI-----DFSSLKMTLGGGMAVQRSVA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 816 KRFVELTrpfGLSqevMAPGYGLAEncvfVSCAYGKKKPILVDWQGRIccGYVDPNdADVDIRIvDADTGLEVdedGKEG 895
Cdd:PRK08751 347 ERWKQVT---GLT---LVEAYGLTE----TSPAACINPLTLKEYNGSI--GLPIPS-TDACIKD-DAGTVLAI---GEIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 896 EIWISSPSAGIGYWGKEELSQKTFrnklqnyPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESS 974
Cdd:PRK08751 410 ELCIKGPQVMKGYWKRPEETAKVM-------DADGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 975 SELLRpgcCAVIGVPEEvlsakgislpdASDEVGLVVIAElRDSKLVNKDIikqiesrvaEEHGVT-VASVKLIR----P 1049
Cdd:PRK08751 483 PGVLE---VAAVGVPDE-----------KSGEIVKVVIVK-KDPALTAEDV---------KAHARAnLTGYKQPRiiefR 538
|
570
....*....|....*
gi 1917948728 1050 RTISKTTSGKIKRFE 1064
Cdd:PRK08751 539 KELPKTNVGKILRRE 553
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
500-1050 |
1.11e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 101.90 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 500 WAAQEITQNKALY---TWINEGGAVGCQRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAK 576
Cdd:PRK09274 14 RAAQERPDQLAVAvpgGRGADGKLAYDELSFAELDARSDAIAHGLNAA---GIGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 577 VIPIPVlppDPlqrgGQAltkIENIAKlcnavaILSTVGYHAAV---RAGLVKNLISFTGKSVK---STGQwpnlpwlht 650
Cdd:PRK09274 91 AVPVLV---DP----GMG---IKNLKQ------CLAEAQPDAFIgipKAHLARRLFGWGKPSVRrlvTVGG--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 651 dSWIKSSKVL-----PASNIAFQ-SESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQ 724
Cdd:PRK09274 146 -RLLWGGTTLatllrDGAAAPFPmADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 725 YhdmgligGLFtAMACGGSAILfSPLTFIR----NPLMWLQTISDYKATHSAGpNFAfelVIRRLeADKAKARNYDLSSM 800
Cdd:PRK09274 225 F-------ALF-GPALGMTSVI-PDMDPTRpatvDPAKLFAAIERYGVTNLFG-SPA---LLERL-GRYGEANGIKLPSL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 801 IFFMIAAEPVRQKTLKRFVELTRPFGlsqEVMAPgYGLAEncVFVSCAYGKKKPILVDWQ-----GRICCGYVDPndaDV 875
Cdd:PRK09274 291 RRVISAGAPVPIAVIERFRAMLPPDA---EILTP-YGATE--ALPISSIESREILFATRAatdngAGICVGRPVD---GV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 876 DIRIVDADTGL--EVDED-----GKEGEIWISSPSAGIGYWGKEELSQKtfrNKLQNYPGRKYTRTGDLGWV-IQGNLFI 947
Cdd:PRK09274 362 EVRIIAISDAPipEWDDAlrlatGEIGEIVVAGPMVTRSYYNRPEATRL---AKIPDGQGDVWHRMGDLGYLdAQGRLWF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 948 TGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEevlsaKGISLPdasdevglVVIAELRDSKLVNKDIIK 1027
Cdd:PRK09274 439 CGRKAHRVETAGGTLYTIPCERIFNTHPGVKR---SALVGVGV-----PGAQRP--------VLCVELEPGVACSKSALY 502
|
570 580
....*....|....*....|....*.
gi 1917948728 1028 QiESRV-AEEHGVTvASVK--LIRPR 1050
Cdd:PRK09274 503 Q-ELRAlAAAHPHT-AGIErfLIHPS 526
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
672-1034 |
1.33e-21 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 101.11 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 672 QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FS 748
Cdd:PRK07514 154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFlpkFD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 749 PLTFIRnpLMwlqtisdYKATHSAG-PNFafelVIRRLEA---DKAKARNydlssMIFFMIAAEPVRQKTLKRFVELT-- 822
Cdd:PRK07514 234 PDAVLA--LM-------PRATVMMGvPTF----YTRLLQEprlTREAAAH-----MRLFISGSAPLLAETHREFQERTgh 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 823 ----RpfglsqevmapgYGLAENCVFVSCAY-GKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVdEDGKEGEI 897
Cdd:PRK07514 296 aileR------------YGMTETNMNTSNPYdGERRA-----------GTVGFPLPGVSLRVTDPETGAEL-PPGEIGMI 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 898 WISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEK------- 969
Cdd:PRK07514 352 EVKGPNVFKGYWRMPEKTAEEFRAD-------GFFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGeidelpg 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728 970 TVESssellrpgccAVIGVPEevlsakgislPDASDEVGLVVIAElRDSKLVNKDIIKQIESRVA 1034
Cdd:PRK07514 425 VVES----------AVIGVPH----------PDFGEGVTAVVVPK-PGAALDEAAILAALKGRLA 468
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
521-991 |
1.44e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 101.44 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 521 VGCQRTYAELDSNASCVAHKLltSRKPTIKPGDRVLlVHVPG-LDFIDAFFGCLRAKVIpipVLPPDPL----------- 588
Cdd:PRK12492 46 LGVTLSYAELERHSAAFAAYL--QQHTDLVPGDRIA-VQMPNvLQYPIAVFGALRAGLI---VVNTNPLytaremrhqfk 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 589 QRGGQALTKIENIAKLCNAVAILSTVGYHAAVRAG---------LVKNLISFTGKSVkstgqwpnlPWLHTDSWIKSSKV 659
Cdd:PRK12492 120 DSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGdllpaakgwLVNTVVDKVKKMV---------PAYHLPQAVPFKQA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 660 LP-ASNIAFQSESQP-DDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRST----------SNTVLVSWLPQYHD 727
Cdd:PRK12492 191 LRqGRGLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqplmkeGQEVMIAPLPLYHI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 728 MGLIGGLFTAMACGGSAILfspLTFIRNPLMWLQTISDYKATHSAGPNFAFELVIrrleaDKAKARNYDLSSMIFFMIAA 807
Cdd:PRK12492 271 YAFTANCMCMMVSGNHNVL---ITNPRDIPGFIKELGKWRFSALLGLNTLFVALM-----DHPGFKDLDFSALKLTNSGG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 808 EPVRQKTLKRFVELTrpfGLSqevMAPGYGLAEnCVFVSCA--YGKkkpilvdwQGRIccGYVDPNDADVDIRIVDaDTG 885
Cdd:PRK12492 343 TALVKATAERWEQLT---GCT---IVEGYGLTE-TSPVASTnpYGE--------LARL--GTVGIPVPGTALKVID-DDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 886 LEVDEdGKEGEIWISSPSAGIGYWGKEELSQKTFrnklqnyPGRKYTRTGDLGwVIQGNLF--ITGRIKDLIIVAGRNIY 963
Cdd:PRK12492 405 NELPL-GERGELCIKGPQVMKGYWQQPEATAEAL-------DAEGWFKTGDIA-VIDPDGFvrIVDRKKDLIIVSGFNVY 475
|
490 500
....*....|....*....|....*...
gi 1917948728 964 SADVEKTVESSSELlrpGCCAVIGVPEE 991
Cdd:PRK12492 476 PNEIEDVVMAHPKV---ANCAAIGVPDE 500
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
526-992 |
4.11e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.96 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIpipVLPPDPlqrggqALTKIENIAKL- 604
Cdd:PRK05852 45 SYRDLARLVDDLAGQL---TRSGLLPGDRVALRMGSNAEFVVALLAASRADLV---VVPLDP------ALPIAEQRVRSq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 605 ---CNAVAILST-VGYHAAVRAGLVKNLISFTGksvkSTGQWPNLPWLHTDSwikssKVLPASNIAFQSESQPDDlCFLQ 680
Cdd:PRK05852 113 aagARVVLIDADgPHDRAEPTTRWWPLTVNVGG----DSGPSGGTLSVHLDA-----ATEPTPATSTPEGLRPDD-AMIM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 681 FTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL-----FSPLTFirn 755
Cdd:PRK05852 183 FTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpargrFSAHTF--- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 756 plmWlQTISDYKAT-HSAGPNFaFELVIRRLEADKAKARNYDLSsmiFFMIAAEPVRQKTLKrfveltrpfGLSQEVMAP 834
Cdd:PRK05852 260 ---W-DDIKAVGATwYTAVPTI-HQILLERAATEPSGRKPAALR---FIRSCSAPLTAETAQ---------ALQTEFAAP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 gyglaencvfVSCAYGKKKPI------LVDWQGR-----ICCGYVDPNDAdVDIRIVDADtGLEVDEDgKEGEIWISSPS 903
Cdd:PRK05852 323 ----------VVCAFGMTEAThqvtttQIEGIGQtenpvVSTGLVGRSTG-AQIRIVGSD-GLPLPAG-AVGEVWLRGTT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 904 AGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgc 982
Cdd:PRK05852 390 VVRGYLGDPTITAANFTDG--------WLRTGDLGSLSAaGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVME--- 458
|
490
....*....|
gi 1917948728 983 CAVIGVPEEV 992
Cdd:PRK05852 459 AAVFGVPDQL 468
|
|
| NRPS_term_dom |
TIGR02353 |
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
1229-1686 |
6.24e-21 |
|
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.
Pssm-ID: 274093 [Multi-domain] Cd Length: 695 Bit Score: 100.21 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1229 RIWSFQLLALLYISFILVFPAYLSISTFQILVSASHKLIDGLPWLHQASVVLLAPLSWILCIALTSISIAFFGNSFLRIN 1308
Cdd:TIGR02353 229 RRRLYVAGALFVVFVLLPPLAFLFAIPVAITFDEIDWTLGPDMVGFILALVLTFVALAGFIAYTVLLLAAVRLLLNLVLK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1309 YALTPEVSVWsvdfvkWWALYKAQEV--SSKVLAVHLRGTVFLKHWFEMLGARIGSSVLLDTVDITDPSLVSIGDGAVIA 1386
Cdd:TIGR02353 309 PGRYYVHSGF------YYQAWTVQQLmdNSRVLLFPLYASSYIPHWYRALGAKIGKVAEISSAQHEVPDLTDIGEETFIA 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1387 EGALLQSHEVRNSILRLQPIRIGRNCSVGPYAVVQKGSVLREGAEVpalqkseGGKSAL----KMAKAENILKVSPGTLK 1462
Cdd:TIGR02353 383 DGLLMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLL-------GVLSMTpkdgKVREGVGWLGSPPFELP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1463 TVQQfmgiyVVGFLSSL-SAATVYLLYMSLSqkVPSLELLAFLCISGALHWVPFTIVAYATMFTKAppNPFEFAISLAIA 1541
Cdd:TIGR02353 456 RRVN-----RDDELEALtFEPDPRRRLARKN--VENLRIILPFLLVQWAMLFALVVLDLQALDDYT--EWGAVALLAALI 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1542 YFAHGLVLSLLTSIFTHLLAGKEKKTQTHIKTWF--GHQLAIA-----CHVRFAKLLSGTEAFCMYLRLLGAKVGRYCSI 1614
Cdd:TIGR02353 527 LMAVGVGAFLILVERKWLVFGRLKPQEHPLWSPFvwLHELHWKlyesvAVPNFLRPFRGTPFLPAILRLLGVKIGRGVYI 606
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 1615 RAINpIADPRMVSIGAGVHLGDFSRIITGFYSQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDVILGAISV 1686
Cdd:TIGR02353 607 DGTD-LTERDLVTIGDDSTLNEGSVIQTHLFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSL 677
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
681-1062 |
1.47e-20 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 95.41 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 681 FTSGSTSDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLfTAMACGGSAILFSPLTFIRNPLMW 759
Cdd:cd17635 8 FTSGTTGEPKAVLLANKTFFaVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWIL-TCLIHGGLCVTGGENTTYKSLFKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 760 LQTisdYKATHSA-GPNFAFELVirrLEADKAKARNYDLSSMIF---FMIAAEpvrqktlKRFVELtrpFGLSQEVMApg 835
Cdd:cd17635 87 LTT---NAVTTTClVPTLLSKLV---SELKSANATVPSLRLIGYggsRAIAAD-------VRFIEA---TGLTNTAQV-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 836 YGLAENCVFVSCAYGKkkpilvdwqGRICCGYVDPNDADVDIRIVDADtGLEVDEDGkEGEIWISSPSAGIGYWGKEELS 915
Cdd:cd17635 149 YGLSETGTALCLPTDD---------DSIEINAVGRPYPGVDVYLAATD-GIAGPSAS-FGTIWIKSPANMLGYWNNPERT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 916 QKTFRNKlqnypgrkYTRTGDLGWVIQGN-LFITGRIKDLIIVAGRNIYSADVEKTVESssellrpgccaVIGVPEevls 994
Cdd:cd17635 218 AEVLIDG--------WVNTGDLGERREDGfLFITGRSSESINCGGVKIAPDEVERIAEG-----------VSGVQE---- 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 995 AKGISLPDAsdEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGvtvasvKLIRPRTIS------KTTSGKIKR 1062
Cdd:cd17635 275 CACYEISDE--EFGELVGLAVVASAELDENAIRALKHTIRRELE------PYARPSTIVivtdipRTQSGKVKR 340
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
526-1018 |
2.41e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 96.96 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPLQRggqaltkienia 602
Cdd:cd12114 14 TYGELAERARRVAGAL---KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVdidQPAARREA------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 603 klcnavaILSTVGYHAAVRAGlvknlisftgksvkstGQWPNLPWLHTDSwIKSSKVLPASNIAFQSESQPDDLCFLQFT 682
Cdd:cd12114 79 -------ILADAGARLVLTDG----------------PDAQLDVAVFDVL-ILDLDALAAPAPPPPVDVAPDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 683 SGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTfIRNPLMWLQT 762
Cdd:cd12114 135 SGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLS-VYDIFGALSAGATLVLPDEAR-RRDPAHWAEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 763 ISDYKATHSagpNFA---FELVIRRLEADKAkarnyDLSSMIFFMIAAEPVRQ---KTLKRFVELTRPFGLSqevmapgy 836
Cdd:cd12114 213 IERHGVTLW---NSVpalLEMLLDVLEAAQA-----LLPSLRLVLLSGDWIPLdlpARLRALAPDARLISLG-------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 837 GLAENCVFvSCAYgKKKPILVDWqGRICCGYVDPNDAdvdIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQ 916
Cdd:cd12114 277 GATEASIW-SIYH-PIDEVPPDW-RSIPYGRPLANQR---YRVLDPR-GRDC-PDWVPGELWIGGRGVALGYLGDPELTA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 917 KTFrnkLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpGCCAVIGVPEE---- 991
Cdd:cd12114 349 ARF---VTHPDGERLYRTGDLGrYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVAR-AVVVVLGDPGGkrla 424
|
490 500
....*....|....*....|....*...
gi 1917948728 992 -VLSAKGISLPDASDEVGLVVIAELRDS 1018
Cdd:cd12114 425 aFVVPDNDGTPIAPDALRAFLAQTLPAY 452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
673-1060 |
3.34e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 94.85 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTF 752
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 753 iRNPLM----WlQTISDYKAThsagpnfAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTrpfGLS 828
Cdd:cd05944 81 -RNPGLfdnfW-KLVERYRIT-------SLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDAT---GLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 829 qevMAPGYGLAENCVFVSCAY--GKKKPilvdwqGRIccGYVDPNdADVDIRIVDADTGLEVDEDGKE-GEIWISSPSAG 905
Cdd:cd05944 149 ---VVEGYGLTEATCLVAVNPpdGPKRP------GSV--GLRLPY-ARVRIKVLDGVGRLLRDCAPDEvGEICVAGPGVF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 906 IGYWGKEelsqktfrNKLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlrpGCCA 984
Cdd:cd05944 217 GGYLYTE--------GNKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV---AFAG 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 985 VIGVPEevlsAKGISLPdasdeVGLVVIAelRDSKLVNKDIIKQIESRVAEEHGVTVAsVKLIRPrtISKTTSGKI 1060
Cdd:cd05944 286 AVGQPD----AHAGELP-----VAYVQLK--PGAVVEEEELLAWARDHVPERAAVPKH-IEVLEE--LPVTAVGKV 347
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
666-991 |
5.87e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 96.38 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 666 AFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACgGSAI 745
Cdd:PRK12583 193 ERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTV-GACL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 746 LFSPLTFirNPLMWLQTISDYKAT--HSAGPNFAFELvirrleaDKAKARNYDLSSMIFFMIAAEPVRQKTLKRFV-ELT 822
Cdd:PRK12583 272 VYPNEAF--DPLATLQAVEEERCTalYGVPTMFIAEL-------DHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMdEMH 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 823 RPfglsqEVMApGYGLAENC-VFVSCAYGKKKPILVDWQGRiccgyvdpNDADVDIRIVDADTglEVDEDGKEGEIWISS 901
Cdd:PRK12583 343 MA-----EVQI-AYGMTETSpVSLQTTAADDLERRVETVGR--------TQPHLEVKVVDPDG--ATVPRGEIGELCTRG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 902 PSAGIGYWGKEELSQKTFrnklqnyPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRp 980
Cdd:PRK12583 407 YSVMKGYWNNPEATAESI-------DEDGWMHTGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVAD- 478
|
330
....*....|.
gi 1917948728 981 gcCAVIGVPEE 991
Cdd:PRK12583 479 --VQVFGVPDE 487
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
522-1062 |
9.90e-20 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 95.10 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENI 601
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRL---RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER-------LAFM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 602 AKLCNAVAILStvgyHAAVRAGLVknlisftgksvkstgqwPNLPWLHTDSWIKSSKVLPASNIAfqsESQPDDLCFLQF 681
Cdd:cd17651 88 LADAGPVLVLT----HPALAGELA-----------------VELVAVTLLDQPGAAAGADAEPDP---ALDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAIL------FSPLTFIRn 755
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSV-QEIFSTLCAGATLVLppeevrTDPPALAA- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 756 plmWLQTisdYKATHSAGPNFAFELVIrrLEADKAKARNYDLSSMIffmIAAEPVRQKTLKRfvELTRpfGLSQEVMAPG 835
Cdd:cd17651 222 ---WLDE---QRISRVFLPTVALRALA--EHGRPLGVRLAALRYLL---TGGEQLVLTEDLR--EFCA--GLPGLRLHNH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 836 YGLAENCVfVSC--------AYGKKKPIlvdwqGRiccgyvdPNDaDVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIG 907
Cdd:cd17651 287 YGPTETHV-VTAlslpgdpaAWPAPPPI-----GR-------PID-NTRVYVLDAA--LRPVPPGVPGELYIGGAGLARG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 908 YWGKEELSQKTFRnKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLRpgccaVI 986
Cdd:cd17651 351 YLNRPELTAERFV-PDPFVPGARMYRTGDLArWLPDGELEFLGRADDQVKIRGFRIELGEIE------AALAR-----HP 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728 987 GVPEEVLSAKgislPDASDEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVTVASVKLIR-PRtiskTTSGKIKR 1062
Cdd:cd17651 419 GVREAVVLAR----EDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDAlPL----TPNGKLDR 487
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
669-991 |
1.21e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 95.44 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 669 SESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFTA--MACGGSAIL 746
Cdd:PRK06188 163 AAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH----AGGAFFLptLLRGGTVIV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 747 ---FSPLTFIRnplmwlqTISDYKAThsagpnFAFeLV---IRRLeADKAKARNYDLSSMIFFMIAAEPVrqkTLKRFVE 820
Cdd:PRK06188 239 lakFDPAEVLR-------AIEEQRIT------ATF-LVptmIYAL-LDHPDLRTRDLSSLETVYYGASPM---SPVRLAE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 821 LTRPFGlsqEVMAPGYGLAEnCVFVSCAYGKKKPILVDWQGRICCGYVDPNdadVDIRIVDADtGLEVDEdGKEGEIWIS 900
Cdd:PRK06188 301 AIERFG---PIFAQYYGQTE-APMVITYLRKRDHDPDDPKRLTSCGRPTPG---LRVALLDED-GREVAQ-GEVGEICVR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 901 SPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELlr 979
Cdd:PRK06188 372 GPLVMDGYWNRPEETAEAFRDG--------WLHTGDVAREDEdGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV-- 441
|
330
....*....|..
gi 1917948728 980 pGCCAVIGVPEE 991
Cdd:PRK06188 442 -AQVAVIGVPDE 452
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
675-1017 |
1.54e-19 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 92.18 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 675 DLCFLQFTSGSTSDAKGVMITHGGLI-------HNVKLmrrryRSTSNTVLVSwlPQYHDMGLIGGLFTAMACGgsAILF 747
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaaawaDCADL-----TEDDRYLIIN--PFFHTFGYKAGIVACLLTG--ATVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 SPLTFirNPLMWLQTISDYKATHSAGPNFAFELVIrrleaDKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVEltrpfGL 827
Cdd:cd17638 72 PVAVF--DVDAILEAIERERITVLPGPPTLFQSLL-----DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRS-----EL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 828 SQEVMAPGYGLAENCVFVSCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDAdtglevdedgkeGEIWISSPSAGIG 907
Cdd:cd17638 140 GFETVLTAYGLTEAGVATMCRPGDDAETVATTCGRAC--------PGFEVRIADD------------GEVLVRGYNVMQG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 908 YWGKEELSQKTFrnklqnyPGRKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVessSELLRPGCCAVI 986
Cdd:cd17638 200 YLDDPEATAEAI-------DADGWLHTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGAL---AEHPGVAQVAVI 269
|
330 340 350
....*....|....*....|....*....|....
gi 1917948728 987 GVPEEVLSAKGISLPDASDEVGLV---VIAELRD 1017
Cdd:cd17638 270 GVPDERMGEVGKAFVVARPGVTLTeedVIAWCRE 303
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
679-1064 |
1.92e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 94.29 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 679 LQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILfspLTFIRNPLM 758
Cdd:cd12118 138 LNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGW-CFPWTVAAVGGTNVC---LRKVDAKAI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 759 WlQTISDYKATH-SAGPnfafelVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpfGLSqevMAPGYG 837
Cdd:cd12118 214 Y-DLIEKHKVTHfCGAP------TVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL----GFD---VTHVYG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 838 LAEncvfvscAYGkkkPILV-DWQ---------------GRICCGYVDPNDADVdiriVDADTGLEVDEDGKE-GEIWIS 900
Cdd:cd12118 280 LTE-------TYG---PATVcAWKpewdelpteerarlkARQGVRYVGLEEVDV----LDPETMKPVPRDGKTiGEIVFR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 901 SPSAGIGYWGKEELSQKTFRNklqnypgrKYTRTGDLGwVIQ--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELL 978
Cdd:cd12118 346 GNIVMKGYLKNPEATAEAFRG--------GWFHSGDLA-VIHpdGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 979 RpgcCAVIGVPEEVLsakgislpdasdevGLVVIA--ELRDSKLVN-KDIIKQIESRVAeehgvtvasvKLIRPRTIS-- 1053
Cdd:cd12118 417 E---AAVVARPDEKW--------------GEVPCAfvELKEGAKVTeEEIIAFCREHLA----------GFMVPKTVVfg 469
|
410
....*....|....
gi 1917948728 1054 ---KTTSGKIKRFE 1064
Cdd:cd12118 470 elpKTSTGKIQKFV 483
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
674-1081 |
2.29e-19 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 95.07 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 674 DDLCFLqFTSGSTSDAKGVMITHGGliHNVKL---MRRRYRSTSNTVLvsWLPQyhDMGLIGG----LFTAMACGGSAIL 746
Cdd:cd05967 231 DPLYIL-YTSGTTGKPKGVVRDNGG--HAVALnwsMRNIYGIKPGDVW--WAAS--DVGWVVGhsyiVYGPLLHGATTVL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 747 FSPL-TFIRNPLMWLQTISDYKATH--SAgPNfAFElVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKrFVE--L 821
Cdd:cd05967 304 YEGKpVGTPDPGAFWRVIEKYQVNAlfTA-PT-AIR-AIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLE-WAEntL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 822 TRPfglsqeVM------APGYGLAENCVFVSCaygkkKPILVDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEG 895
Cdd:cd05967 380 GVP------VIdhwwqtETGWPITANPVGLEP-----LPIKAGSPGKPVPGY--------QVQVLDED-GEPV-GPNELG 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 896 EIWIS---SPSAGIGYWGKEELSQKTFrnkLQNYPGrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTV 971
Cdd:cd05967 439 NIVIKlplPPGCLLTLWKNDERFKKLY---LSKFPG--YYDTGDAGYKDEdGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 972 essseLLRPGC--CAVIGVPEEVlsaKGislpdaSDEVGLVVIAElrDSKLVNKDIIKQIESRVAEEHGvTVASVKL-IR 1048
Cdd:cd05967 514 -----LSHPAVaeCAVVGVRDEL---KG------QVPLGLVVLKE--GVKITAEELEKELVALVREQIG-PVAAFRLvIF 576
|
410 420 430
....*....|....*....|....*....|...
gi 1917948728 1049 PRTISKTTSGKIKRfECLKQFVDGNLNTVPDPI 1081
Cdd:cd05967 577 VKRLPKTRSGKILR-RTLRKIADGEDYTIPSTI 608
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
526-1064 |
2.41e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.52 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltSRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIpipVLPPDPLQRGGQALTKIENIAkLC 605
Cdd:PLN02574 68 SYSELQPLVKSMAAGL--YHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI---VTTMNPSSSLGEIKKRVVDCS-VG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTVGYHAAVRAG--LVKNLISFTGKSVkstgQWPNLPWLhtdsWIKSSKVLPASNIafqsesQPDDLCFLQFTS 683
Cdd:PLN02574 142 LAFTSPENVEKLSPLGVPviGVPENYDFDSKRI----EFPKFYEL----IKEDFDFVPKPVI------KQDDVAAIMYSS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRR------RYRSTSNTVLVSwLPQYHDMGLigGLF-TAMACGGSAILFSPlTFIRNP 756
Cdd:PLN02574 208 GTTGASKGVVLTHRNLIAMVELFVRfeasqyEYPGSDNVYLAA-LPMFHIYGL--SLFvVGLLSLGSTIVVMR-RFDASD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 757 LmwLQTISDYKATHsagpnfaFELVIRRLEADKAKARNY---DLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQevma 833
Cdd:PLN02574 284 M--VKVIDRFKVTH-------FPVVPPILMALTKKAKGVcgeVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQ---- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 834 pGYGLAENCVFVSCAYGKKKpilvdWQGRICCGYVDPNdadVDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEE 913
Cdd:PLN02574 351 -GYGMTESTAVGTRGFNTEK-----LSKYSSVGLLAPN---MQAKVVDWSTGCLL-PPGNCGELWIQGPGVMKGYLNNPK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 914 LSQKTFRNKlqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEv 992
Cdd:PLN02574 421 ATQSTIDKD-------GWLRTGDIAYFDEdGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIID---AAVTAVPDK- 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 993 lsakgislpdASDEVGLVVIAELRDSKLVNKDIIKQIESRVAEEHGVTvasvKLIRPRTISKTTSGKIKRFE 1064
Cdd:PLN02574 490 ----------ECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVR----KVVFVQSIPKSPAGKILRRE 547
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
662-1062 |
6.24e-19 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 93.12 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 662 ASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNV--KLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMA 739
Cdd:PLN02330 172 AGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcsSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 740 CGGSAILFSPLTfirnplmwLQTISDYKATHSAGPNFAFELVIRRLEADKAkARNYDLSSMIF--FMIAAEPVRQKTLKR 817
Cdd:PLN02330 252 NKGKVVVMSRFE--------LRTFLNALITQEVSFAPIVPPIILNLVKNPI-VEEFDLSKLKLqaIMTAAAPLAPELLTA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 818 FvELTRPFGLSQEvmapGYGLAE-NCVFVSCAYGKKKpilvdwQG---RICCGYVDPNdadVDIRIVDADTGLEVDEDgK 893
Cdd:PLN02330 323 F-EAKFPGVQVQE----AYGLTEhSCITLTHGDPEKG------HGiakKNSVGFILPN---LEVKFIDPDTGRSLPKN-T 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 894 EGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVe 972
Cdd:PLN02330 388 PGELCVRSQCVMQGYYNNKEETDRTIDED-------GWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELEAIL- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 973 ssseLLRPGC--CAVIGVPEEvlsaKGISLPDASdevglVVIAelRDSKLVNKDIIKQIESRVAeeHGVTVASVKLIrpR 1050
Cdd:PLN02330 460 ----LTHPSVedAAVVPLPDE----EAGEIPAAC-----VVIN--PKAKESEEDILNFVAANVA--HYKKVRVVQFV--D 520
|
410
....*....|..
gi 1917948728 1051 TISKTTSGKIKR 1062
Cdd:PLN02330 521 SIPKSLSGKIMR 532
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
522-1063 |
7.79e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 92.90 E-value: 7.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppDPLQRGGQaltkIENI 601
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHAL---AAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI---NTALRGPQ----LEHI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 602 AKLCNAVAILSTVGYHAAVRAGLVKNLisftgkSVKSTGQWPNLPWLHTDSWIKSSKVLPASNIAFQSESQPDDLCFLQF 681
Cdd:PRK06155 114 LRNSGARLLVVEAALLAALEAADPGDL------PLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDTAAILY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAIL---FSPLTFirnplm 758
Cdd:PRK06155 188 TSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLeprFSASGF------ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 759 WlqtisDYKATHSAGPNFAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPvrqktlKRFVELTRPFGLSqevMAPGYGL 838
Cdd:PRK06155 261 W-----PAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPA------ALHAAFRERFGVD---LLDGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 839 AENCVFVSCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEGEIWISS--PSA-GIGYWGKEELS 915
Cdd:PRK06155 327 TETNFVIAVTHGSQRP---GSMGRLAPGF--------EARVVDEH-DQEL-PDGEPGELLLRAdePFAfATGYFGMPEKT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 916 QKTFRNkLQNYPGRKYTRTGDlgwviqGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsa 995
Cdd:PRK06155 394 VEAWRN-LWFHTGDRVVRDAD------GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA---AAVFPVPSEL--- 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728 996 kgislpdASDEVGLVVIaeLRDSKLVN-KDIIKQIESRVAeehgvtvasvKLIRPRTIS------KTTSGKIKRF 1063
Cdd:PRK06155 461 -------GEDEVMAAVV--LRDGTALEpVALVRHCEPRLA----------YFAVPRYVEfvaalpKTENGKVQKF 516
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
690-989 |
8.97e-19 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 90.02 E-value: 8.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 690 KGVMITHGGLIH-NVKLMRRrYRSTSNTVLVSWLPQYHdmglIGGLFTAMAC---GGSAILFSPLtfirNPLMWLQTISD 765
Cdd:cd17637 16 RGAVLSHGNLIAaNLQLIHA-MGLTEADVYLNMLPLFH----IAGLNLALATfhaGGANVVMEKF----DPAEALELIEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 766 YKATHSagpnFAFELVIRRLEaDKAKARNYDLSSM--IFFMIAAEpvrqkTLKRFVELTRPFGLSqevmapGYGLAENCV 843
Cdd:cd17637 87 EKVTLM----GSFPPILSNLL-DAAEKSGVDLSSLrhVLGLDAPE-----TIQRFEETTGATFWS------LYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 844 FVSCAYGKKKPilvdwqGriCCGYVDPNdadVDIRIVDaDTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNkl 923
Cdd:cd17637 151 LVTLSPYRERP------G--SAGRPGPL---VRVRIVD-DNDRPV-PAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 924 qnypgrKYTRTGDLGWV-IQGNLFITGRI--KDLIIVAGRNIYSADVEKTVessseLLRPGCCA--VIGVP 989
Cdd:cd17637 216 ------GWHHTGDLGRFdEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVI-----LEHPAIAEvcVIGVP 275
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
673-1063 |
1.15e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 92.42 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSpltf 752
Cdd:PRK13295 196 PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD---- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 753 IRNPLMWLQTISDYKATHSAGPN-FAFELvirrleADKAKARNYDLSSMIFFMIAAEPVRQKTLKRfveLTRPFGLSqev 831
Cdd:PRK13295 272 IWDPARAAELIRTEGVTFTMASTpFLTDL------TRAVKESGRPVSSLRTFLCAGAPIPGALVER---ARAALGAK--- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 832 MAPGYGLAENCVFVSCAYGK--KKPILVDwqgriccGYVDPNdadVDIRIVDADtGLEVDEdGKEGEIWISSPSAGIGYW 909
Cdd:PRK13295 340 IVSAWGMTENGAVTLTKLDDpdERASTTD-------GCPLPG---VEVRVVDAD-GAPLPA-GQIGRLQVRGCSNFGGYL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 910 GKEELSQKTFRNklqnypgrkYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGV 988
Cdd:PRK13295 408 KRPQLNGTDADG---------WFDTGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQ---VAIVAY 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728 989 PEEVLS--AKGISLPDASDEVGLVVIAELRDSKLVNKDIIKQiesrvaeehgvtvasvKLIRPRTISKTTSGKIKRF 1063
Cdd:PRK13295 476 PDERLGerACAFVVPRPGQSLDFEEMVEFLKAQKVAKQYIPE----------------RLVVRDALPRTPSGKIQKF 536
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
524-968 |
1.57e-18 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 91.62 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAK 603
Cdd:cd17655 22 TLTYRELNERANQLARTL---REKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER-------IQYILE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 604 LCNAVAILSTvgyhaavraGLVKNLISFTGKSVKSTGQwpnlpwlhtDSWIKSSKVLPAsniafqsESQPDDLCFLQFTS 683
Cdd:cd17655 92 DSGADILLTQ---------SHLQPPIAFIGLIDLLDED---------TIYHEESENLEP-------VSKSDDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILfSPLTFIRNPLMWLQTI 763
Cdd:cd17655 147 GSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDAS-VTEIFASLLSGNTLYI-VRKETVLDGQALTQYI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 764 SDYKATHSAGPNFAFELVirrleadkAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpFGLSQEVMApGYGLAENCv 843
Cdd:cd17655 225 RQNRITIIDLTPAHLKLL--------DAADDSEGLSLKHLIVGGEALSTELAKKIIEL---FGTNPTITN-AYGPTETT- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 844 fVSCAYGKKKPiLVDWQGRICCGyvdpnDADVDIRIVDADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFrnkL 923
Cdd:cd17655 292 -VDASIYQYEP-ETDQQVSVPIG-----KPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKF---V 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1917948728 924 QN--YPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17655 362 DDpfVPGERMYRTGDLArWLPDGNIEFLGRIDHQVKIRGYRIELGEIE 409
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
519-1062 |
2.21e-18 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 91.20 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 519 GAVGCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRakvipipvlppdplqRGGQALT-- 596
Cdd:PLN02246 45 GATGRVYTYADVELLSRRVAAGL---HKLGIRQGDVVMLLLPNCPEFVLAFLGASR---------------RGAVTTTan 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 597 ------KIENIAKLCNAVAILSTVGYhaavrAGLVKNLISFTGKSVKSTGQwpnlpwlHTDSWIKSSKVLPASNIAF-QS 669
Cdd:PLN02246 107 pfytpaEIAKQAKASGAKLIITQSCY-----VDKLKGLAEDDGVTVVTIDD-------PPEGCLHFSELTQADENELpEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLM----RRRYRSTSNTVLVSWLPQYHdmglIGGLFTAMACG---G 742
Cdd:PLN02246 175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQvdgeNPNLYFHSDDVILCVLPMFH----IYSLNSVLLCGlrvG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 743 SAILFSPlTFIRNPLMWLqtISDYKAThsAGPnFAFELVIrrleadkAKARN-----YDLSSMIFFMIAAEPVRQktlkr 817
Cdd:PLN02246 251 AAILIMP-KFEIGALLEL--IQRHKVT--IAP-FVPPIVL-------AIAKSpvvekYDLSSIRMVLSGAAPLGK----- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 818 fvELTRPFG--LSQEVMAPGYGLAE-NCVFVSCAYGKKKPILVDwQGriCCGYVDPNdadVDIRIVDADTGLEVDEdGKE 894
Cdd:PLN02246 313 --ELEDAFRakLPNAVLGQGYGMTEaGPVLAMCLAFAKEPFPVK-SG--SCGTVVRN---AELKIVDPETGASLPR-NQP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 895 GEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQGN-LFITGRIKDLIIVAGRNIYSADVEKTVES 973
Cdd:PLN02246 384 GEICIRGPQIMKGYLNDPEATANTIDKD-------GWLHTGDIGYIDDDDeLFIVDRLKELIKYKGFQVAPAELEALLIS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 974 SSELLRpgcCAVIGVPEEVLSakgiSLPdasdeVGLVVIAElrDSKlVNKDIIKQIesrVAEEhgvtVASVKLIRP---- 1049
Cdd:PLN02246 457 HPSIAD---AAVVPMKDEVAG----EVP-----VAFVVRSN--GSE-ITEDEIKQF---VAKQ----VVFYKRIHKvffv 514
|
570
....*....|...
gi 1917948728 1050 RTISKTTSGKIKR 1062
Cdd:PLN02246 515 DSIPKAPSGKILR 527
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
526-1063 |
5.18e-18 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 89.46 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTsrKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPdpLQRGgqALTKIenIAKLC 605
Cdd:cd05958 12 TYRDLLALANRIANVLVG--ELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPL--LRPK--ELAYI--LDKAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafQSESQPDDLCFLQFTSGS 685
Cdd:cd05958 84 ITVALCA-------------------------------------------------------HALTASDDICILAFTSGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHggliHNVKLMRRRY-----RSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTfirnPLMWL 760
Cdd:cd05958 109 TGAPKATMHFH----RDPLASADRYavnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEAT----PDLLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 761 QTISDYKATHSAGPNFAFelvirRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTrpfGLsqEVMaPGYGLAE 840
Cdd:cd05958 181 SAIARYKPTVLFTAPTAY-----RAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT---GI--PII-DGIGSTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 841 NC-VFVSCAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVdEDGKEGEIWISSPSagiGYWGKEELSQKTF 919
Cdd:cd05958 250 MFhIFISARPGDARP---GATGKPVPGY--------EAKVVDDE-GNPV-PDGTIGRLAVRGPT---GCRYLADKRQRTY 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 920 RNKLQNYPGRKYTRTGDlgwviqGNLFITGRIKDLIIVAGRNIYSADVEKTVessseLLRPGC--CAVIGVPeevlsakg 997
Cdd:cd05958 314 VQGGWNITGDTYSRDPD------GYFRHQGRSDDMIVSGGYNIAPPEVEDVL-----LQHPAVaeCAVVGHP-------- 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728 998 islpdasDEVGLVVIAE---LRDSKLVNKDIIKQIESRVAEEhgvtVASVKliRPRTIS------KTTSGKIKRF 1063
Cdd:cd05958 375 -------DESRGVVVKAfvvLRPGVIPGPVLARELQDHAKAH----IAPYK--YPRAIEfvtelpRTATGKLQRF 436
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
674-1064 |
7.45e-18 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 88.93 E-value: 7.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 674 DDLCFLQFTSGSTSDAKGVMITH---------GGLIHNVKlMRRRYRSTSNTvlvSWLpqyhdMGLIGGLFTAMACGGSA 744
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHsyplghiptAAYWLGLR-PDDIHWNIADP---GWA-----KGAWSSFFGPWLLGATV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 745 ILFSPLTFirNPLMWLQTISDYKATHSAGPNFAFELVIRRLEAdkakarNYDLSSMIFFMIAAEPVRQKTLKRFVEltrP 824
Cdd:cd05972 152 FVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS------SYKFSHLRLVVSAGEPLNPEVIEWWRA---A 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 825 FGLSqevMAPGYGLAENCVFVS-CAYGKKKPilvDWQGRICCGYvdpndadvDIRIVDADtGLEVDEdGKEGEIWISSPS 903
Cdd:cd05972 221 TGLP---IRDGYGQTETGLTVGnFPDMPVKP---GSMGRPTPGY--------DVAIIDDD-GRELPP-GEEGDIAIKLPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 904 AGI--GYWGKEELSQKTFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR- 979
Cdd:cd05972 285 PGLflGYVGDPEKTEASIRG--------DYYLTGDRAYRDEdGYFWFVGRADDIIKSSGYRIGPFEVE------SALLEh 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 980 PGC--CAVIGVPEEVlsaKGiSLPDAsdevgLVVIA--ELRDSKLVnKDIIKQIESRVAEEhgvtvASVKLIR-PRTISK 1054
Cdd:cd05972 351 PAVaeAAVVGSPDPV---RG-EVVKA-----FVVLTsgYEPSEELA-EELQGHVKKVLAPY-----KYPREIEfVEELPK 415
|
410
....*....|
gi 1917948728 1055 TTSGKIKRFE 1064
Cdd:cd05972 416 TISGKIRRVE 425
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
660-1068 |
1.53e-17 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 87.40 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 660 LPASNIAFQ---SESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFT 736
Cdd:cd05912 60 LTPNELAFQlkdSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFH----ISGLSI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 737 AMAcggSAILFSPLTFIR--NPLMWLQTISDYKATH-SAGPNfafelVIRRLEADKAKARNYDLSSMiffMIAAEPVRQK 813
Cdd:cd05912 136 LMR---SVIYGMTVYLVDkfDAEQVLHLINSGKVTIiSVVPT-----MLQRLLEILGEGYPNNLRCI---LLGGGPAPKP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 814 TLKRFVELTRPFGLSqevmapgYGLAENC---VFVSCAYGKKKPilvdwqgriccGYVDPNDADVDIRIVDADTGLEVDe 890
Cdd:cd05912 205 LLEQCKEKGIPVYQS-------YGMTETCsqiVTLSPEDALNKI-----------GSAGKPLFPVELKIEDDGQPPYEV- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 891 dgkeGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEK 969
Cdd:cd05912 266 ----GEILLKGPNVTKGYLNRPDATEESFENG--------WFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 970 TVESssellRPGC--CAVIGVPEevlsakgislpdasDEVGLVVIAELRDSKLVNKD-IIKQIESRVAeehgvtvasvKL 1046
Cdd:cd05912 334 VLLS-----HPAIkeAGVVGIPD--------------DKWGQVPVAFVVSERPISEEeLIAYCSEKLA----------KY 384
|
410 420
....*....|....*....|....*...
gi 1917948728 1047 IRPRTI------SKTTSGKIKRFEcLKQ 1068
Cdd:cd05912 385 KVPKKIyfvdelPRTASGKLLRHE-LKQ 411
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
666-992 |
1.58e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 88.71 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 666 AFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGlftAMAC--GGS 743
Cdd:PRK08315 191 ARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLG---NLACvtHGA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 744 AILFSPLTFirNPLMWLQTISDYKATHSAG-----------PNFAfelvirrleadkakarNYDLSSMIFFMIAAEPVRQ 812
Cdd:PRK08315 268 TMVYPGEGF--DPLATLAAVEEERCTALYGvptmfiaeldhPDFA----------------RFDLSSLRTGIMAGSPCPI 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 813 KTLKRFVELtrpFGLSQEVMApgYGLAEnCVFVSCAYGKKKPIL--VDWQGRiccgyVDPNdadVDIRIVDADTGLEVdE 890
Cdd:PRK08315 330 EVMKRVIDK---MHMSEVTIA--YGMTE-TSPVSTQTRTDDPLEkrVTTVGR-----ALPH---LEVKIVDPETGETV-P 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 891 DGKEGEIWISSPSAGIGYWGKEElsqKTfrnklqnypgRK------YTRTGDLGwVI--QGNLFITGRIKDLIIVAGRNI 962
Cdd:PRK08315 395 RGEQGELCTRGYSVMKGYWNDPE---KT----------AEaidadgWMHTGDLA-VMdeEGYVNIVGRIKDMIIRGGENI 460
|
330 340 350
....*....|....*....|....*....|....*....
gi 1917948728 963 YSADVEktvesssELLR--PGC--CAVIGVP-----EEV 992
Cdd:PRK08315 461 YPREIE-------EFLYthPKIqdVQVVGVPdekygEEV 492
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
670-1062 |
3.14e-17 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 87.03 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFtAMACGGSAILFSP 749
Cdd:cd17640 84 ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF-IFACGCSQAYTSI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 750 LTFirnplmwLQTISDYKATHSAGpnfafelVIRRLEAdkakarnydLSSMIFFMIAAEP-VRQKTLKRFVELTR-PFGL 827
Cdd:cd17640 163 RTL-------KDDLKRVKPHYIVS-------VPRLWES---------LYSGIQKQVSKSSpIKQFLFLFFLSGGIfKFGI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 828 SQE-VMAP---------------GYGLAENCVFVSCayGKKKPILVDWQGRICcgyvdpndADVDIRIVDADTGlEVDED 891
Cdd:cd17640 220 SGGgALPPhvdtffeaigievlnGYGLTETSPVVSA--RRLKCNVRGSVGRPL--------PGTEIKIVDPEGN-VVLPP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 892 GKEGEIWISSPSAGIGYWGKEE-----LSQKTFRNklqnypgrkytrTGDLGW-VIQGNLFITGRIKDLIIVA-GRNIYS 964
Cdd:cd17640 289 GEKGIVWVRGPQVMKGYYKNPEatskvLDSDGWFN------------TGDLGWlTCGGELVLTGRAKDTIVLSnGENVEP 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 965 ADVEKTVEsSSELLRPgcCAVIG----------VP-----EEVLSAKGISLPdaSDEVGLvvIAELRDSKLVNKDIIKQI 1029
Cdd:cd17640 357 QPIEEALM-RSPFIEQ--IMVVGqdqkrlgaliVPnfeelEKWAKESGVKLA--NDRSQL--LASKKVLKLYKNEIKDEI 429
|
410 420 430
....*....|....*....|....*....|....*.
gi 1917948728 1030 ESRVAEEHGVTVASVKLIRPRTISK---TTSGKIKR 1062
Cdd:cd17640 430 SNRPGFKSFEQIAPFALLEEPFIENgemTQTMKIKR 465
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
526-1035 |
3.68e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 87.22 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLtsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPL--QRGGQALTKIEN 600
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLI--YELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLnirLTENELifQLKDSGTTVLFV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 601 IAKLCNAVAILSTVGYhaavraglVKNLISFTGksvkstgqwpnlpwlhtdswIKSSKVLPASNIAFQSESQPDDLCFlq 680
Cdd:PRK06839 107 EKTFQNMALSMQKVSY--------VQRVISITS--------------------LKEIEDRKIDNFVEKNESASFIICY-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 681 fTSGSTSDAKGVMITHGGL----IHNVKLMRRryrsTSNTVLVSWLPQYHDMGLigGLFT--AMACGGSAILfsPLTFir 754
Cdd:PRK06839 157 -TSGTTGKPKGAVLTQENMfwnaLNNTFAIDL----TMHDRSIVLLPLFHIGGI--GLFAfpTLFAGGVIIV--PRKF-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 755 NPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKAkarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGlsqevmaP 834
Cdd:PRK06839 226 EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETT-----NLQSVRWFYNGGAPCPEELMREFIDRGFLFG-------Q 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 GYGLAENC--VF-VSCAYGKKKPILVDWQGRICcgyvdpndadvDIRIVDADTGlEVdEDGKEGEIWISSPSAGIGYWGK 911
Cdd:PRK06839 294 GFGMTETSptVFmLSEEDARRKVGSIGKPVLFC-----------DYELIDENKN-KV-EVGEVGELLIRGPNVMKEYWNR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 912 EELSQKTFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPE 990
Cdd:PRK06839 361 PDATEETIQD--------GWLCTGDLARVDEdGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYE---VAVVGRQH 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1917948728 991 EVLSakgislpdasdEVGLVVIAELRDSKLVNKDIIKQIESRVAE 1035
Cdd:PRK06839 430 VKWG-----------EIPIAFIVKKSSSVLIEKDVIEHCRLFLAK 463
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
501-1034 |
3.71e-17 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 87.30 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 501 AAQEITqnkalyTWINEGGAVgcQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFG--CLRAKVI 578
Cdd:cd12119 10 GDREIV------SRTHEGEVH--RYTYAEVAERARRLANAL---RRLGVKPGDRVATLAWNTHRHLELYYAvpGMGAVLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 579 PI-PVLPPdplqrggqaltkiENIAKLCNavailstvgyHAAVRAGLVKnlISFTGKSVKSTGQWPNLP-WLHTDSWIKS 656
Cdd:cd12119 79 TInPRLFP-------------EQIAYIIN----------HAEDRVVFVD--RDFLPLLEAIAPRLPTVEhVVVMTDDAAM 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 657 SKVLPASNIAFQS--ESQPDDL----------CFLQFTSGSTSDAKGVMITHGGLI-HNVKLMRR--RYRSTSNTVLVSw 721
Cdd:cd12119 134 PEPAGVGVLAYEEllAAESPEYdwpdfdentaAAICYTSGTTGNPKGVVYSHRSLVlHAMAALLTdgLGLSESDVVLPV- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 722 LPQYHDMGLigGL-FTAMACGGSAILFSPLTfirNPLMWLQTISDYKATHSAG-PnfafelVIRRLEADKAKARNYDLSS 799
Cdd:cd12119 213 VPMFHVNAW--GLpYAAAMVGAKLVLPGPYL---DPASLAELIEREGVTFAAGvP------TVWQGLLDHLEANGRDLSS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 800 MIFFMIAAEPVRQKTLKRFVELtrpfGLsqEVMApGYGLAENCVFVSCAYGKKK----PILVDW-----QGRICCGyvdp 870
Cdd:cd12119 282 LRRVVIGGSAVPRSLIEAFEER----GV--RVIH-AWGMTETSPLGTVARPPSEhsnlSEDEQLalrakQGRPVPG---- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 871 ndadVDIRIVDADTGlEVDEDGKE-GEIWISSPSAGIGYWGKEELSQKTFRNklqnypGrkYTRTGDLGwVI--QGNLFI 947
Cdd:cd12119 351 ----VELRIVDDDGR-ELPWDGKAvGELQVRGPWVTKSYYKNDEESEALTED------G--WLRTGDVA-TIdeDGYLTI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 948 TGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEvlsaKGISLPdasdeVGLVVIAElrDSKLVNKDIIK 1027
Cdd:cd12119 417 TDRSKDVIKSGGEWISSVELENAIMAHPAVAE---AAVIGVPHP----KWGERP-----LAVVVLKE--GATVTAEELLE 482
|
....*..
gi 1917948728 1028 QIESRVA 1034
Cdd:cd12119 483 FLADKVA 489
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
526-968 |
6.29e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 86.21 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd17643 14 TYGELDARANRLARTL---RAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER-------IAFILADS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQFTSGS 685
Cdd:cd17643 84 GPSLLLT-----------------------------------------------------------DPDDLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVlvsWLpQYHDMGL---IGGLFTAMACGGSAILFSPLTfIRNPLMWLQT 762
Cdd:cd17643 105 TGRPKGVVVSHANVLALFAATQRWFGFNEDDV---WT-LFHSYAFdfsVWEIWGALLHGGRLVVVPYEV-ARSPEDFARL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 763 ISDYKAT-HSAGPNfAFElviRRLEADKAKARNYDLSSMIFFmiAAEPVRQKTLKRFVEltrPFGLSQEVMAPGYGLAEN 841
Cdd:cd17643 180 LRDEGVTvLNQTPS-AFY---QLVEAADRDGRDPLALRYVIF--GGEALEAAMLRPWAG---RFGLDRPQLVNMYGITET 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 842 CVFVSCaygkkKPILVDwqgriccgYVDPNDA--------DVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEE 913
Cdd:cd17643 251 TVHVTF-----RPLDAA--------DLPAAAAspigrplpGLRVYVLDAD-GRPV-PPGVVGELYVSGAGVARGYLGRPE 315
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 914 LSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17643 316 LTAERFVANPFGGPGSRMYRTGDLArRLPDGELEYLGRADEQVKIRGFRIELGEIE 371
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
526-1060 |
6.64e-17 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 86.86 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLlVHVPGL-DFIDAFFGCLRAKVIPIPVLppdplqrGGQALTKIENIAKL 604
Cdd:cd17634 86 SYRELHREVCRFAGTL---LDLGVKKGDRVA-IYMPMIpEAAVAMLACARIGAVHSVIF-------GGFAPEAVAGRIID 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 605 CNAVAILSTVGYhaaVRAGLVKNLISFTGKS-------------VKSTG---QWPNLPWLHTDSWIKsskvlpASNIAFQ 668
Cdd:cd17634 155 SSSRLLITADGG---VRAGRSVPLKKNVDDAlnpnvtsvehvivLKRTGsdiDWQEGRDLWWRDLIA------KASPEHQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 669 SES-QPDDLCFLQFTSGSTSDAKGVMITHGGliHNVKL---MRRRYRSTSNTVlVSWlpqYHDMGLIGG----LFTAMAC 740
Cdd:cd17634 226 PEAmNAEDPLFILYTSGTTGKPKGVLHTTGG--YLVYAattMKYVFDYGPGDI-YWC---TADVGWVTGhsylLYGPLAC 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 741 GGSAILFSPLTFIRNPLMWLQTISDYKATHSagpnFAFELVIRRL--EADKAKARnYDLSSMIFFMIAAEPVRQKTLKRF 818
Cdd:cd17634 300 GATTLLYEGVPNWPTPARMWQVVDKHGVNIL----YTAPTAIRALmaAGDDAIEG-TDRSSLRILGSVGEPINPEAYEWY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 819 velTRPFGLSQEVMAPGYGLAENCVFVScaygkkkPILvdwQGRICCGYVDPNDADVDIRIVDADTGLEVDEDGKEGEIW 898
Cdd:cd17634 375 ---WKKIGKEKCPVVDTWWQTETGGFMI-------TPL---PGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 899 ISSPSAG--IGYWGKEELSQKTFRNKLQNYpgrkYTrTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 975
Cdd:cd17634 442 ITDPWPGqtRTLFGDHERFEQTYFSTFKGM----YF-SGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 976 ELLRpgcCAVIGVPEEVlsaKGISLpdasdeVGLVViaeLRDSKLVNKDIIKQIESRVAEEHGVTVASVKLIRPRTISKT 1055
Cdd:cd17634 517 KVAE---AAVVGIPHAI---KGQAP------YAYVV---LNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKT 581
|
....*
gi 1917948728 1056 TSGKI 1060
Cdd:cd17634 582 RSGKI 586
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
515-988 |
8.95e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 86.34 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 515 INEGGAVgcqrTYAELDSNASCVAHKLLtsrKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLP-------PDP 587
Cdd:PRK06164 30 IDEDRPL----SRAELRALVDRLAAWLA---AQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTryrshevAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 588 LQRGGQALTKIENIAKLCNAVAILSTVGYhaAVRAGLvKNLISFTGKSVKSTGQWP----NLPWLHtdswiksskvLPAS 663
Cdd:PRK06164 103 LGRGRARWLVVWPGFKGIDFAAILAAVPP--DALPPL-RAIAVVDDAADATPAPAPgarvQLFALP----------DPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 664 NIAFQSESQPDDLCFLQFT-SGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMAcGG 742
Cdd:PRK06164 170 PAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALA-GG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 743 SAILFSPlTFIRNPLmwLQTISDYKATHSAGPNFAFELVIRRL--EADKAKARNYDLSSmifFMIAAEPVRQKTLKRFVE 820
Cdd:PRK06164 248 APLVCEP-VFDAART--ARALRRHRVTHTFGNDEMLRRILDTAgeRADFPSARLFGFAS---FAPALGELAALARARGVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 821 LTRPFGlSQEVMApgyglaencvFVSCaygkkKPILVDWQGRICCGYVdPNDADVDIRIVDADTGlEVDEDGKEGEIWIS 900
Cdd:PRK06164 322 LTGLYG-SSEVQA----------LVAL-----QPATDPVSVRIEGGGR-PASPEARVRARDPQDG-ALLPDGESGEIEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 901 SPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWVIQGNLFI-TGRIKDLIIVAGRNIYSADVEKTVESssellR 979
Cdd:PRK06164 384 APSLMRGYLDNPDATARALTDD-------GYFRTGDLGYTRGDGQFVyQTRMGDSLRLGGFLVNPAEIEHALEA-----L 451
|
490
....*....|.
gi 1917948728 980 PGC--CAVIGV 988
Cdd:PRK06164 452 PGVaaAQVVGA 462
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
674-990 |
1.21e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 85.86 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 674 DDLCFLQFTSGSTSDAKGVMITHGGLIHNVkLMRRRYR---STSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPL 750
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNT-LMGVQWLyncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKF 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 TFirnpLMWLQTISDYKATHSAG-PNFAFELVIRRLeadkakARNYDLSSMIFFMIAAEPVRQKTLKRFVELTrpfglsQ 829
Cdd:PRK06710 285 DM----KMVFEAIKKHKVTLFPGaPTIYIALLNSPL------LKEYDISSIRACISGSAPLPVEVQEKFETVT------G 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 830 EVMAPGYGLAENCVFVSCAYgkkkpilvDWQGRIcCGYVDPNDADVDIRIVDADTGlEVDEDGKEGEIWISSPSAGIGYW 909
Cdd:PRK06710 349 GKLVEGYGLTESSPVTHSNF--------LWEKRV-PGSIGVPWPDTEAMIMSLETG-EALPPGEIGEIVVKGPQIMKGYW 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 910 GKEELSQKTFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGV 988
Cdd:PRK06710 419 NKPEETAAVLQD--------GWLHTGDVGYMDEdGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQE---VVTIGV 487
|
..
gi 1917948728 989 PE 990
Cdd:PRK06710 488 PD 489
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
526-1034 |
1.46e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 85.48 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPV----LPPDplqrggqaltkIEN 600
Cdd:PRK07470 34 TWREIDARVDALAAALAAR---GVRKGDRIL-VHSRnCNQMFESMFAAFRLGAVWVPTnfrqTPDE-----------VAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 601 IAKLCNAVAILSTVGYHAAVRAglvknlisftgksVKSTGqwpnlPWLHTDSWIKSSKV------LPASNIAFQSESQP- 673
Cdd:PRK07470 99 LAEASGARAMICHADFPEHAAA-------------VRAAS-----PDLTHVVAIGGARAgldyeaLVARHLGARVANAAv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 674 --DDLCFLQFTSGSTSDAKGVMITHGGLI-----HNVKLMRRryrSTSNTVLVSWLPQYHDMGlIGGLfTAMACGGSAIL 746
Cdd:PRK07470 161 dhDDPCWFFFTSGTTGRPKAAVLTHGQMAfvitnHLADLMPG---TTEQDASLVVAPLSHGAG-IHQL-CQVARGAATVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 747 -----FSPLTFirnplmWlQTISDYKATHSagpnFAFELVIRRLEADKAKARnYDLSSMIFFMIAAEPVRQKTLKRFVEL 821
Cdd:PRK07470 236 lpserFDPAEV------W-ALVERHRVTNL----FTVPTILKMLVEHPAVDR-YDHSSLRYVIYAGAPMYRADQKRALAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 822 TRPfglsqeVMAPGYGLAEncvfVSCAYGKKKPILVDW----QGRI-CCGYvdpndadvdirivdADTGLEV---DEDGK 893
Cdd:PRK07470 304 LGK------VLVQYFGLGE----VTGNITVLPPALHDAedgpDARIgTCGF--------------ERTGMEVqiqDDEGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 894 E------GEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSAD 966
Cdd:PRK07470 360 ElppgetGEICVIGPAVFAGYYNNPEANAKAFRDG--------WFRTGDLGHLdARGFLYITGRASDMYISGGSNVYPRE 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 967 VEKTVessseLLRPGC--CAVIGVPEEVLSakgislpdasdEVGLVVIAeLRDSKLVNKD-IIKQIESRVA 1034
Cdd:PRK07470 432 IEEKL-----LTHPAVseVAVLGVPDPVWG-----------EVGVAVCV-ARDGAPVDEAeLLAWLDGKVA 485
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
673-989 |
2.24e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 85.39 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILFSPLTF 752
Cdd:PRK07529 212 PDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 753 iRNP-LM---WlQTISDYKATH-SAGPNFAFELVIRRLEAdkakarnYDLSSMIFFMIAAEPVRQKTLKRFVELTrpfGL 827
Cdd:PRK07529 292 -RGPgVIanfW-KIVERYRINFlSGVPTVYAALLQVPVDG-------HDISSLRYALCGAAPLPVEVFRRFEAAT---GV 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 828 SqevMAPGYGLAENCVFVSCAY--GKKKP----ILVDWQgriccgyvdpndaDVDIRIVDADTGLEVD-EDGKEGEIWIS 900
Cdd:PRK07529 360 R---IVEGYGLTEATCVSSVNPpdGERRIgsvgLRLPYQ-------------RVRVVILDDAGRYLRDcAVDEVGVLCIA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 901 SPSAGIGYWGKEelsqktfrnklQN---YPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTvessse 976
Cdd:PRK07529 424 GPNVFSGYLEAA-----------HNkglWLEDGWLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIEEA------ 486
|
330
....*....|....*.
gi 1917948728 977 LLR-P--GCCAVIGVP 989
Cdd:PRK07529 487 LLRhPavALAAAVGRP 502
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
658-1031 |
4.01e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 85.36 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 658 KVLPASNI--AFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLF 735
Cdd:PRK08633 764 RLLPARLLkrLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLW 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 736 TAMACGGSAILFSpltfirNPLMWL---QTISDYKATHSAG-PNFaFELVIRRLEADKAkarnyDLSSMIFFMIAAEPVR 811
Cdd:PRK08633 844 LPLLEGIKVVYHP------DPTDALgiaKLVAKHRATILLGtPTF-LRLYLRNKKLHPL-----MFASLRLVVAGAEKLK 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 812 QKTLKRFVEltrPFGLsqEVMApGYGLAEncvfvsCAygkkkPIlvdwqgrICCGYVDPNDAD----------------- 874
Cdd:PRK08633 912 PEVADAFEE---KFGI--RILE-GYGATE------TS-----PV-------ASVNLPDVLAADfkrqtgskegsvgmplp 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 875 -VDIRIVDADTGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTfrnkLQNYPGRKYTRTGDLGWV-IQGNLFITGRIK 952
Cdd:PRK08633 968 gVAVRIVDPETFEEL-PPGEDGLILIGGPQVMKGYLGDPEKTAEV----IKDIDGIGWYVTGDKGHLdEDGFLTITDRYS 1042
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 953 DLIIVAGRNIYSADVEktvESSSELL--RPGCCAVIGVPEEvlsAKGISL-----PDASDEVGLV-VIAELRDSKLVNKD 1024
Cdd:PRK08633 1043 RFAKIGGEMVPLGAVE---EELAKALggEEVVFAVTAVPDE---KKGEKLvvlhtCGAEDVEELKrAIKESGLPNLWKPS 1116
|
....*..
gi 1917948728 1025 IIKQIES 1031
Cdd:PRK08633 1117 RYFKVEA 1123
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
26-92 |
2.16e-15 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 72.56 E-value: 2.16e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728 26 IVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKE 92
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDE 66
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
526-1070 |
2.60e-15 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 81.43 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSRkptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd05918 26 TYAELDRLSSRLAHHLRSLG---VGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQR-------LQEILQDT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqseSQPDDLCFLQFTSGS 685
Cdd:cd05918 96 GAKVVLT----------------------------------------------------------SSPSDAAYVIFTSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VL--------VSwlpqyhdmglIGGLFTAMACGGSaiLFSPLTFIR-N 755
Cdd:cd05918 118 TGKPKGVVIEHRALSTSALAHGRALGLTSESrVLqfasytfdVS----------ILEIFTTLAAGGC--LCIPSEEDRlN 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 756 PLmwLQTISDYKATHsagpnfAFeL---VIRRLEADkakarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRpfglsqeVM 832
Cdd:cd05918 186 DL--AGFINRLRVTW------AF-LtpsVARLLDPE-------DVPSLRTLVLGGEALTQSDVDTWADRVR-------LI 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 833 ApGYGLAENCVFVSCaygkkKPILVDWQGRI------CCGY-VDPNDADvdiRIVDAdtglevdedGKEGEIWISSPSAG 905
Cdd:cd05918 243 N-AYGPAECTIAATV-----SPVVPSTDPRNigrplgATCWvVDPDNHD---RLVPI---------GAVGELLIEGPILA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 906 IGYWGKEELSQKTF-------RNKLQNYPGRKYtRTGDLgwVIQ---GNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 975
Cdd:cd05918 305 RGYLNDPEKTAAAFiedpawlKQEGSGRGRRLY-RTGDL--VRYnpdGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSL 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 976 ELLRPgCCAVIGVPeevlsakgislPDASDEVGLVVIAELRDSKLVNKDiikqIESRVAEEHGVTVASVKLIRPR----- 1050
Cdd:cd05918 382 PGAKE-VVVEVVKP-----------KDGSSSPQLVAFVVLDGSSSGSGD----GDSLFLEPSDEFRALVAELRSKlrqrl 445
|
570 580 590
....*....|....*....|....*....|...
gi 1917948728 1051 -------------TISKTTSGKIKRfECLKQFV 1070
Cdd:cd05918 446 psymvpsvflplsHLPLTASGKIDR-RALRELA 477
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
660-968 |
4.23e-15 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 80.20 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 660 LPASNIAFQSE--------SQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYhDMGLI 731
Cdd:cd17650 71 YPAERLQYMLEdsgaklllTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASF-SFDVF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 732 GGLFTAMACGGSAILFSPLTFIRNPLMWLQTISDYKAThsagpnfAFELV---IRRLEADKAKaRNYDLSSMIFFMIAAE 808
Cdd:cd17650 150 AGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRIT-------LMESTpalIRPVMAYVYR-NGLDLSAMRLLIVGSD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 809 PVrqkTLKRFVELTRPFGLSQEVMApGYGLAENCVFVSCAYGKKKPILVdwQGRICCGYVDPNDAdvdIRIVDADtgLEV 888
Cdd:cd17650 222 GC---KAQDFKTLAARFGQGMRIIN-SYGVTEATIDSTYYEEGRDPLGD--SANVPIGRPLPNTA---MYVLDER--LQP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 889 DEDGKEGEIWISSPSAGIGYWGKEELSQKTF-RNKLQnyPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSAD 966
Cdd:cd17650 291 QPVGVAGELYIGGAGVARGYLNRPELTAERFvENPFA--PGERMYRTGDLArWRADGNVELLGRVDHQVKIRGFRIELGE 368
|
..
gi 1917948728 967 VE 968
Cdd:cd17650 369 IE 370
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
504-1064 |
5.10e-15 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 80.62 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 504 EITQNKALYTWINEGGaVGCQRTYAELdSNASCVAHKLLTSRKptIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPvl 583
Cdd:cd05970 28 KEYPDKLALVWCDDAG-EERIFTFAEL-ADYSDKTANFFKAMG--IGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 584 ppdplqrgGQALTKIENIAKLCNAVAILSTVgyhaAVRAGLVKNLISftgKSVKSTGQWPNLPWLH---TDSWIKSSKVL 660
Cdd:cd05970 102 --------ATHQLTAKDIVYRIESADIKMIV----AIAEDNIPEEIE---KAAPECPSKPKLVWVGdpvPEGWIDFRKLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 661 PASNIAFQ-----SESQPDDLCFLQFTSGSTSDAKgvMITH------GGLI-----HNVKLMRRRYrSTSNTvlvSWlpq 724
Cdd:cd05970 167 KNASPDFErptanSYPCGEDILLVYFSSGTTGMPK--MVEHdftyplGHIVtakywQNVREGGLHL-TVADT---GW--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 725 yhDMGLIGGLFTAMACGGSAILFSPLTFIrnPLMWLQTISDYKATHSAGPNFAFELVIRrleadkAKARNYDLSSMIFFM 804
Cdd:cd05970 238 --GKAVWGKIYGQWIAGAAVFVYDYDKFD--PKALLEKLSKYGVTTFCAPPTIYRFLIR------EDLSRYDLSSLRYCT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 805 IAAEPVRQKTLKRFVELTrpfGLSqevMAPGYGLAENCVFVSCAYG-KKKPILVdwqGRICCGYvdpndadvDIRIVDAD 883
Cdd:cd05970 308 TAGEALNPEVFNTFKEKT---GIK---LMEGFGQTETTLTIATFPWmEPKPGSM---GKPAPGY--------EIDLIDRE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 884 tGLEVdEDGKEGEIWISSpSAGI------GYWGKEELSQKTFRNklqnypgrKYTRTGDLGWVIQ-GNLFITGRIKDLII 956
Cdd:cd05970 371 -GRSC-EAGEEGEIVIRT-SKGKpvglfgGYYKDAEKTAEVWHD--------GYYHTGDAAWMDEdGYLWFVGRTDDLIK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 957 VAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVLsakgislpdasdevGLVVIAELrdskLVNKD------IIKQIE 1030
Cdd:cd05970 440 SSGYRIGPFEVESALIQHPAVLE---CAVTGVPDPIR--------------GQVVKATI----VLAKGyepseeLKKELQ 498
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1917948728 1031 SRVAEehgVTvASVKLirPRTIS------KTTSGKIKRFE 1064
Cdd:cd05970 499 DHVKK---VT-APYKY--PRIVEfvdelpKTISGKIRRVE 532
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
677-992 |
5.72e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 78.50 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 677 CFLQFTSGSTSDAKGVMITHGGLI-HNVKLMRRRyRSTSNTVLVSWLPQYHdmglIGGLFTAMA---CGGSAIlfspltF 752
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQALLaQALVLAVLQ-AIDEGTVFLNSGPLFH----IGTLMFTLAtfhAGGTNV------F 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 753 IR--NPLMWLQTISDYKATHS--AGPNFAfelVIRRLEADkakaRNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLS 828
Cdd:cd17636 72 VRrvDAEEVLELIEAERCTHAflLPPTID---QIVELNAD----GLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGGYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 829 Q-EVMapgyGLAencvfVSCAYGKKkpilvdwqGRICCGYVDPNdadVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIG 907
Cdd:cd17636 145 QtEVM----GLA-----TFAALGGG--------AIGGAGRPSPL---VQVRILDED-GREV-PDGEVGEIVARGPTVMAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 908 YWGKEELSQKTFRNklqnypgrKYTRTGDLGW-VIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESssellRPGC--CA 984
Cdd:cd17636 203 YWNRPEVNARRTRG--------GWHHTNDLGRrEPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-----HPAVadAA 269
|
....*...
gi 1917948728 985 VIGVPEEV 992
Cdd:cd17636 270 VIGVPDPR 277
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
525-1017 |
9.04e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 79.56 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 525 RTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDplqrggqaltKIENI 601
Cdd:PRK08276 12 VTYGELEARSNRLAHGL---RALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPInwhLTAA----------EIAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 602 AKLCNAVAILSTVGYhAAVRAGLVKNLISftGKSVKSTGQWPNLPWLHTDSWIKSSkvlPASNIAFQSESQPddlcfLQF 681
Cdd:PRK08276 79 VDDSGAKVLIVSAAL-ADTAAELAAELPA--GVPLLLVVAGPVPGFRSYEEALAAQ---PDTPIADETAGAD-----MLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 682 TSGSTSDAKGVM-------ITHGGLIHNVKLMRRRYRSTSNTVLVSwLPQYHDMGLIGGLfTAMACGGSAIL---FSPLT 751
Cdd:PRK08276 148 SSGTTGRPKGIKrplpgldPDEAPGMMLALLGFGMYGGPDSVYLSP-APLYHTAPLRFGM-SALALGGTVVVmekFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 752 FirnplmwLQTISDYKATHSagpnfafELV----IRRLE-ADKAKARnYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfg 826
Cdd:PRK08276 226 A-------LALIERYRVTHS-------QLVptmfVRMLKlPEEVRAR-YDVSSLRVAIHAAAPCPVEVKRAMIDWWGP-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 827 lsqeVMAPGYGLAENC--VFVSCAYGKKKPILVD--WQGRIccgyvdpndadvdiRIVDADtGLEVDEdGKEGEIWISSP 902
Cdd:PRK08276 289 ----IIHEYYASSEGGgvTVITSEDWLAHPGSVGkaVLGEV--------------RILDED-GNELPP-GEIGTVYFEMD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 903 SAGIGYWGKEElsqKTfrnkLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-P 980
Cdd:PRK08276 349 GYPFEYHNDPE---KT----AAARNPHGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIE------NLLVThP 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1917948728 981 GC--CAVIGVP-----EEVlsaKGISLP----DASDEVGLVVIAELRD 1017
Cdd:PRK08276 416 KVadVAVFGVPdeemgERV---KAVVQPadgaDAGDALAAELIAWLRG 460
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
661-990 |
1.19e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 79.16 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 661 PASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLihnvklmrrRYRSTSNTVLVSwLPQYHDMGLIGGLFTAMAC 740
Cdd:PRK06145 136 GGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNL---------HWKSIDHVIALG-LTASERLLVVGPLYHVGAF 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 741 G--GSAILF--SPLTFIRN--PLMWLQTISDYKAThsaGPNFAFELVIRRL---EADKakarnYDLSSMIFFMIAAEPVR 811
Cdd:PRK06145 206 DlpGIAVLWvgGTLRIHREfdPEAVLAAIERHRLT---CAWMAPVMLSRVLtvpDRDR-----FDLDSLAWCIGGGEKTP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 812 QKTLKRFVELTRpfglsQEVMAPGYGLAENCVFVSCAYGKKKPILVDWQGRICcgyvdpndADVDIRIVDADTGLEvdED 891
Cdd:PRK06145 278 ESRIRDFTRVFT-----RARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRAL--------AHVEIRIADGAGRWL--PP 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 892 GKEGEIWISSPSAGIGYWGKEELSQKTFRNklqnypgrKYTRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PRK06145 343 NMKGEICMRGPKVTKGYWKDPEKTAEAFYG--------DWFRSGDVGYLDeEGFLYLTDRKKDMIISGGENIASSEVERV 414
|
330 340
....*....|....*....|
gi 1917948728 971 VESSSELLRpgcCAVIGVPE 990
Cdd:PRK06145 415 IYELPEVAE---AAVIGVHD 431
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
497-1062 |
1.36e-14 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 79.46 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 497 LKHWAAQEITQnkALYTWINEGGAVGcQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAK 576
Cdd:cd05968 67 LDKWLADTRTR--PALRWEGEDGTSR-TLTYGELLYEVKRLANGL---RALGVGKGDRVGIYLPMIPEIVPAFLAVARIG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 577 VIPIPVLP---PDPlqrggqALTKIENiaklCNAVAILSTVGYhaaVRAGLVKNLISFTGKSVKST-----------GQW 642
Cdd:cd05968 141 GIVVPIFSgfgKEA------AATRLQD----AEAKALITADGF---TRRGREVNLKEEADKACAQCptvekvvvvrhLGN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 643 PNLPWLHTDSWIKSSKvlpASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWL 722
Cdd:cd05968 208 DFTPAKGRDLSYDEEK---ETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 723 PqyhDMGLIGG---LFTAMACGGSAILFSPLTFIRNPLMWLQTISDYKATH-SAGPNfafelVIRRLEA-DKAKARNYDL 797
Cdd:cd05968 285 T---DLGWMMGpwlIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHlGLSPT-----LIRALKPrGDAPVNAHDL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 798 SSMIFFMIAAEPVRQKTLKRFVELTrpfglsqevmapgygLAENCVFVSCAYGkkkpilVDWQGRICCGYV----DPNDA 873
Cdd:cd05968 357 SSLRVLGSTGEPWNPEPWNWLFETV---------------GKGRNPIINYSGG------TEISGGILGNVLikpiKPSSF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 874 DVDIRIVDADTgleVDEDGK-----EGEIWISSPSAGI--GYWGKEELSQKTFRNKLQNypgrKYTRtGDLGWV-IQGNL 945
Cdd:cd05968 416 NGPVPGMKADV---LDESGKparpeVGELVLLAPWPGMtrGFWRDEDRYLETYWSRFDN----VWVH-GDFAYYdEEGYF 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 946 FITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVlsaKGislpdaSDEVGLVViaeLRDSKLVNKDI 1025
Cdd:cd05968 488 YILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE---SAAIGVPHPV---KG------EAIVCFVV---LKPGVTPTEAL 552
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1917948728 1026 IKQIESRVAEEHGvtvasvKLIRPRTI------SKTTSGKIKR 1062
Cdd:cd05968 553 AEELMERVADELG------KPLSPERIlfvkdlPKTRNAKVMR 589
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
524-988 |
1.49e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 78.66 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIEniak 603
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAY---GIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 604 lcnavailstvgyhaavraglvknlisftgksvkstgqwPNlpwlhtdswiksskvlpasniAFQSESQPDDLCFLQFTS 683
Cdd:cd05910 75 ---------------------------------------PD---------------------AFIGIPKADEPAAILFTS 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYhdmgligGLFTAmACGGSAIL--FSPLTFIR-NPLMWL 760
Cdd:cd05910 95 GSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGP-ALGLTSVIpdMDPTRPARaDPQKLV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 761 QTISDYKATHSAGPNFAFELVIRRLEADKAKarnydLSSMIFFMIAAEPVRQKTLKRFVELTRPfglSQEVMAPgYGLAE 840
Cdd:cd05910 167 GAIRQYGVSIVFGSPALLERVARYCAQHGIT-----LPSLRRVLSAGAPVPIALAARLRKMLSD---EAEILTP-YGATE 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 841 N---CVFVSCAYGKKKPILVDWQGRICCGY-VDPNDADV----DIRIVDADTGLEVDeDGKEGEIWISSPSAGIGYWGKE 912
Cdd:cd05910 238 AlpvSSIGSRELLATTTAATSGGAGTCVGRpIPGVRVRIieidDEPIAEWDDTLELP-RGEIGEITVTGPTVTPTYVNRP 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728 913 elsQKTFRNKLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGV 988
Cdd:cd05910 317 ---VATALAKIDDNSEGFWHRMGDLGYLdDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRR---SALVGV 387
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
675-1062 |
2.39e-14 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 76.60 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 675 DLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHdmglIGGLFTAMACggsAILFSPLTFIR 754
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYH----VGGLAILVRS---LLAGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 755 NPLMWLQTISDYKATHSAgpnfafeLV---IRRLEADKAKARNYDLSSMIFfmIAAEPVRQKTLKRFVELTRPfglsqev 831
Cdd:cd17630 74 RNQALAEDLAPPGVTHVS-------LVptqLQRLLDSGQGPAALKSLRAVL--LGGAPIPPELLERAADRGIP------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 832 MAPGYGLAEncvFVSCAYGKKkpilvdwQGRICCGYVDPNDADVDIRIVDadtglevdedgkEGEIWISSPSAGIGYWGK 911
Cdd:cd17630 138 LYTTYGMTE---TASQVATKR-------PDGFGRGGVGVLLPGRELRIVE------------DGEIWVGGASLAMGYLRG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 912 EELSQktfrnklqnYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPE 990
Cdd:cd17630 196 QLVPE---------FNEDGWFTTKDLGeLHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD---AFVVGVPD 263
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 991 EVLSAKgislpdasdevgLVVIAELRDSKLVnkdiiKQIESRVAEEHGVTVASVKLIRPRTISKTTSGKIKR 1062
Cdd:cd17630 264 EELGQR------------PVAVIVGRGPADP-----AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDR 318
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
526-1002 |
4.49e-14 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 77.21 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd17645 25 TYKQLNEKANQLARHL---RGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER-------IAYMLADS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQFTSGS 685
Cdd:cd17645 95 SAKILLT-----------------------------------------------------------NPDDLAYVIYTSGS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHnvklmrrryrstsntvLVSWlpqYHDMgligglFTAMACGGSAIlFSPLTFIRNPLMWLQTISD 765
Cdd:cd17645 116 TGLPKGVMIEHHNLVN----------------LCEW---HRPY------FGVTPADKSLV-YASFSFDASAWEIFPHLTA 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 766 YKATHSAGPNfafelviRRLEADKAKARNYDLSSMIFFMI--AAEPVRQ-------------KTLKRFVEltRPFGLSQe 830
Cdd:cd17645 170 GAALHVVPSE-------RRLDLDALNDYFNQEGITISFLPtgAAEQFMQldnqslrvlltggDKLKKIER--KGYKLVN- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 831 vmapGYGLAENCVFVSCAYgkkkpilvdwqgriccgyVDPNDADVDI-------RIVDADTGLEVDEDGKEGEIWISSPS 903
Cdd:cd17645 240 ----NYGPTENTVVATSFE------------------IDKPYANIPIgkpidntRVYILDEALQLQPIGVAGELCIAGEG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 904 AGIGYWGKEELSQKTFRNKLQnYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELL---- 978
Cdd:cd17645 298 LARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAkFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIElaav 376
|
490 500 510
....*....|....*....|....*....|....*..
gi 1917948728 979 --------RPGCCAVIGVPEEVLSAK-----GISLPD 1002
Cdd:cd17645 377 lakedadgRKYLVAYVTAPEEIPHEElrewlKNDLPD 413
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
19-264 |
4.85e-14 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 76.88 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 19 PLDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEI--EGKVYDLGGQVLAANSaPVIFHLAKESGTE 96
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSH-TNLLALARELGLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 97 LEEM-DLHKLALIDsFTGEYHDIN-VAEDYMSLVSLTLEIQDKAKDSnhIGIHAVSDIASDLTP--AYLEAHGIKSVPKS 172
Cdd:COG1231 83 LEPFpNENGNALLY-LGGKRVRAGeIAADLRGVAELLAKLLRALAAA--LDPWAHPAAELDRESlaEWLRRNGASPSARR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 173 VQYGYTASGYG-------FVQDMPYAYIHEFtrtsmAGKIRRMKGGYMSLWKKISKSLLIKVCCNTEVQAVRRDGSDVNV 245
Cdd:COG1231 160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQDGDGVTV 234
|
250
....*....|....*....
gi 1917948728 246 DITNssGETEHkeFDKIII 264
Cdd:COG1231 235 TTDD--GGTVR--ADAVIV 249
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
520-1062 |
4.85e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 77.15 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 520 AVGCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPdplqrggqalT 596
Cdd:PRK09088 18 ALGRRWTYAELDALVGRLAAVL---RRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnwrLSA----------S 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 597 KIENIAKLCNAVAILSTvgyhAAVRAGlvknlisftgksvkstgqwpNLPWLHTDSWIKSSKvlpASNIAFQSESQPDDL 676
Cdd:PRK09088 85 ELDALLQDAEPRLLLGD----DAVAAG--------------------RTDVEDLAAFIASAD---ALEPADTPSIPPERV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 677 CFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSaILFSPLTFIRNP 756
Cdd:PRK09088 138 SLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGS-ILVSNGFEPKRT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 757 LMWLQTiSDYKATHSAG-PNFAFELvirRLEADKAKARnydLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqevMAPG 835
Cdd:PRK09088 217 LGRLGD-PALGITHYFCvPQMAQAF---RAQPGFDAAA---LRHLTALFTGGAPHAAEDILGWLDDGIP-------MVDG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 836 YGLAE-NCVF---VSCAYGKKKpilvdwqgricCGYVDPNDADVDIRIVDADtglevDED---GKEGEIWISSPSAGIGY 908
Cdd:PRK09088 283 FGMSEaGTVFgmsVDCDVIRAK-----------AGAAGIPTPTVQTRVVDDQ-----GNDcpaGVPGELLLRGPNLSPGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 909 WGKEELSQKTFrnklqnyPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIG 987
Cdd:PRK09088 347 WRRPQATARAF-------TGDGWFRTGDIARRdADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRE---CAVVG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 988 VpeevlsakgislPDAS-DEVGLVVIAELRDSKLVNKDIIKQIESRVAE----EHGVTVASVklirPRtiskTTSGKIKR 1062
Cdd:PRK09088 417 M------------ADAQwGEVGYLAIVPADGAPLDLERIRSHLSTRLAKykvpKHLRLVDAL----PR----TASGKLQK 476
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
526-968 |
7.49e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 76.56 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd12116 14 SYAELDERANRLAARL---RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR-------LRYILEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTvgyhAAVRAGLVKNLisftgksvkstgqwpnlpwlhtDSWIKSSKVLPASNIAFQSESQPDDLCFLQFTSGS 685
Cdd:cd12116 84 EPALVLTD----DALPDRLPAGL----------------------PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIgGLFTAMACGGSAILFSPLTfIRNPLMWLQTISD 765
Cdd:cd12116 138 TGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGARVVIAPRET-QRDPEALARLIEA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 766 YKATHsagpnfafelvirrLEADKAKARnydlssmifFMIAAEPVRQKTLKRFV---ELtrPFGLSQEVMAPG------Y 836
Cdd:cd12116 216 HSITV--------------MQATPATWR---------MLLDAGWQGRAGLTALCggeAL--PPDLAARLLSRVgslwnlY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 837 GLAENCVfvscaygkkkpilvdWQgriCCGYVDPNDADVDI-------RIVDADTGLEVDEDGKEGEIWISSPSAGIGYW 909
Cdd:cd12116 271 GPTETTI---------------WS---TAARVTAAAGPIPIgrplantQVYVLDAALRPVPPGVPGELYIGGDGVAQGYL 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 910 GKEELSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd12116 333 GRPALTAERFVPDPFAGPGSRLYRTGDLVrRRADGRLEYLGRADGQVKIRGHRIELGEIE 392
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
22-94 |
9.47e-14 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 76.02 E-value: 9.47e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728 22 TRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESG 94
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
675-1062 |
1.26e-13 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 74.36 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 675 DLCFLQFTSGSTSDAKGVMITHGGLIH----NVKLMrrrYRSTSNTVLVSWlPQYHDMGLIGGLFtAMACGGSAILFSPL 750
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIEsfvcNEDLF---NISGEDAILAPG-PLSHSLFLYGAIS-ALYLGGTFIGQRKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 tfirNPLMWLQTISDYKAThsagpnfAFELVIRRLEAdKAKARNYDLSSMIFFMIAA--EPVRQKTLKRfveltrpfGLS 828
Cdd:cd17633 76 ----NPKSWIRKINQYNAT-------VIYLVPTMLQA-LARTLEPESKIKSIFSSGQklFESTKKKLKN--------IFP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 829 QEVMAPGYGLAE-NCVFVSCAYGKKKPILVdwqGRICcgyvdPNdadVDIRIVDADtglevdeDGKEGEIWISSPSAGIG 907
Cdd:cd17633 136 KANLIEFYGTSElSFITYNFNQESRPPNSV---GRPF-----PN---VEIEIRNAD-------GGEIGKIFVKSEMVFSG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 908 YWgKEELSQKTfrnklqnypgrKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGccaVI 986
Cdd:cd17633 198 YV-RGGFSNPD-----------GWMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAI---VV 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 987 GVPEEVLSAKGislpdasdeVGLVVIAELRDSKLvnKDIIKQIESRvaEEhgvtVASvKLIRPRTISKTTSGKIKR 1062
Cdd:cd17633 263 GIPDARFGEIA---------VALYSGDKLTYKQL--KRFLKQKLSR--YE----IPK-KIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
522-968 |
1.41e-13 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 75.48 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 522 GCQRTYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkieni 601
Cdd:cd17649 10 DQSLSYAELDARANRLAHRL---RALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 602 aklcnavailstvgyhaavraglvknlisftgksvkstgqwpnLPWLHTDSWIKSskVLPAsniafqsesQPDDLCFLQF 681
Cdd:cd17649 76 -------------------------------------------LRYMLEDSGAGL--LLTH---------HPRQLAYVIY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMACGGSAILfspltfiRNPLMWLQ 761
Cdd:cd17649 102 TSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFD-GAHEQLLPPLICGACVVL-------RPDELWAS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 762 TISDYKATHSAG-------PNFAFELVirrLEADKAKARNYdlSSMIFFMIAAEPVRQKTLKRF----VELTRPFGLSQE 830
Cdd:cd17649 174 ADELAEMVRELGvtvldlpPAYLQQLA---EEADRTGDGRP--PSLRLYIFGGEALSPELLRRWlkapVRLFNAYGPTEA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 831 VMAPgygLAENCVFVSCAYGKKKPIlvdwqGRICCGYVdpndadvdIRIVDADTGLEvdEDGKEGEIWISSPSAGIGYWG 910
Cdd:cd17649 249 TVTP---LVWKCEAGAARAGASMPI-----GRPLGGRS--------AYILDADLNPV--PVGVTGELYIGGEGLARGYLG 310
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 911 KEELSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17649 311 RPELTAERFVPDPFGAPGSRLYRTGDLArWRDDGVIEYLGRVDHQVKIRGFRIELGEIE 369
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
526-968 |
2.08e-13 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 75.39 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHkLLTSRkpTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKL 604
Cdd:cd17646 25 TYRELDERANRLAH-LLRAR--GVGPEDRVA-VLLPrSADLVVALLAVLKAGAAYLPLDPGYPADR-------LAYMLAD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 605 CNAVAILSTVGYHAAVRAGLVKNLISFTG-KSVKSTGQWPnlpwlhtdswiksskvlpasniafqsESQPDDLCFLQFTS 683
Cdd:cd17646 94 AGPAVVLTTADLAARLPAGGDVALLGDEAlAAPPATPPLV--------------------------PPRPDNLAYVIYTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTFiRNPLMWLQTI 763
Cdd:cd17646 148 GSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVARPGGH-RDPAYLAALI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 764 SDYKAThsagpnfAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRpfglsqevmAP---GYGLAE 840
Cdd:cd17646 226 REHGVT-------TCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPG---------AElhnLYGPTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 841 NCVFVScaYGKKKPilVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFR 920
Cdd:cd17646 290 AAIDVT--HWPVRG--PAETPSVPIGRPVPN---TRLYVLDDA--LRPVPVGVPGELYLGGVQLARGYLGRPALTAERFV 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1917948728 921 NKLQNYPGRKYtRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17646 361 PDPFGPGSRMY-RTGDLArWRPDGALEFLGRSDDQVKIRGFRVEPGEIE 408
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
669-1011 |
9.06e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 73.31 E-value: 9.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 669 SESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGL-IGGLFTAMAcgGSAILF 747
Cdd:PRK06334 178 SDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLS--GVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 S--PLtfirNPLMWLQTISDYKATHSAGPNFAFELVIRrleadKAKARNYDLSSMIFFMIAAE----PVRQKTLKRFVEL 821
Cdd:PRK06334 256 AynPL----YPKKIVEMIDEAKVTFLGSTPVFFDYILK-----TAKKQESCLPSLRFVVIGGDafkdSLYQEALKTFPHI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 822 TrpfgLSQevmapGYGLAEnCVFVSCAYGKKKPilvdwQGRICCGYvdPNDAdVDIRIVDADTGLEVdEDGKEGEIWISS 901
Cdd:PRK06334 327 Q----LRQ-----GYGTTE-CSPVITINTVNSP-----KHESCVGM--PIRG-MDVLIVSEETKVPV-SSGETGLVLTRG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 902 PSAGIGYWGKEelsqktFRNKLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIysadvekTVESSSELLRP 980
Cdd:PRK06334 388 TSLFSGYLGED------FGQGFVELGGETWYVTGDLGYVdRHGELFLKGRLSRFVKIGAEMV-------SLEALESILME 454
|
330 340 350
....*....|....*....|....*....|.
gi 1917948728 981 GCcavigvpeevlsakgiSLPDASDEVGLVV 1011
Cdd:PRK06334 455 GF----------------GQNAADHAGPLVV 469
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
526-1018 |
1.94e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 72.42 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppdplqrgGQALTKIENIAKLC 605
Cdd:PRK13391 26 TYRELDERSNRLAHLF---RSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV---------NSHLTPAEAAYIVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVA-ILSTVGYHAAVRAGLVKNLISFTGKSV-KSTGQWPnlPWLHTDSWIKSskvLPASNIAFQSESQPddlcfLQFTS 683
Cdd:PRK13391 94 DSGArALITSAAKLDVARALLKQCPGVRHRLVlDGDGELE--GFVGYAEAVAG---LPATPIADESLGTD-----MLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVM--ITHGGLIHNVKL---MRRRYRSTSNTVLVSWLPQYHDmgliGGLFTAM---ACGGSAIL---FSPLTF 752
Cdd:PRK13391 164 GTTGRPKGIKrpLPEQPPDTPLPLtafLQRLWGFRSDMVYLSPAPLYHS----APQRAVMlviRLGGTVIVmehFDAEQY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 753 irnplmwLQTISDYKATHSagpNFAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVM 832
Cdd:PRK13391 240 -------LALIEEYGVTHT---QLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGP------II 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 833 APGYGLAENCVFVSCAYGK--KKPILVdwqGRICCGyvdpndadvDIRIVDaDTGLEVDEdGKEGEIWIsspsagigywg 910
Cdd:PRK13391 304 HEYYAATEGLGFTACDSEEwlAHPGTV---GRAMFG---------DLHILD-DDGAELPP-GEPGTIWF----------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 911 KEELSQKTF----RNKLQNYPGRKYTRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAV 985
Cdd:PRK13391 359 EGGRPFEYLndpaKTAEARHPDGTWSTVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVAD---AAV 435
|
490 500 510
....*....|....*....|....*....|....*....
gi 1917948728 986 IGVPEEVL--SAKGISLP----DASDEVGLVVIAELRDS 1018
Cdd:PRK13391 436 FGVPNEDLgeEVKAVVQPvdgvDPGPALAAELIAFCRQR 474
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
640-992 |
2.34e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 72.02 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 640 GQWPNLPWLHTDSWIKSSKVLPASNIAFQ-SESQPDDLCFLQFTSGSTSDAKGVMITHGGL-IHNVKLMRRRYRSTSNTV 717
Cdd:PRK07867 117 GLDPGVRVINVDSPAWADELAAHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVMLAQRFGLGPDDVC 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 718 LVSwLPQYHDMGLIGGLFTAMACGGSAIL---FSPLTFirnplmwLQTISDYKATHSagpnfafelvirrleadkakarN 794
Cdd:PRK07867 197 YVS-MPLFHSNAVMAGWAVALAAGASIALrrkFSASGF-------LPDVRRYGATYA----------------------N 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 795 Y---DLSsmifFMIAAEPV---RQKTLK-------------RFVeltRPFGLsqeVMAPGYGLAENCVFVSCAYGKKKPI 855
Cdd:PRK07867 247 YvgkPLS----YVLATPERpddADNPLRivygnegapgdiaRFA---RRFGC---VVVDGFGSTEGGVAITRTPDTPPGA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 856 LvdwqGRiccgyvdpndADVDIRIVDADTGLEV-----DEDGKE------GEIW-ISSPSAGIGYWGKEELSQKTFRNkl 923
Cdd:PRK07867 317 L----GP----------LPPGVAIVDPDTGTECppaedADGRLLnadeaiGELVnTAGPGGFEGYYNDPEADAERMRG-- 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917948728 924 qnypGRKYtrTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEKTvessseLLR-PGC--CAVIGVPEEV 992
Cdd:PRK07867 381 ----GVYW--SGDLAYRdADGYAYFAGRLGDWMRVDGENLGTAPIERI------LLRyPDAteVAVYAVPDPV 441
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
526-951 |
3.52e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 71.46 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSRKPTIKPgdrvLLVHvPGLDF--IDAFFGCLRAKVIPIPVLPPDPLQRggqaLTKIENIAK 603
Cdd:PRK04813 29 TYGQLKEDSDALAAFIDSLKLPDKSP----IIVF-GHMSPemLATFLGAVKAGHAYIPVDVSSPAER----IEMIIEVAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 604 lcnAVAILSTVGyhaavraglvknlISFTGKSVKstgqwpnlpwLHTDSWIKSSKVLPASnIAFQSESQPDDLCFLQFTS 683
Cdd:PRK04813 100 ---PSLIIATEE-------------LPLEILGIP----------VITLDELKDIFATGNP-YDFDHAVKGDDNYYIIFTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGgLFTAMACGGSaiLFS-PLTFIRNPLMWLQT 762
Cdd:PRK04813 153 GTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMD-LYPTLASGGT--LVAlPKDMTANFKQLFET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 763 ISDYK-ATHSAGPNFA-FELVIRRLEADKakarnydLSSMIFFMIAAE--PVR--QKTLKRFveltrPfglsQEVMAPGY 836
Cdd:PRK04813 230 LPQLPiNVWVSTPSFAdMCLLDPSFNEEH-------LPNLTHFLFCGEelPHKtaKKLLERF-----P----SATIYNTY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 837 GLAENCVFVS--------CAYGKKKPIlvdwqgriccGYVDPndaDVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGY 908
Cdd:PRK04813 294 GPTEATVAVTsieitdemLDQYKRLPI----------GYAKP---DSPLLIIDEE--GTKLPDGEQGEIVISGPSVSKGY 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1917948728 909 WGKEELSQKTF--RNKLQNYpgrkytRTGDLGWVIQGNLFITGRI 951
Cdd:PRK04813 359 LNNPEKTAEAFftFDGQPAY------HTGDAGYLEDGLLFYQGRI 397
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
1757-1993 |
3.87e-12 |
|
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin.
Pssm-ID: 163708 Cd Length: 305 Bit Score: 69.60 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1757 KGYLKLYDDiqgLPEH---DIFGPGKRYTVIVRHSNSLSADDDARL-DARGAALRIL---------SDDSPLLDLTLKTG 1823
Cdd:cd08152 16 KAEFTVLDD---LPPElaqGLFAEPGTYPAVIRFSNAPGDILDDSVpDPRGMAIKVLgvpgekllpEEDATTQDFVLVNH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1824 KAFYARTISDFA--TWLVCGLAAREEHVKRVPH----VRDAVWTSLRQADSFADLH-----------YYSNTCrlFRFKD 1886
Cdd:cd08152 93 PVFFARDAKDYLalLKLLARTTSLPDGAKAALSaplrGALRVLEAAGGESPTLKLGghppahplgetYWSQAP--YRFGD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1887 RqemYVKFKLRPSDENIEEdigkvepsgiLPPETGAIPRDANDTRPLL--FLAEDfhnrvkspsGVRYIFQLQVRpipQD 1964
Cdd:cd08152 171 Y---VAKYSVVPASPALPA----------LTGKELDLTDDPDALREALadFLAEN---------DAEFEFRIQLC---TD 225
|
250 260
....*....|....*....|....*....
gi 1917948728 1965 EAARDIAlDCTKPWDESQFPYIDVGEVII 1993
Cdd:cd08152 226 LEKMPIE-DASVEWPEALSPFVPVATITI 253
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
670-993 |
4.60e-12 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 70.87 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 670 ESQPDDLcflQFTSGSTSDAKGVMITH-GGLIHNVKLMRRRYRS--TSNTVLVSWLPQYHDMGLIGgLFTAMACGGSAIL 746
Cdd:cd05929 124 EAAGWKM---LYSGGTTGRPKGIKRGLpGGPPDNDTLMAAALGFgpGADSVYLSPAPLYHAAPFRW-SMTALFMGGTLVL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 747 ---FSPLTFirnplmwLQTISDYKATHSagpNFAFELVIRRLEADKAKARNYDLSSMIFFMIAAEP----VRQKTLKrfv 819
Cdd:cd05929 200 mekFDPEEF-------LRLIERYRVTFA---QFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPcppwVKEQWID--- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 820 eltrpfgLSQEVMAPGYGLAEnCVFVSCAYGKkkpilvDWQ------GRICCGyvdpndadvDIRIVDADtGLEVdEDGK 893
Cdd:cd05929 267 -------WGGPIIWEYYGGTE-GQGLTIINGE------EWLthpgsvGRAVLG---------KVHILDED-GNEV-PPGE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 894 EGEIWISsPSAGIGY-----WGKEELSQKTFRNklqnypgrkytrTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADV 967
Cdd:cd05929 322 IGEVYFA-NGPGFEYtndpeKTAAARNEGGWST------------LGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEI 388
|
330 340
....*....|....*....|....*.
gi 1917948728 968 EKTVESSSELLRpgcCAVIGVPEEVL 993
Cdd:cd05929 389 ENALIAHPKVLD---AAVVGVPDEEL 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
874-1068 |
5.31e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 70.76 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 874 DVDIRIVDadtGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLGWV-IQGNLFITGRIK 952
Cdd:PRK03640 315 PCELKIEK---DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG--------WFKTGDIGYLdEEGFLYVLDRRS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 953 DLIIVAGRNIYSADVEKTVESSSELLRPGccaVIGVPEEVLsakgislpdasdevGLVVIAELRDSKLVNKDIIKQIesr 1032
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAEAG---VVGVPDDKW--------------GQVPVAFVVKSGEVTEEELRHF--- 443
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1917948728 1033 vAEEHgvtVASVKliRPRTI------SKTTSGKIKRFEcLKQ 1068
Cdd:PRK03640 444 -CEEK---LAKYK--VPKRFyfveelPRNASGKLLRHE-LKQ 478
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
670-955 |
5.94e-12 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 70.71 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRS--TSNTVLVSWLPQYHDMGLIgGLFTAMACGGsAILF 747
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPEllGPDDRYLAYLPLAHIFELA-AENVCLYRGG-TIGY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 -SPLTFI----RNPlmwLQTISDYKATHSAGPNFAFELVIRRLEAD------------------KAKARNYDLSSMIFFM 804
Cdd:cd17639 162 gSPRTLTdkskRGC---KGDLTEFKPTLMVGVPAIWDTIRKGVLAKlnpmgglkrtlfwtayqsKLKALKEGPGTPLLDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 805 IAAEPVRQKT-----------------LKRFVE-LTRPfglsqevMAPGYGLAEncvfvSCAYGkkkPILVDWQGRICCg 866
Cdd:cd17639 239 LVFKKVRAALggrlrymlsggaplsadTQEFLNiVLCP-------VIQGYGLTE-----TCAGG---TVQDPGDLETGR- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 867 yVDPNDADVDIRIVD-ADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRnklqnypGRKYTRTGDLG-WVIQGN 944
Cdd:cd17639 303 -VGPPLPCCEIKLVDwEEGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFD-------GDGWFHTGDIGeFHPDGT 374
|
330
....*....|.
gi 1917948728 945 LFITGRIKDLI 955
Cdd:cd17639 375 LKIIDRKKDLV 385
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
681-991 |
8.73e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 70.11 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 681 FTSGSTSDAKGVM---ITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMAcGGSAIL---FSPLTFir 754
Cdd:PRK12406 159 YTSGTTGHPKGVRraaPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRL-GGVLVLqprFDPEEL-- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 755 nplmwLQTISDYKATHSAGPNFAFelvIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPfglsqeVMAP 834
Cdd:PRK12406 236 -----LQLIERHRITHMHMVPTMF---IRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGP------VIYE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 GYGLAENCVFVSCAYGK--KKPILVdwqGRICCGyvdpndadVDIRIVDADtGLEVdEDGKEGEIWISSPS-AGIGYWGK 911
Cdd:PRK12406 302 YYGSTESGAVTFATSEDalSHPGTV---GKAAPG--------AELRFVDED-GRPL-PQGEIGEIYSRIAGnPDFTYHNK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 912 EELSQKTFRNKLqnypgrkyTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvessSELLR-PGC--CAVIG 987
Cdd:PRK12406 369 PEKRAEIDRGGF--------ITSGDVGYLDAdGYLFLCDRKRDMVISGGVNIYPAEIE------AVLHAvPGVhdCAVFG 434
|
....
gi 1917948728 988 VPEE 991
Cdd:PRK12406 435 IPDA 438
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
673-1062 |
9.81e-12 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 70.19 E-value: 9.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYH-------DMG-LIGGLFTAMAcgGSA 744
Cdd:cd05932 136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHvtervfvEGGsLYGGVLVAFA--ESL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 745 ILF-------SPLTFIRNPLMWLQTisdYKATHSAGPNFAFEL-----VIRRLEADKAkARNYDLSSMIFFMIAAEPVRQ 812
Cdd:cd05932 214 DTFvedvqraRPTLFFSVPRLWTKF---QQGVQDKIPQQKLNLllkipVVNSLVKRKV-LKGLGLDQCRLAGCGSAPVPP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 813 KTLkrfvELTRPFGLSqevMAPGYGLAENCvfvscAYGkkkpiLVDWQGRICCGYVDPNDADVDIRIVDadtglevdedg 892
Cdd:cd05932 290 ALL----EWYRSLGLN---ILEAYGMTENF-----AYS-----HLNYPGRDKIGTVGNAGPGVEVRISE----------- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 893 kEGEIWISSPSAGIGYWGKEELSQKTFrnklqNYPGrkYTRTGDLGWV-IQGNLFITGRIKDLIIVA-GRNIYSADVEKT 970
Cdd:cd05932 342 -DGEILVRSPALMMGYYKDPEATAEAF-----TADG--FLRTGDKGELdADGNLTITGRVKDIFKTSkGKYVAPAPIENK 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 971 VESSSellRPGCCAVIG------VPEEVLSAKGISLPDASDEvglvviAELRDSKlvnKDIIKQIESRVaEEHGVTVASV 1044
Cdd:cd05932 414 LAEHD---RVEMVCVIGsglpapLALVVLSEEARLRADAFAR------AELEASL---RAHLARVNSTL-DSHEQLAGIV 480
|
410 420
....*....|....*....|.
gi 1917948728 1045 KLIRPRTISK---TTSGKIKR 1062
Cdd:cd05932 481 VVKDPWSIDNgilTPTLKIKR 501
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
673-1064 |
1.56e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 69.44 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHN--VKLMRRRYrsTSNTVLVSWLPQYHdmglIGGLFTAMA---CGGSAILF 747
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQslAKIAIVGY--GEDDVYLHTAPLCH----IGGLSSALAmlmVGACHVLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 spltfirnplmwlqtisdykathsagPNFAFELVIRRLEadkakarNYDLSSMIFF--MIA--AEPVRQK-TLKRFVELT 822
Cdd:PLN02860 245 --------------------------PKFDAKAALQAIK-------QHNVTSMITVpaMMAdlISLTRKSmTWKVFPSVR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 823 RPF----GLSQEVMA------------PGYGLAENC---VFVS-------------CAYGKKKPILVDWQGRICCGYVDP 870
Cdd:PLN02860 292 KILngggSLSSRLLPdakklfpnaklfSAYGMTEACsslTFMTlhdptlespkqtlQTVNQTKSSSVHQPQGVCVGKPAP 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 871 NdadVDIRIvdadtglEVDEDGKEGEIWISSPSAGIGYWG--KEELSQKTFRNKLQnypgrkytrTGDLGWVIQ-GNLFI 947
Cdd:PLN02860 372 H---VELKI-------GLDESSRVGRILTRGPHVMLGYWGqnSETASVLSNDGWLD---------TGDIGWIDKaGNLWL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 948 TGRIKDLIIVAGRNIYSADVEKTVessseLLRPGC--CAVIGVPEEVLSAKgislpdasdevglvVIAELR--------D 1017
Cdd:PLN02860 433 IGRSNDRIKTGGENVYPEEVEAVL-----SQHPGVasVVVVGVPDSRLTEM--------------VVACVRlrdgwiwsD 493
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 1018 SKLVNKDIIKQIESRVAEEH-------GVTVASVKLIRPRTISKTTSGKIKRFE 1064
Cdd:PLN02860 494 NEKENAKKNLTLSSETLRHHcreknlsRFKIPKLFVQWRKPFPLTTTGKIRRDE 547
|
|
| NRPS_term_dom |
TIGR02353 |
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
1569-2302 |
1.88e-11 |
|
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.
Pssm-ID: 274093 [Multi-domain] Cd Length: 695 Bit Score: 69.39 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1569 THIKTWFGHQLAIACHVRFaklLSGTEAFCMYLRLLGAKVGRYCSIRAINP-IADprMVSIGAGVHLGDFSrIITGFYSQ 1647
Cdd:TIGR02353 79 TYLRFWTVKRLVDAAPTVL---LSGSPLYSLYLRALGAKIGKGVDIGSLPPvCTD--LLTIGAGTIVRKEV-MLLGYRAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1648 SGYIQ-GNVDIKDNSVTGSQSLILPGSVVEKDVILGAISVAPVNSVLQSGGVYMGSQSpvmvkNTIHALDDRIEEMDPky 1726
Cdd:TIGR02353 153 RGRLHtGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPA-----QKTGADYRKVQPARP-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1727 kkivgnlaanlaattlkVKSRYFHRIGVSGKGYLKLYDDIQGLPEHDIFgpgkryTVIVRHSNSLsadddarldarGAAL 1806
Cdd:TIGR02353 226 -----------------YTVRRRLYVAGALFVVFVLLPPLAFLFAIPVA------ITFDEIDWTL-----------GPDM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1807 RILSDdspLLDLTLKTGKAFYARTI-SDFATWLVCGLAAREEHVKRVPHVRDAVWT-SLRQADSFADLHYYSNTcrlfrf 1884
Cdd:TIGR02353 272 VGFIL---ALVLTFVALAGFIAYTVlLLAAVRLLLNLVLKPGRYYVHSGFYYQAWTvQQLMDNSRVLLFPLYAS------ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1885 kdrqeMYVKFKLRpsdeNIEEDIGKVEPSGilpPETGAIPrDANDTRPLLFLAED--FHNRVKSPSGVRyIFQLQVRP-- 1960
Cdd:TIGR02353 343 -----SYIPHWYR----ALGAKIGKVAEIS---SAQHEVP-DLTDIGEETFIADGllMGNARLSGGWFR-LGRTRIGRrs 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1961 -------IPQDEAARDIALDCTKpwdeSQFPyIDvGEViiNENLTKEGSEKLEVNpflRCHEVDviratsssqsasiDHG 2033
Cdd:TIGR02353 409 flgnsgyYPPGAKTGDNVLLGVL----SMTP-KD-GKV--REGVGWLGSPPFELP---RRVNRD-------------DEL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2034 RSLIYEicqhlrngdplPEAWRVFLeqsdvkvdlsgcpmaaaleRKDTEKVTLSRPWYLTTWAVFAQPL---LQTIVPYF 2110
Cdd:TIGR02353 465 EALTFE-----------PDPRRRLA-------------------RKNVENLRIILPFLLVQWAMLFALVvldLQALDDYT 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2111 LLGLIIyFPLNLLLhcknarnmpvhwtfpffwVSTGILAALTCAAAKYILVGKKKEDETVhIWSRGVFM-DTIWQAIRTV 2189
Cdd:TIGR02353 515 EWGAVA-LLAALIL------------------MAVGVGAFLILVERKWLVFGRLKPQEHP-LWSPFVWLhELHWKLYESV 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2190 FGDYFVEMTSGSALFLMWMKLMGssVELDKGTYVDSmgaALNPE--MVEVEGGGSVEREALLFGHVYdgEGGAVKFGKIV 2267
Cdd:TIGR02353 575 AVPNFLRPFRGTPFLPAILRLLG--VKIGRGVYIDG---TDLTErdLVTIGDDSTLNEGSVIQTHLF--EDRVMKSDTVT 647
|
730 740 750
....*....|....*....|....*....|....*..
gi 1917948728 2268 VGEGGFVGSRAVAMPGVESGGS--LSALSLAMKGEAI 2302
Cdd:TIGR02353 648 IGDGATLGPGAIVLYGVVMGEGsvLGPDSLVMKGEEV 684
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
497-1068 |
2.98e-11 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 68.65 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 497 LKHWAAQEIT----QNKALYtWINEGGAvGCQRTYAELDSNASCVAHKLltSRKPTIKPGDRVLLV--HVPGLDFIDAff 570
Cdd:cd05928 12 LDQWADKEKAgkrpPNPALW-WVNGKGD-EVKWSFRELGSLSRKAANVL--SGACGLQRGDRVAVIlpRVPEWWLVNV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 571 GCLRAKVIPIP----VLPPDPLQR----GGQALTKIENIAKLCNAVAILSTvgyhaavraglvknliSFTGKSVKSTGQW 642
Cdd:cd05928 86 ACIRTGLVFIPgtiqLTAKDILYRlqasKAKCIVTSDELAPEVDSVASECP----------------SLKTKLLVSEKSR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 643 PNlpWLHTDSWIKSSKvlpASNIAFQSESQpdDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVlVSWl 722
Cdd:cd05928 150 DG--WLNFKELLNEAS---TEHHCVETGSQ--EPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASD-IMW- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 723 pQYHDMG----LIGGLFTAMACGGSAILFSPLTFirNPLMWLQTISDYKATHSAGPNFAFELVIRRleadkakarnyDLS 798
Cdd:cd05928 221 -NTSDTGwiksAWSSLFEPWIQGACVFVHHLPRF--DPLVILKTLSSYPITTFCGAPTVYRMLVQQ-----------DLS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 799 SMIF-----FMIAAEPVRQKTLKRFVELTrpfGLSqevMAPGYGLAEncVFVSCAYGKKKPILVDWQGRICCGYvdpnda 873
Cdd:cd05928 287 SYKFpslqhCVTGGEPLNPEVLEKWKAQT---GLD---IYEGYGQTE--TGLICANFKGMKIKPGSMGKASPPY------ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 874 dvDIRIVDaDTGlEVDEDGKEGEIWIS-SPSAGIG----YWGKEELSQKTFRNKLQNypgrkytrTGDLGWVIQ-GNLFI 947
Cdd:cd05928 353 --DVQIID-DNG-NVLPPGTEGDIGIRvKPIRPFGlfsgYVDNPEKTAATIRGDFYL--------TGDRGIMDEdGYFWF 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 948 TGRIKDLIIVAGRNIYSADVEKtvesssellrpgccAVIGVPEEVLSAKgISLPDA-SDEV--GLVVIAElrDSKLVNKD 1024
Cdd:cd05928 421 MGRADDVINSSGYRIGPFEVES--------------ALIEHPAVVESAV-VSSPDPiRGEVvkAFVVLAP--QFLSHDPE 483
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1917948728 1025 -IIKQIESRVAEehgvTVASVKLirPRTIS------KTTSGKIKRFECLKQ 1068
Cdd:cd05928 484 qLTKELQQHVKS----VTAPYKY--PRKVEfvqelpKTVTGKIQRNELRDK 528
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
526-937 |
6.33e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.45 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqALTKIENiaklc 605
Cdd:PRK12316 4578 TYAELNRRANRLAHALIAR---GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER---LAYMMED----- 4646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTVGyHAAVRAGLVKNLISFtgkSVKSTGQWPNLPwlHTDswiksskvlPASNIAfqsesqPDDLCFLQFTSGS 685
Cdd:PRK12316 4647 SGAALLLTQS-HLLQRLPIPDGLASL---ALDRDEDWEGFP--AHD---------PAVRLH------PDNLAYVIYTSGS 4705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMACGGSAIlfspltfIRNPLMWL----- 760
Cdd:PRK12316 4706 TGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFD-GSHEGLYHPLINGASVV-------IRDDSLWDperly 4777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 761 QTISDYKATHSAGPNFAFELVIRRLEADKakarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQevmapGYGLAE 840
Cdd:PRK12316 4778 AEIHEHRVTVLVFPPVYLQQLAEHAERDG------EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFN-----GYGPTE 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 841 NCVFVSCaygkkkpilvdwqgRICCGYVDPNDADVDIRIVDADTGLEVDED-------GKEGEIWISSPSAGIGYWGKEE 913
Cdd:PRK12316 4847 TTVTVLL--------------WKARDGDACGAAYMPIGTPLGNRSGYVLDGqlnplpvGVAGELYLGGEGVARGYLERPA 4912
|
410 420
....*....|....*....|....
gi 1917948728 914 LSQKTFRNKLQNYPGRKYTRTGDL 937
Cdd:PRK12316 4913 LTAERFVPDPFGAPGGRLYRTGDL 4936
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
651-1062 |
6.84e-11 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 67.55 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 651 DSWIKSSKVLPASNIAFQSES--QPDDLCFLQFTSGSTSDAKGVMITHGGLIhnVKLMRRRYRSTSN-----TVLVSWLP 723
Cdd:cd17642 159 YTFITQNLPPGFNEYDFKPPSfdRDEQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHARDPIFGNqiipdTAILTVIP 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 724 QYHDMGLIGGLFTAMaCGGSAIL---FSPLTFirnplmwLQTISDYKATHS--AGPNFAF----ELVirrleaDKakarn 794
Cdd:cd17642 237 FHHGFGMFTTLGYLI-CGFRVVLmykFEEELF-------LRSLQDYKVQSAllVPTLFAFfaksTLV------DK----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 795 YDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQevmapGYGLAENcvfvscaygkKKPILVDWQGRI---CCGYVDPN 871
Cdd:cd17642 298 YDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQ-----GYGLTET----------TSAILITPEGDDkpgAVGKVVPF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 872 dadVDIRIVDADTG--LEVDEdgkEGEIWISSPSAGIGYWGKEElSQKTFRNKlqnypgRKYTRTGDLG-WVIQGNLFIT 948
Cdd:cd17642 363 ---FYAKVVDLDTGktLGPNE---RGELCVKGPMIMKGYVNNPE-ATKALIDK------DGWLHSGDIAyYDEDGHFFIV 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 949 GRIKDLIIVAGRNIYSADVEKTVESSSELLRPGccaVIGVPEevlsakgislPDASDEVGLVVIAElRDSKLVNKDIIKQ 1028
Cdd:cd17642 430 DRLKSLIKYKGYQVPPAELESILLQHPKIFDAG---VAGIPD----------EDAGELPAAVVVLE-AGKTMTEKEVMDY 495
|
410 420 430
....*....|....*....|....*....|....
gi 1917948728 1029 IESRVAEEHGVTvASVKLIrpRTISKTTSGKIKR 1062
Cdd:cd17642 496 VASQVSTAKRLR-GGVKFV--DEVPKGLTGKIDR 526
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
672-971 |
7.53e-11 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 67.38 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 672 QPDDLCFLQFTSGSTSDAKGVMITHGGL----IHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGsAILF 747
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGG-QVYF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 S-----------------PLTFIRNPLMW-----------------------------LQTISDYKATHSagPNFAFELV 781
Cdd:cd05933 227 AqpdalkgtlvktlrevrPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgLETNLKLMGGES--PSPLFYRL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 782 IRRLEADKAKARnYDLSSMIFFMIAAEPVRQKTLKRFVELTRPFGlsqevmaPGYGLAEN--CVFVSCAYGkkkpilvdw 859
Cdd:cd05933 305 AKKLVFKKVRKA-LGLDRCQKFFTGAAPISRETLEFFLSLNIPIM-------ELYGMSETsgPHTISNPQA--------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 860 QGRICCGYVDPNdadVDIRIVdadtglEVDEDGkEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGW 939
Cdd:cd05933 368 YRLLSCGKALPG---CKTKIH------NPDADG-IGEICFWGRHVFMGYLNMEDKTEEAIDED-------GWLHSGDLGK 430
|
330 340 350
....*....|....*....|....*....|....
gi 1917948728 940 V-IQGNLFITGRIKDLIIVA-GRNIYSADVEKTV 971
Cdd:cd05933 431 LdEDGFLYITGRIKELIITAgGENVPPVPIEDAV 464
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
527-1062 |
1.18e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 66.57 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 527 YAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPLQRggqaltkienIAK 603
Cdd:PRK05857 44 YRELVAEVGGLAADL---RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAdgnLPIAAIER----------FCQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 604 LCNAVAILSTVGYHAAvRAGLVKNLISFTGKSVKSTGQwpnlpwlHTDSWIKSSKVLPASNIafqsESQPDDLCFLQFTS 683
Cdd:PRK05857 111 ITDPAAALVAPGSKMA-SSAVPEALHSIPVIAVDIAAV-------TRESEHSLDAASLAGNA----DQGSEDPLAMIFTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMR----RRYRSTSNTVLVSWLPQYHdmglIGGLFTAMAC---GGSAIlfsplTFIRNP 756
Cdd:PRK05857 179 GTTGEPKAVLLANRTFFAVPDILQkeglNWVTWVVGETTYSPLPATH----IGGLWWILTClmhGGLCV-----TGGENT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 757 LMWLQTISDYK-ATHSAGPNFAFELVirrleaDKAKARNYDLSSMIFF------MIAAEpvrqktlKRFVELTrpfGLSQ 829
Cdd:PRK05857 250 TSLLEILTTNAvATTCLVPTLLSKLV------SELKSANATVPSLRLVgyggsrAIAAD-------VRFIEAT---GVRT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 830 evmAPGYGLAENCVFVSCAYGKKKPIlvdwqGRICCGYVDPNDADVDIRIVDADTGLEVDEDGKE----GEIWISSPSAG 905
Cdd:PRK05857 314 ---AQVYGLSETGCTALCLPTDDGSI-----VKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPsasfGTLWIKSPANM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 906 IGYWGKEElsqktfrnklqnypgrkytRTGDL---GWVIQGNL---------FITGRIKDLIIVAGRNIYSADVEKTVES 973
Cdd:PRK05857 386 LGYWNNPE-------------------RTAEVlidGWVNTGDLlerredgffYIKGRSSEMIICGGVNIAPDEVDRIAEG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 974 ssellrpgccaVIGVPEevlsAKGISLPDA--SDEVGLVVIAelrdSKLVNKDIIKQIESRVAEEHGVTVASVKliRPRT 1051
Cdd:PRK05857 447 -----------VSGVRE----AACYEIPDEefGALVGLAVVA----SAELDESAARALKHTIAARFRRESEPMA--RPST 505
|
570
....*....|....*..
gi 1917948728 1052 ------ISKTTSGKIKR 1062
Cdd:PRK05857 506 ivivtdIPRTQSGKVMR 522
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
526-991 |
1.70e-10 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 65.99 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLtSRKPtiKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVlppDPLQRGGQALTKIENiAKLC 605
Cdd:cd05923 30 TYSELRARIEAVAARLH-ARGL--RPGQRVAVVLPNSVEAVIALLALHRLGAVPALI---NPRLKAAELAELIER-GEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAilstvgyhaAVRAGLVKNLISFTGKsVKSTGQWPNLPWLHTDSwikssKVLPASniafqsESQPDDLCFLQFTSGS 685
Cdd:cd05923 103 AAVI---------AVDAQVMDAIFQSGVR-VLALSDLVGLGEPESAG-----PLIEDP------PREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRR--YRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPltfiRNPLMWL 760
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTQagLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVveeFDP----ADALKLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 761 QT--ISDYKAThsagPNFAFELVIRRLEADKakarnyDLSSMIFFMIAAEPVRQKTLKRF-----VELTRPFGlSQEVM- 832
Cdd:cd05923 238 EQerVTSLFAT----PTHLDALAAAAEFAGL------KLSSLRHVTFAGATMPDAVLERVnqhlpGEKVNIYG-TTEAMn 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 833 -------APGYGLaencvfvscaygkkKPilvdwqgriccGYVDpndadvDIRIVDADTG-LEVDEDGKEGEIWI--SSP 902
Cdd:cd05923 307 slymrdaRTGTEM--------------RP-----------GFFS------EVRIVRIGGSpDEALANGEEGELIVaaAAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 903 SAGIGYWGKEELSQKTFRNklqnypgRKYtRTGDLGWVI-QGNLFITGRIKDLIIVAGRNIYSADVEKTVEssselLRPG 981
Cdd:cd05923 356 AAFTGYLNQPEATAKKLQD-------GWY-RTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLS-----RHPG 422
|
490
....*....|..
gi 1917948728 982 C--CAVIGVPEE 991
Cdd:cd05923 423 VteVVVIGVADE 434
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
682-1064 |
2.00e-10 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 65.56 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 682 TSGSTSDAKGVMITHGGLIHNVKLMRRRYRS---TSNTVLVSWLPqyhdMGL-IGGLFTAMAC---GGSAILFSPLtfir 754
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFARSLRAagvRPGDRVQNAFG----YGLfTGGLGLHYGAerlGATVIPAGGG---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 755 NPLMWLQTISDYKATHSAG-PNFAFELvIRRLEADKAKARNYDLSSMIFfmiAAEPVRQKTLKRFVELtrpFGLsqEVMA 833
Cdd:COG1541 163 NTERQLRLMQDFGPTVLVGtPSYLLYL-AEVAEEEGIDPRDLSLKKGIF---GGEPWSEEMRKEIEER---WGI--KAYD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 834 pGYGLAE--NCVFVSCAYgkkKPILVDWQGRIccgYVDpndadvdirIVDADTGlEVDEDGKEGEIWISS------Psag 905
Cdd:COG1541 234 -IYGLTEvgPGVAYECEA---QDGLHIWEDHF---LVE---------IIDPETG-EPVPEGEEGELVVTTltkeamP--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 906 igywgkeelsqktfrnkLQNYpgrkytRTGDLGWVIQGN----------LFITGRIKDLIIVAGRNIYSADVEKTVESSS 975
Cdd:COG1541 294 -----------------LIRY------RTGDLTRLLPEPcpcgrthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 976 ELlrpGCCAVIGVPEEvlsakgislpDASDEvgLVVIAELRDsKLVNKDIIKQIESRVAEEHGVTVAsVKLIRPRTISKT 1055
Cdd:COG1541 351 EV---GPEYQIVVDRE----------GGLDE--LTVRVELAP-GASLEALAEAIAAALKAVLGLRAE-VELVEPGSLPRS 413
|
....*....
gi 1917948728 1056 TsGKIKRFE 1064
Cdd:COG1541 414 E-GKAKRVI 421
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
526-973 |
2.42e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 65.30 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAKLC 605
Cdd:cd12117 24 TYAELNERANRLARRL---RAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAER-------LAFMLADA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTVGYHAAVRAGLVknlisftgksvkstgqwpnlPWLHTDSWIKSSKVLPASNIAfqsesqPDDLCFLQFTSGS 685
Cdd:cd12117 94 GAKVLLTDRSLAGRAGGLEV--------------------AVVIDEALDAGPAGNPAVPVS------PDDLAYVMYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKlmRRRYRS-TSNTVLVSWLPQYHDMGLIGgLFTAMACGGSAILFSPLTFIRnplmwLQTIS 764
Cdd:cd12117 148 TGRPKGVAVTHRGVVRLVK--NTNYVTlGPDDRVLQTSPLAFDASTFE-IWGALLNGARLVLAPKGTLLD-----PDALG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 765 DYKATHsaGPNFAFelvirrleadkakarnydLSSMIFFMIAAE-PVRQKTLKRFVeltrpFGlsQEVMAP--------- 834
Cdd:cd12117 220 ALIAEE--GVTVLW------------------LTAALFNQLADEdPECFAGLRELL-----TG--GEVVSPphvrrvlaa 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 835 --------GYGLAENCVFvSCAYGKKKPilvdwqgriccgyvDPNDADVDI-RIVDADTGLEVDEDGK------EGEIWI 899
Cdd:cd12117 273 cpglrlvnGYGPTENTTF-TTSHVVTEL--------------DEVAGSIPIgRPIANTRVYVLDEDGRpvppgvPGELYV 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 900 SSPSAGIGYWGKEELSQKTF-RNKLQnyPGRKYTRTGDL-GWVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVES 973
Cdd:cd12117 338 GGDGLALGYLNRPALTAERFvADPFG--PGERLYRTGDLaRWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRA 411
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
1778-1994 |
3.08e-10 |
|
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to the Synechococcus elongatus PCC 7942 periplasmic protein srpA, of mostly bacterial origin. The plasmid-encoded srpA is regulated by sulfate, but does not seem to function in its uptake or metabolism.
Pssm-ID: 163709 Cd Length: 295 Bit Score: 63.79 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1778 GKRYTVIVRHSNS--LSADDDARLDARGAALRILSDDSPLLDLTLKTGKAFYARTISDFATWLVCGL---------AARE 1846
Cdd:cd08153 45 GGSVPVTGRFSLGggNPKAPDDAANPRGMALKFRLPDGEQWRMVMNSFPVFPVRTPEEFLALLKAIApdatgkpdpAKLK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1847 EHVKRVPHVRDAVwTSLRQA---DSFADLHYYS-NTcrlFRFKDRQ--EMYVKFKLRPSDenieedigkvEPSGILPPET 1920
Cdd:cd08153 125 AFLAAHPEAAAFL-AWIKTApppASFANTTYYGvNA---FYFTNANgkRQPVRWRFVPED----------GVKYLSDEEA 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728 1921 GAIPRDandtrpllFLAEDFHNRVKS-PsgVRYIFQLQVrPIPQDEAArdialDCTKPWDESQfPYIDVGEVIIN 1994
Cdd:cd08153 191 AKLGPD--------FLFDELAQRLAQgP--VRWDLVLQL-AEPGDPTD-----DPTKPWPADR-KEVDAGTLTIT 248
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
32-264 |
5.06e-10 |
|
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
Pssm-ID: 396255 [Multi-domain] Cd Length: 446 Bit Score: 64.43 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 32 SGLSAAYALAKLGyRDITVMEKHKSVGGMCESVEIEGKVYDLGGQVLaANSAPVIFHLAKESGTELEE--MDLHKLALID 109
Cdd:pfam01593 2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGLEDRLvlPDPAPFYTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 110 SFTGEYHDINVAEDYMSLVSL-----TLEIQDKAK---DSNHIGIHAVSDIASDLTPAYLEAHGIKSVPKSVQYGYTASG 181
Cdd:pfam01593 80 FAGGRRYPGDFRRVPAGWEGLlefgrLLSIPEKLRlglAALASDALDEFDLDDFSLAESLLFLGRRGPGDVEVWDRLIDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 182 YGFvQDMPY----------------AYIHEFTRTSMAGKIRRMKGGYMSLWKKISKSLL---IKVccNTEVQAVRRDGSD 242
Cdd:pfam01593 160 ELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLggdVRL--NTRVRSIDREGDG 236
|
250 260
....*....|....*....|..
gi 1917948728 243 VNVDITNSsgetEHKEFDKIII 264
Cdd:pfam01593 237 VTVTLTDG----EVIEADAVIV 254
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1124-1185 |
7.23e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 56.80 E-value: 7.23e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 1124 EFLKQLISEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIAD 1185
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
524-991 |
8.88e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 63.79 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLR--AKVIpipvlppdpLQRGGQALTKIENI 601
Cdd:PRK07788 74 TLTYAELDEQSNALARGLLAL---GVRAGDGVAVLARNHRGFVLALYAAGKvgARII---------LLNTGFSGPQLAEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 602 AKLCNAVAILSTVGYHAAVRA-----GLVKNLISFTGKSVKSTGQWPNLpwlhtDSWI--KSSKVLPASniafqseSQPD 674
Cdd:PRK07788 142 AAREGVKALVYDDEFTDLLSAlppdlGRLRAWGGNPDDDEPSGSTDETL-----DDLIagSSTAPLPKP-------PKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 675 DLCFLqfTSGSTSDAKGVMITH-------GGLIHNVKLmrrryRSTSNTVLVSwlPQYHDMGLiGGLFTAMACGGSAIL- 746
Cdd:PRK07788 210 GIVIL--TSGTTGTPKGAPRPEpsplaplAGLLSRVPF-----RAGETTLLPA--PMFHATGW-AHLTLAMALGSTVVLr 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 747 --FSPLTFIRNplmwlqtISDYKAThsagpnfafELVI------RRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRF 818
Cdd:PRK07788 280 rrFDPEATLED-------IAKHKAT---------ALVVvpvmlsRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 819 VELtrpFGlsqEVMAPGYGLAEnCVFVSCAYGK---KKPILVdwqGRICCGyvdpndadVDIRIVDADtGLEVDEdGKEG 895
Cdd:PRK07788 344 LEA---FG---PVLYNLYGSTE-VAFATIATPEdlaEAPGTV---GRPPKG--------VTVKILDEN-GNEVPR-GVVG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 896 EIWISSPSAGIGYWGKeelsqktfRNKlQNYPGrkYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEktvess 974
Cdd:PRK07788 404 RIFVGNGFPFEGYTDG--------RDK-QIIDG--LLSSGDVGYFDEdGLLFVDGRDDDMIVSGGENVFPAEVE------ 466
|
490 500
....*....|....*....|.
gi 1917948728 975 sELL--RPGC--CAVIGVPEE 991
Cdd:PRK07788 467 -DLLagHPDVveAAVIGVDDE 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
673-990 |
1.63e-09 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 62.78 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLihnvkLMRRRYRS-----TSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL- 746
Cdd:PRK08008 172 TDDTAEILFTSGTTSRPKGVVITHYNL-----RFAGYYSAwqcalRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLl 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 747 --FSPLTFirnplmWLQtISDYKATHSAgpnfAFELVIRRLEADKAKA--RNYDLSSMIFFMIAAEPVRQKTLKRF-VEL 821
Cdd:PRK08008 247 ekYSARAF------WGQ-VCKYRATITE----CIPMMIRTLMVQPPSAndRQHCLREVMFYLNLSDQEKDAFEERFgVRL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 822 TRPFGLSQEVMA-----PGyglaencvfvscayGKKKpilvdWQ--GRICCGYvdpndadvDIRIVDADtGLEVDEdGKE 894
Cdd:PRK08008 316 LTSYGMTETIVGiigdrPG--------------DKRR-----WPsiGRPGFCY--------EAEIRDDH-NRPLPA-GEI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 895 GEIWISS-PSAGI--GYWGKEELSQKTFRnklqnypGRKYTRTGDLGWVIQGNLF-ITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PRK08008 367 GEICIKGvPGKTIfkEYYLDPKATAKVLE-------ADGWLHTGDTGYVDEEGFFyFVDRRCNMIKRGGENVSCVELENI 439
|
330 340
....*....|....*....|
gi 1917948728 971 VESSSELLRpgcCAVIGVPE 990
Cdd:PRK08008 440 IATHPKIQD---IVVVGIKD 456
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
526-970 |
1.64e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.03 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGgQALTKIENIAKLC 605
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAA---GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL-AYMLDDSGVRLLL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTVGYHAAVRAgLVKNLISftgksvkstgqwpnlpwlhtDSWIKSSKVLPASNIAfqsesqPDDLCFLQFTSGS 685
Cdd:PRK12467 615 TQSHLLAQLPVPAGLRS-LCLDEPA--------------------DLLCGYSGHNPEVALD------PDNLAYVIYTSGS 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTfIRNPLMWLQTISD 765
Cdd:PRK12467 668 TGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG-VTELFGALASGATLHLLPPDC-ARDAEAFAALMAD 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 766 YKAThsagpnfAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVEL---TRPFGLsqevmapgYGLAENC 842
Cdd:PRK12467 746 QGVT-------VLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALgpgARLINH--------YGPTETT 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 843 VFVScaygkkkpilvdwQGRICCGYVDPND-------ADVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELS 915
Cdd:PRK12467 811 VGVS-------------TYELSDEERDFGNvpigqplANLGLYILDHY--LNPVPVGVVGELYIGGAGLARGYHRRPALT 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 916 QKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PRK12467 876 AERFVPDPFGADGGRLYRTGDLArYRADGVIEYLGRMDHQVKIRGFRIELGEIEAR 931
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
524-968 |
1.88e-09 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 62.27 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaltkIENIAK 603
Cdd:cd17652 12 TLTYAELNARANRLARLLAAR---GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER-------IAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 604 LCNAVAILStvgyhaavraglvknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQFTS 683
Cdd:cd17652 82 DARPALLLT-----------------------------------------------------------TPDNLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT-VLvswlpQYHDMGLIGG---LFTAMACGGSAILFSPLTFIR-NPLm 758
Cdd:cd17652 103 GSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrVL-----QFASPSFDASvweLLMALLAGATLVLAPAEELLPgEPL- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 759 wLQTISDYKATHSAGPNFAfelvIRRLEADkakarnyDLSSMIFFMIAAEPVRQKTLKRFVELTRpfglsqevMAPGYGL 838
Cdd:cd17652 177 -ADLLREHRITHVTLPPAA----LAALPPD-------DLPDLRTLVVAGEACPAELVDRWAPGRR--------MINAYGP 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 839 AENCVFVSCAY----GKKKPILVDWQGriccgyvdpndadVDIRIVDAdtGLEVDEDGKEGEIWISSPSAGIGYWGKEEL 914
Cdd:cd17652 237 TETTVCATMAGplpgGGVPPIGRPVPG-------------TRVYVLDA--RLRPVPPGVPGELYIAGAGLARGYLNRPGL 301
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728 915 SQKTFrnkLQN---YPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:cd17652 302 TAERF---VADpfgAPGSRMYRTGDLArWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
526-968 |
1.90e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.82 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALtkieniaklc 605
Cdd:PRK12316 2030 SYAELDSRANRLAHRL---RARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML---------- 2096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 navailstvgyhAAVRAGLvknLISFTGKSVK--STGQWPNLPWLHTDSWIKSSKVLPASNIAfqsesqPDDLCFLQFTS 683
Cdd:PRK12316 2097 ------------EDSGAAL---LLTQRHLLERlpLPAGVARLPLDRDAEWADYPDTAPAVQLA------GENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRRRYR-STSNTVLvSWLPQYHDmGLIGGLFTAMaCGGSAILFSPLTfIRNPLMWLQT 762
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVAHCQAAGERYElSPADCEL-QFMSFSFD-GAHEQWFHPL-LNGARVLIRDDE-LWDPEQLYDE 2231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 763 ISDYKATHSAGPNFAFELVIRRLEAD--KAKARNYDLSsmiffmiaAEPVRQKTLKRFVELTRPFGLSQevmapGYGLAE 840
Cdd:PRK12316 2232 MERHGVTILDFPPVYLQQLAEHAERDgrPPAVRVYCFG--------GEAVPAASLRLAWEALRPVYLFN-----GYGPTE 2298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 841 NCVFVSCaygkkkpilvdWQgricCGYVDPNDA----------DVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWG 910
Cdd:PRK12316 2299 AVVTPLL-----------WK----CRPQDPCGAayvpigralgNRRAYILDAD--LNLLAPGMAGELYLGGEGLARGYLN 2361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 911 KEELSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK12316 2362 RPGLTAERFVPDPFSASGERLYRTGDLArYRADGVVEYLGRIDHQVKIRGFRIELGEIE 2420
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
524-991 |
2.06e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 62.60 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPDPLQRggqaltkien 600
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQ---GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYVEDELRY---------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 601 IAKLCNAVAILstvgYHAAVrAGLVKNLIsftgksvkstgqwPNLPWLHTdsWIK----SSKVLPASNIAFQS------- 669
Cdd:PRK07798 95 LLDDSDAVALV----YEREF-APRVAEVL-------------PRLPKLRT--LVVvedgSGNDLLPGAVDYEDalaagsp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 670 -----ESQPDDLCFLqFTSGSTSDAKGVMITH--------GGL-------IHNVKLMRRRYRSTSNTVLVSWLPQYHDMG 729
Cdd:PRK07798 155 erdfgERSPDDLYLL-YTGGTTGMPKGVMWRQedifrvllGGRdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 730 LIGGlFTAMACGGSAILFSPLTFirNPLMWLQTISDYKATHSA--GPNFAfelviRRLEADKAKARNYDLSSMifFMIA- 806
Cdd:PRK07798 234 QWAA-FAALFSGQTVVLLPDVRF--DADEVWRTIEREKVNVITivGDAMA-----RPLLDALEARGPYDLSSL--FAIAs 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 807 -AEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAE--NCVFVSCAYGKKKpilvDWQGRIccgyvdpnDADVDIRIVDAD 883
Cdd:PRK07798 304 gGALFSPSVKEALLEL-----LPNVVLTDSIGSSEtgFGGSGTVAKGAVH----TGGPRF--------TIGPRTVVLDED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 884 TGLEVDEDGKEGeiWIS-SPSAGIGYWGKEELSQKTFRnklqNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRN 961
Cdd:PRK07798 367 GNPVEPGSGEIG--WIArRGHIPLGYYKDPEKTAETFP----TIDGVRYAIPGDRArVEADGTITLLGRGSVCINTGGEK 440
|
490 500 510
....*....|....*....|....*....|....
gi 1917948728 962 IYSADVEktvesssELLR--PGC--CAVIGVPEE 991
Cdd:PRK07798 441 VFPEEVE-------EALKahPDVadALVVGVPDE 467
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
653-750 |
3.64e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 62.03 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 653 WIKSSKVLPASNIAFQsesQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIG 732
Cdd:PRK08043 347 WIFAHLLMPRLAQVKQ---QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTV 423
|
90
....*....|....*....
gi 1917948728 733 GLFTAMACGGSAILF-SPL 750
Cdd:PRK08043 424 GLFTPLLTGAEVFLYpSPL 442
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
23-60 |
3.87e-09 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 61.30 E-value: 3.87e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:COG0493 123 KVAVVGSGPAGLAAAYQLARAGH-EVTVFEALDKPGGL 159
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
875-1062 |
4.43e-09 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 61.81 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 875 VDIRIVDADTGlEVDEDGkEGEIWISSPSAGI--GYWGKEELSQKTFrnkLQNYPGrkYTRTGDlGWVI--QGNLFITGR 950
Cdd:cd05966 419 IEPAILDEEGN-EVEGEV-EGYLVIKRPWPGMarTIYGDHERYEDTY---FSKFPG--YYFTGD-GARRdeDGYYWITGR 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 951 IKDLIIVAGRNIYSADVEktvesSSELLRPGC--CAVIGVPEEVlsaKGISLpdasdeVGLVViaeLRDSKLVNKDIIKQ 1028
Cdd:cd05966 491 VDDVINVSGHRLGTAEVE-----SALVAHPAVaeAAVVGRPHDI---KGEAI------YAFVT---LKDGEEPSDELRKE 553
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1917948728 1029 IESRVAEEHGvtvasvKLIRPRTI------SKTTSGKIKR 1062
Cdd:cd05966 554 LRKHVRKEIG------PIATPDKIqfvpglPKTRSGKIMR 587
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
497-919 |
4.62e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 61.68 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 497 LKHWAAQEITQnkalyTWINEGGAVGCQR--TYAELDSNASCVAHKLLtSRKptIKPGDRVLLVHVPGLDFIDAFFGCLR 574
Cdd:cd05921 1 LAHWARQAPDR-----TWLAEREGNGGWRrvTYAEALRQVRAIAQGLL-DLG--LSAERPLLILSGNSIEHALMALAAMY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 575 AKVIPIPVLPPDPLQrgGQALTKIENIAKLCN--AVAILSTVGYHAAVRAGL---VKNLISFTGKSVKSTGQWPNLpwLH 649
Cdd:cd05921 73 AGVPAAPVSPAYSLM--SQDLAKLKHLFELLKpgLVFAQDAAPFARALAAIFplgTPLVVSRNAVAGRGAISFAEL--AA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 650 TDSWIKSSKVLPASniafqsesQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMR--RRYRSTSNTVLVSWLPQYHD 727
Cdd:cd05921 149 TPPTAAVDAAFAAV--------GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEqtYPFFGEEPPVLVDWLPWNHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 728 MGLIGGLFTAMACGGSAILF----SPLTF---IRNplmwLQTIS-DYKATHSAGpnfaFELVIRRLEADKAKARNYdLSS 799
Cdd:cd05921 221 FGGNHNFNLVLYNGGTLYIDdgkpMPGGFeetLRN----LREISpTVYFNVPAG----WEMLVAALEKDEALRRRF-FKR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 800 MIFFMIAAEPVRQKTLKRFVELTRPFGLSQEVMAPGYGLAENCVFVSCAYGKkkpilvdwQGRIccGYVDPNDADVDIRI 879
Cdd:cd05921 292 LKLMFYAGAGLSQDVWDRLQALAVATVGERIPMMAGLGATETAPTATFTHWP--------TERS--GLIGLPAPGTELKL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1917948728 880 VDADTGLEVDEDGkegeiwissPSAGIGYWGKEELSQKTF 919
Cdd:cd05921 362 VPSGGKYEVRVKG---------PNVTPGYWRQPELTAQAF 392
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
673-954 |
4.72e-09 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 61.46 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNV----KLMRRRYRSTSNTVLVSWLPQYHdmgliggLF-----TAMACGGS 743
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAH-------IFervveALFLYHGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 744 AILF---------------SPLTFIRNPLMwLQTISD-YKATHSAGP-------NFAFELVIRRLEA------------- 787
Cdd:cd05927 186 KIGFysgdirlllddikalKPTVFPGVPRV-LNRIYDkIFNKVQAKGplkrklfNFALNYKLAELRSgvvraspfwdklv 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 788 -DKAKARnydLSSMIFFMI-AAEPVRQKTLKRfveLTRPFGLsqEVMApGYGLAENCVFVSCAygkkkpilvdWQGRICC 865
Cdd:cd05927 265 fNKIKQA---LGGNVRLMLtGSAPLSPEVLEF---LRVALGC--PVLE-GYGQTECTAGATLT----------LPGDTSV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 866 GYVDPNDADVDIRIVD-ADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypGrkYTRTGDLG-WVIQG 943
Cdd:cd05927 326 GHVGGPLPCAEVKLVDvPEMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDED-----G--WLHTGDIGeWLPNG 398
|
330
....*....|.
gi 1917948728 944 NLFITGRIKDL 954
Cdd:cd05927 399 TLKIIDRKKNI 409
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
23-68 |
6.59e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 60.67 E-value: 6.59e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEG 68
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGG 45
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
670-954 |
1.11e-08 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 60.51 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 670 ESQPDDLCFLQFTSGSTSDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVlVSWLPQYHDMGLIGGLFTAMACGgSAILF- 747
Cdd:cd17641 154 AGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLgHCAAYLAADPLGPGDEY-VSVLPLPWIGEQMYSVGQALVCG-FIVNFp 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 -SPLTFIRNplmwLQTIsdykathsaGPNFAFeLVIRRLEADKAKARNYdlssmiffMIAAEPVRQKTLKRFVELTR--- 823
Cdd:cd17641 232 eEPETMMED----LREI---------GPTFVL-LPPRVWEGIAADVRAR--------MMDATPFKRFMFELGMKLGLral 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 824 PFGLSQEVMAPG----YGLAENCVF-----------VSCAYGKKKPILVD----------------WQGRICCGYVDPND 872
Cdd:cd17641 290 DRGKRGRPVSLWlrlaSWLADALLFrplrdrlgfsrLRSAATGGAALGPDtfrffhaigvplkqlyGQTELAGAYTVHRD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 873 ADVDIRIVD---ADTGLEVDEdgkEGEIWISSPSAGIGYWGKEELSQKTFrnklqnyPGRKYTRTGDLGWVIQ-GNLFIT 948
Cdd:cd17641 370 GDVDPDTVGvpfPGTEVRIDE---VGEILVRSPGVFVGYYKNPEATAEDF-------DEDGWLHTGDAGYFKEnGHLVVI 439
|
....*.
gi 1917948728 949 GRIKDL 954
Cdd:cd17641 440 DRAKDV 445
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
524-968 |
1.16e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.95 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 524 QRTYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqALTKIENiak 603
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIAL---GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER---LAYMIED--- 1669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 604 lcNAVAILSTvgyHAAVRAGLVknlisfTGKSVKSTGQWPNLPWLHTDSwikssKVLPASNIAfqsesqPDDLCFLQFTS 683
Cdd:PRK12467 1670 --SGIELLLT---QSHLQARLP------LPDGLRSLVLDQEDDWLEGYS-----DSNPAVNLA------PQNLAYVIYTS 1727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 684 GSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTFiRNPLMWLQTI 763
Cdd:PRK12467 1728 GSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVS-VWELFWPLINGARLVIAPPGAH-RDPEQLIQLI 1805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 764 SDYKATHSAGPNFAFELVirrLEADKAKARNYDLSSMIFfmiAAEPVRQKTLKRFVELTRPFGLSQevmapGYGLAENCV 843
Cdd:PRK12467 1806 ERQQVTTLHFVPSMLQQL---LQMDEQVEHPLSLRRVVC---GGEALEVEALRPWLERLPDTGLFN-----LYGPTETAV 1874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 844 FVScaygKKKPILVDWQGRICCGYVDPNdADVDIRIVDAdtGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKL 923
Cdd:PRK12467 1875 DVT----HWTCRRKDLEGRDSVPIGQPI-ANLSTYILDA--SLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADP 1947
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1917948728 924 QNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK12467 1948 FGTVGSRLYRTGDLArYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
660-989 |
2.20e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 59.26 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 660 LPASNIAFQSESQPDDLcflQFTSGSTSDAKGVMITHGGlihnvklmrrRYRSTSNTVlVSW-----------LPQYHDM 728
Cdd:PLN03102 175 LVARMFRIQDEHDPISL---NYTSGTTADPKGVVISHRG----------AYLSTLSAI-IGWemgtcpvylwtLPMFHCN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 729 GLIGGLFTAmACGGSAILFSPLTfirNPLMWlQTISDYKATHSAGPNFAFELVIRRLEADKAKArnydlSSMIFFMIAAE 808
Cdd:PLN03102 241 GWTFTWGTA-ARGGTSVCMRHVT---APEIY-KNIEMHNVTHMCCVPTVFNILLKGNSLDLSPR-----SGPVHVLTGGS 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 809 PVRQKTLKRFVELtrpfGLsqEVMApGYGLAEncvfvscAYGkkkPIL-VDWQG-------------RICCGYVDPNDAD 874
Cdd:PLN03102 311 PPPAALVKKVQRL----GF--QVMH-AYGLTE-------ATG---PVLfCEWQDewnrlpenqqmelKARQGVSILGLAD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 875 VDIRivDADTGLEVDEDGKE-GEIWISSPSAGIGYWGKEELSQKTFRNKLQNypgrkytrTGDLGwVIQ--GNLFITGRI 951
Cdd:PLN03102 374 VDVK--NKETQESVPRDGKTmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLN--------TGDVG-VIHpdGHVEIKDRS 442
|
330 340 350
....*....|....*....|....*....|....*...
gi 1917948728 952 KDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVP 989
Cdd:PLN03102 443 KDIIISGGENISSVEVENVLYKYPKVLE---TAVVAMP 477
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
873-1080 |
2.21e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 59.41 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 873 ADVDIRIVDADTGLEvDEDGKEGEIWISSPSAGIGYW----GKEELSQKTFRNKLQNYPGRKYT-----RTGDLGWVIQ- 942
Cdd:PRK05620 365 ASLEYRIVNDGQVME-STDRNEGEIQVRGNWVTASYYhsptEEGGGAASTFRGEDVEDANDRFTadgwlRTGDVGSVTRd 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 943 GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEE---------VLSAKGISLPDASDEvglvvia 1013
Cdd:PRK05620 444 GFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVE---CAVIGYPDDkwgerplavTVLAPGIEPTRETAE------- 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 1014 ELRDSklvnkdIIKQIESRVAEEHGVTVASvklirprtISKTTSGKIKRFECLKQFVDGNLN--TVPDP 1080
Cdd:PRK05620 514 RLRDQ------LRDRLPNWMLPEYWTFVDE--------IDKTSVGKFDKKDLRQHLADGDFEiiKLKGP 568
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
642-991 |
2.36e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 59.39 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 642 WPNLPWLHTdswiksSKVLPASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVK--LMRRRYRSTSNTVLV 719
Cdd:PRK13382 170 WTDEDHDLT------VEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKaiLDRTPWRAEEPTVIV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 720 SwlPQYHDMGLIGGLFTA-MACggsailfsPLTFIR--NPLMWLQTISDYKATHSAGPNFAFElviRRLEADKAKARNYD 796
Cdd:PRK13382 244 A--PMFHAWGFSQLVLAAsLAC--------TIVTRRrfDPEATLDLIDRHRATGLAVVPVMFD---RIMDLPAEVRNRYS 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 797 LSSMIFFMIAAEPVRQKTLKRFVEltrPFGlsqEVMAPGYGLAEnCVFVSCAYGKKKPILVDWQGRiccgyvdPNDAdVD 876
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMD---QFG---DVIYNNYNATE-AGMIATATPADLRAAPDTAGR-------PAEG-TE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 877 IRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKeelSQKTFRNKlqnypgrkYTRTGDLG-WVIQGNLFITGRIKDLI 955
Cdd:PRK13382 376 IRILDQD-FREV-PTGEVGTIFVRNDTQFDGYTSG---STKDFHDG--------FMASGDVGyLDENGRLFVVGRDDEMI 442
|
330 340 350
....*....|....*....|....*....|....*.
gi 1917948728 956 IVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEE 991
Cdd:PRK13382 443 VSGGENVYPIEVEKTLATHPDVAE---AAVIGVDDE 475
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
13-60 |
3.47e-08 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 58.73 E-value: 3.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1917948728 13 KLHPCLPlDT--RIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGM 60
Cdd:PRK12771 128 KFPAPAP-DTgkRVAVIGGGPAGLSAAYHLRRMGHA-VTIFEAGPKLGGM 175
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
674-1063 |
4.69e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 57.91 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 674 DDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLvsWlpQYHDMGLIGGLFTA----MACGGSAIL--- 746
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF--W--NAADPGWAYGLYYAitgpLALGHPTILleg 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 747 -FSPltfirnPLMWlQTISDYKATHSAGPNFAFelviRRLEADKAKARNYDLSSMIFFMIAAEPVRQktlkrfvELTRPF 825
Cdd:cd05973 164 gFSV------ESTW-RVIERLGVTNLAGSPTAY----RLLMAAGAEVPARPKGRLRRVSSAGEPLTP-------EVIRWF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 826 GLSQEV-MAPGYGLAENCVFVSCAYGKKKPILVDWQGRICCGYvdpndadvdiRI-VDADTGLEVDEdGKEGEIWI---S 900
Cdd:cd05973 226 DAALGVpIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGW----------RVaVLDDDGDELGP-GEPGRLAIdiaN 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 901 SPSAGI-GYWGKEelsQKTFrnklqnyPGRKYtRTGDLGWV-IQGNLFITGRIKDLIIVAGRNIYSADVEktvesSSELL 978
Cdd:cd05973 295 SPLMWFrGYQLPD---TPAI-------DGGYY-LTGDTVEFdPDGSFSFIGRADDVITMSGYRIGPFDVE-----SALIE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 979 RPGC--CAVIGVPE----EVLSAkgislpdasdevgLVVIAE-LRDSKLVNKDIIKQIESRVAeEHGvtvasvkliRPRT 1051
Cdd:cd05973 359 HPAVaeAAVIGVPDpertEVVKA-------------FVVLRGgHEGTPALADELQLHVKKRLS-AHA---------YPRT 415
|
410
....*....|....*...
gi 1917948728 1052 IS------KTTSGKIKRF 1063
Cdd:cd05973 416 IHfvdelpKTPSGKIQRF 433
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
526-973 |
6.46e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 57.71 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGqaltkieniaklc 605
Cdd:cd12115 26 TYAELNRRANRLAARL---RAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLR------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 navAILSTvgyhAAVRAGLVknlisftgksvkstgqwpnlpwlhtdswiksskvlpasniafqsesQPDDLCFLQFTSGS 685
Cdd:cd12115 90 ---FILED----AQARLVLT----------------------------------------------DPDDLAYVIYTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLihnVKLMRRRYRSTSNTVLVSWL---PQYHDMGlIGGLFTAMACGGSAILF-SPLTFIRNP----L 757
Cdd:cd12115 117 TGRPKGVAIEHRNA---AAFLQWAAAAFSAEELAGVLastSICFDLS-VFELFGPLATGGKVVLAdNVLALPDLPaaaeV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 758 MWLQTIsdykathsagPNFAFELVirRLEADKAKARNYDLssmiffmiAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYG 837
Cdd:cd12115 193 TLINTV----------PSAAAELL--RHDALPASVRVVNL--------AGEPLPRDLVQRLYAR-----LQVERVVNLYG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 838 LAEncvfvSCAYGKKKPILVDWQGRICCGYVDPND-ADVdirivdADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQ 916
Cdd:cd12115 248 PSE-----DTTYSTVAPVPPGASGEVSIGRPLANTqAYV------LDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTA 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728 917 KTFRNKlQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVES 973
Cdd:cd12115 317 ERFLPD-PFGPGARLYRTGDLVrWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRS 373
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
671-970 |
7.64e-08 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 57.44 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 671 SQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILfSPL 750
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEEIYVTLLSGATLVL-RPE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 TFIRNPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKAKArnydLSSMIFFMIAAEPVRQKTLKRFVELTRPFGLSQE 830
Cdd:cd17644 181 EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDL----PSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLIN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 831 VmapgYGLAENCVFVSCAYGKKkpILVDWQGRICCGYVDPNdadVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWG 910
Cdd:cd17644 257 V----YGPTEATIAATVCRLTQ--LTERNITSVPIGRPIAN---TQVYILDEN--LQPVPVGVPGELHIGGVGLARGYLN 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917948728 911 KEELSQKTF-RNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:cd17644 326 RPELTAEKFiSHPFNSSESERLYKTGDLArYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAV 387
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
833-1005 |
8.35e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 57.31 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 833 APGYGLAENCVFVSCAygkkKPilvD--WQGRICCGYVDPNdADVDIRivdadtglevdeDGKEGEIWISSPSAGIGYWG 910
Cdd:PRK07445 258 APTYGMTETASQIATL----KP---DdfLAGNNSSGQVLPH-AQITIP------------ANQTGNITIQAQSLALGYYP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 911 KEELSQKTFRnklqnypgrkytrTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEkTVESSSELLRPGCcaVIGVP 989
Cdd:PRK07445 318 QILDSQGIFE-------------TDDLGyLDAQGYLHILGRNSQKIITGGENVYPAEVE-AAILATGLVQDVC--VLGLP 381
|
170 180
....*....|....*....|
gi 1917948728 990 E----EVLSAkgISLPDASD 1005
Cdd:PRK07445 382 DphwgEVVTA--IYVPKDPS 399
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
1605-1686 |
8.84e-08 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 53.34 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1605 GAKVGRYCSIRAINPIADPRMVSIGAGVHLGDFSRIITGFY-----SQSGYIQGNVDIKDNSVTGSQSLILPGSVVEKDV 1679
Cdd:COG0110 27 NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHpiddpATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGA 106
|
....*..
gi 1917948728 1680 ILGAISV 1686
Cdd:COG0110 107 VVGAGSV 113
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1118-1194 |
1.08e-07 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 51.01 E-value: 1.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728 1118 SNRNIVEFLKQLISEQTGISIQNISATESLVS-YGIDSIGVVRAAQKLSDFLGVPVGAVDIFTATCIADLANFAENLL 1194
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
26-75 |
1.42e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 56.44 E-value: 1.42e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1917948728 26 IVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGMCESVEIEGKVYDLGG 75
Cdd:PRK07208 9 IIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGISRTVTYKGNRFDIGG 57
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
678-1081 |
1.67e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 56.67 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 678 FLQFTSGSTSDAKGVMITHGGlihNVKLMRRRYRSTSNTVLVSWLPQYHDMGLI---GGLFTAMACGGSAILFSPlTFIR 754
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGP---HLVGLKYYWRSIIEKDIPTVVFSHSSIGWVsfhGFLYGSLSLGNTFVMFEG-GIIK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 755 NPLM----WlQTISDYKATHSagpnFAFELVIRRL-----EADKAKArNYDLSSMIFFMIAAEPVRQkTLKRFVELTRPF 825
Cdd:PTZ00237 334 NKHIeddlW-NTIEKHKVTHT----LTLPKTIRYLiktdpEATIIRS-KYDLSNLKEIWCGGEVIEE-SIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 826 GLSQevmapGYGLAE-NCVFVSCAYGKKKPILVdwqgricCG----YVDPndadvdirivdadtgLEVDEDGKE------ 894
Cdd:PTZ00237 407 KSSR-----GYGQTEiGITYLYCYGHINIPYNA-------TGvpsiFIKP---------------SILSEDGKElnvnei 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 895 GEIWIS---SPSAGIGYWGKEELSQKTFrNKlqnYPGrkYTRTGDLGWVIQGNLF-ITGRIKDLIIVAGRNIYSADVEKT 970
Cdd:PTZ00237 460 GEVAFKlpmPPSFATTFYKNDEKFKQLF-SK---FPG--YYNSGDLGFKDENGYYtIVSRSDDQIKISGNKVQLNTIETS 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 971 VESSSELLRpgCCAVigvpeevlsakGISLPD-ASDEVGLVVIAELRDS------KLVNK--DIIKQ-IESrvaeehgVT 1040
Cdd:PTZ00237 534 ILKHPLVLE--CCSI-----------GIYDPDcYNVPIGLLVLKQDQSNqsidlnKLKNEinNIITQdIES-------LA 593
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1917948728 1041 VASVKLIRPRtISKTTSGKIKRfECLKQFVDGNLNTVPDPI 1081
Cdd:PTZ00237 594 VLRKIIIVNQ-LPKTKTGKIPR-QIISKFLNDSNYQLPDNV 632
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
521-1020 |
2.03e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 56.32 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 521 VGCQRTYAELDSNASCVAHKLltSRKpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPV---LPPdplqrggqalTK 597
Cdd:PRK07786 39 LGNTTTWRELDDRVAALAGAL--SRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVnfrLTP----------PE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 598 IENIAKLCNAVAIL---STVGYHAAVRAglvknlISFTGKSVKSTGQWPNlpwlhtDSWIKSSKVLPASNIAFQSESQPD 674
Cdd:PRK07786 106 IAFLVSDCGAHVVVteaALAPVATAVRD------IVPLLSTVVVAGGSSD------DSVLGYEDLLAEAGPAHAPVDIPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 675 DL-CFLQFTSGSTSDAKGVMITHGGLI-HNVKLMRRRYRSTSNTVLVSWLPQYHDMGLiGGLFTAMACGGSAILFSPLTF 752
Cdd:PRK07786 174 DSpALIMYTSGTTGRPKGAVLTHANLTgQAMTCLRTNGADINSDVGFVGVPLFHIAGI-GSMLPGLLLGAPTVIYPLGAF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 753 irNPLMWLQTISDYKATHsagpnfAFeLVIRRLEA--DKAKARNYDLSsMIFFMIAAEPVRQKTLKRFVElTRP------ 824
Cdd:PRK07786 253 --DPGQLLDVLEAEKVTG------IF-LVPAQWQAvcAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAA-TFPeaqila 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 825 -FGlsQEVMAPgyglaencvfVSCAYGKKKPIlvdwQGRICCGYVDPNdadVDIRIVDADTGlEVDEdGKEGEIWISSPS 903
Cdd:PRK07786 322 aFG--QTEMSP----------VTCMLLGEDAI----RKLGSVGKVIPT---VAARVVDENMN-DVPV-GEVGEIVYRAPT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 904 AGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLgwVIQ---GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRp 980
Cdd:PRK07786 381 LMSGYWNNPEATAEAFAGG--------WFHSGDL--VRQdeeGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVE- 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1917948728 981 gcCAVIGVPE----EVLSAKgISLPDASDEVGLVVIAELRDSKL 1020
Cdd:PRK07786 450 --VAVIGRADekwgEVPVAV-AAVRNDDAALTLEDLAEFLTDRL 490
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
23-59 |
2.15e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 55.96 E-value: 2.15e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGG 59
Cdd:PRK11749 142 KVAVIGAGPAGLTAAHRLARKGY-DVTIFEARDKAGG 177
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
1341-1432 |
2.92e-07 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 51.80 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1341 VHLRGTVFLKHWfemlGARIGSSVLLDT-VDITDPSLVSIGDGAVIAEGALL--QSHEVRN---SILRLQPIRIGRNCSV 1414
Cdd:COG0110 15 VVIGPGVRIYGG----NITIGDNVYIGPgVTIDDPGGITIGDNVLIGPGVTIltGNHPIDDpatFPLRTGPVTIGDDVWI 90
|
90
....*....|....*...
gi 1917948728 1415 GPYAVVQKGSVLREGAEV 1432
Cdd:COG0110 91 GAGATILPGVTIGDGAVV 108
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
21-74 |
4.29e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 55.24 E-value: 4.29e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1917948728 21 DTRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEGKVYDLG 74
Cdd:COG1233 3 MYDVVVIGAGIGGLAAAALLARAGYR-VTVLEKNDTPGGRARTFERPGFRFDVG 55
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
526-968 |
4.98e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.73 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKiENIAKLC 605
Cdd:PRK12316 538 DYAELNRRANRLAHAL---IERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLED-SGVQLLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 606 NAVAILSTVgyhaAVRAGLvkNLISFTGKSVKSTGQWPNLPWLHTDswiksskvlpasniafqsesqPDDLCFLQFTSGS 685
Cdd:PRK12316 614 SQSHLGRKL----PLAAGV--QVLDLDRPAAWLEGYSEENPGTELN---------------------PENLAYVIYTSGS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 686 TSDAKGVMITHGGLIHNVKLMRRRY-RSTSNTVLVSwLPQYHDMGlIGGLFTAMACGGSAILFSPlTFIRNPLMWLQTIs 764
Cdd:PRK12316 667 TGKPKGAGNRHRALSNRLCWMQQAYgLGVGDTVLQK-TPFSFDVS-VWEFFWPLMSGARLVVAAP-GDHRDPAKLVELI- 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 765 dykATHSAGpnfAFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELtrpfgLSQEVMAPGYGLAENCVF 844
Cdd:PRK12316 743 ---NREGVD---TLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAK-----LPQAGLYNLYGPTEAAID 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 845 VSC-----AYGKKKPIlvdwqGRICcgyvdpndADVDIRIVDADtgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTF 919
Cdd:PRK12316 812 VTHwtcveEGGDSVPI-----GRPI--------ANLACYILDAN--LEPVPVGVLGELYLAGRGLARGYHGRPGLTAERF 876
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1917948728 920 RNKLQNYPGRKYtRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVE 968
Cdd:PRK12316 877 VPSPFVAGERMY-RTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIE 925
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
526-769 |
1.25e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 54.28 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLltsRKPTIKPGDRVLlVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqaLTKIENIAKl 604
Cdd:PRK10252 485 SYREMREQVVALANLL---RERGVKPGDSVA-VALPrSVFLTLALHAIVEAGAAWLPLDTGYPDDR----LKMMLEDAR- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 605 cnAVAILSTvgyhAAVRAglvknliSFTGKsvkstgqwPNLPWLHTDSWiksskvLPASNIAFQSESQPDDLCFLQFTSG 684
Cdd:PRK10252 556 --PSLLITT----ADQLP-------RFADV--------PDLTSLCYNAP------LAPQGAAPLQLSQPHHTAYIIFTSG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 685 STSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFTAMACGGSAILFSPLTFiRNPLMWLQTIS 764
Cdd:PRK10252 609 STGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVS-VWEFFWPFIAGAKLVMAEPEAH-RDPLAMQQFFA 686
|
....*
gi 1917948728 765 DYKAT 769
Cdd:PRK10252 687 EYGVT 691
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
1605-1702 |
1.29e-06 |
|
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.
Pssm-ID: 100051 [Multi-domain] Cd Length: 153 Bit Score: 50.10 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1605 GAKVGRYCSIRA-INPIadprmvSIGAGVHLGDFSrIITGFYSQSGYIQGNV-----------DIKDNSVTGSQSLILPG 1672
Cdd:cd04645 23 GSSVWFGAVLRGdVNPI------RIGERTNIQDGS-VLHVDPGYPTIIGDNVtvghgavlhgcTIGDNCLIGMGAIILDG 95
|
90 100 110
....*....|....*....|....*....|
gi 1917948728 1673 SVVEKDVILGAISVAPVNSVLQSGGVYMGS 1702
Cdd:cd04645 96 AVIGKGSIVAAGSLVPPGKVIPPGSLVAGS 125
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
681-991 |
1.55e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 53.46 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 681 FTSGSTSDAKGV----MITHGGLIHNVKLMRRRYRSTSNTVLVswLPQYHDMGLiGGLFTAMACGGSAILFSPLtfirnp 756
Cdd:PRK13383 181 LTSGTTGKPKGVprapQLRSAVGVWVTILDRTRLRTGSRISVA--MPMFHGLGL-GMLMLTIALGGTVLTHRHF------ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 757 lmwlqtisDYKAT------HSAGPNFAFELVIRRLE--ADKAKARNyDLSSMIFFMIAAEPVRQKTLKRFVEltrPFGls 828
Cdd:PRK13383 252 --------DAEAAlaqaslHRADAFTAVPVVLARILelPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMD---TYG-- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 829 qEVMAPGYGLAEncvfVSCAYGKKKPILVDWQ---GRICCGyvdpndadVDIRIVDAD---TGLEVdedgkEGEIWISSP 902
Cdd:PRK13383 318 -DILYNGYGSTE----VGIGALATPADLRDAPetvGKPVAG--------CPVRILDRNnrpVGPRV-----TGRIFVGGE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 903 SAGIGYWGKeelSQKTFRNKLqnypgrkyTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPg 981
Cdd:PRK13383 380 LAGTRYTDG---GGKAVVDGM--------TSTGDMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADN- 447
|
330
....*....|
gi 1917948728 982 ccAVIGVPEE 991
Cdd:PRK13383 448 --AVIGVPDE 455
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
429-1003 |
2.58e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.42 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 429 FAFELTERNSSYAMALICKHFASANSLPTFPYVKSLFTLQLDQEETGLKTLSETSGvvfpNLPTLDCYLKHWAAQEITQN 508
Cdd:PRK12316 2996 YATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAA----EYPLERGVHRLFEEQVERTP 3071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 509 KALYTWINEGgavgcQRTYAELDSNASCVAHKLltsRKPTIKPgDRVLLVHVP-GLDFIDAFFGCLRAKVIPIPVLPPDP 587
Cdd:PRK12316 3072 DAVALAFGEQ-----RLSYAELNRRANRLAHRL---IERGVGP-DVLVGVAVErSLEMVVGLLAILKAGGAYVPLDPEYP 3142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 588 LQRGGQALTKieniaklcNAVAILSTVGYHAAVRAGLVKNLISFTGKSVKSTGQWPNLpwlhtdswiksskvlpasniaf 667
Cdd:PRK12316 3143 EERLAYMLED--------SGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIR---------------------- 3192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 668 qseSQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMACGGSAILf 747
Cdd:PRK12316 3193 ---TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVL- 3267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 spltfiRNPLMWLQTISDYKATHSAGPNF--AFELVIRRLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVELTRPF 825
Cdd:PRK12316 3268 ------AGPEDWRDPALLVELINSEGVDVlhAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLY 3341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 826 GLSQEVMAPgygLAENCVFVSCAYgkkKPIlvdwqgriccGYVDPNDAdvdirIVDADTGLEVDEDGKEGEIWISSPSAG 905
Cdd:PRK12316 3342 GPTEATITV---THWQCVEEGKDA---VPI----------GRPIANRA-----CYILDGSLEPVPVGALGELYLGGEGLA 3400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 906 IGYWGKEELSQKTFRNKLQNYPGRKYtRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSELLRPGCCA 984
Cdd:PRK12316 3401 RGYHNRPGLTAERFVPDPFVPGERLY-RTGDLArYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA 3479
|
570 580
....*....|....*....|..
gi 1917948728 985 VIG---VPEEVLSAKGISLPDA 1003
Cdd:PRK12316 3480 VDGrqlVAYVVPEDEAGDLREA 3501
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
487-995 |
2.78e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 52.79 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 487 FPNLPTLDCYLKHwAAQEITQNKALYTWINEGGAVGCQR--TYAELDSNASCVAHKLLTSrkpTIKPGDRVLLVHVPGLD 564
Cdd:PLN02736 40 HPEIGTLHDNFVY-AVETFRDYKYLGTRIRVDGTVGEYKwmTYGEAGTARTAIGSGLVQH---GIPKGACVGLYFINRPE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 565 FIDAFFGCLRAKVIPIPV---LPPDplqrggqALTKIENIAKL----CNAV---AILSTVGYHAAVRaglvknLISFTGK 634
Cdd:PLN02736 116 WLIVDHACSAYSYVSVPLydtLGPD-------AVKFIVNHAEVaaifCVPQtlnTLLSCLSEIPSVR------LIVVVGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 635 SvksTGQWPNLPWLHTDSWIKSSKVLPASNIAFQS--ESQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRS 712
Cdd:PLN02736 183 A---DEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPfrPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 713 TSNTVLVSWLPQ---YHDMGLIGGLFtamacGGSAILF---------------SPLTFIRNPLMWlQTISD--YKATHSA 772
Cdd:PLN02736 260 YPSDVHISYLPLahiYERVNQIVMLH-----YGVAVGFyqgdnlklmddlaalRPTIFCSVPRLY-NRIYDgiTNAVKES 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 773 GP------NFAFELVIRRLEADKAKARNYDlsSMIFFMIAAepvRQKTLKRFVeLTRPFGLSQEVM-----------APG 835
Cdd:PLN02736 334 GGlkerlfNAAYNAKKQALENGKNPSPMWD--RLVFNKIKA---KLGGRVRFM-SSGASPLSPDVMeflricfggrvLEG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 836 YGLAE-NCVFVSCAygkkkpilvdwQGRICCGYVDPNDADVDIRIVDADTGLEVDEDG--KEGEIWISSPSAGIGYWGKE 912
Cdd:PLN02736 408 YGMTEtSCVISGMD-----------EGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpyPRGEICVRGPIIFKGYYKDE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 913 ELSQKTFRNKlqnypgrKYTRTGDLG-WVIQGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS---------SELLRPG 981
Cdd:PLN02736 477 VQTREVIDED-------GWLHTGDIGlWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYAKCkfvaqcfvyGDSLNSS 549
|
570
....*....|....
gi 1917948728 982 CCAVIGVPEEVLSA 995
Cdd:PLN02736 550 LVAVVVVDPEVLKA 563
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
497-968 |
5.02e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.48 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 497 LKHWAAQEiTQNKALyTWinEGGAVGcqrtYAELDSNASCVAHKLltsRKPTIKPGDRVLLVHVPGLDFIDAFFGCLRAK 576
Cdd:PRK05691 1137 LNEQARQT-PERIAL-VW--DGGSLD----YAELHAQANRLAHYL---RDKGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 577 VIPIPVLPPDPLQRGGQALTKieniaklCNAVAILStvgyhaavRAGLVKNLISFTGKSVKSTGQwpnlpwLHTDSWIKS 656
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLAD-------SGVELLLT--------QSHLLERLPQAEGVSAIALDS------LHLDSWPSQ 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 657 SKVLPASNiafqsesqpDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGlIGGLFT 736
Cdd:PRK05691 1265 APGLHLHG---------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVS-VWECFW 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 737 AMACGGSAILFSPLTFiRNPLMWLQTISDYKAT--HSAGPnfafelvIRRLEADKAKARNYDLSSMIFFMIAAEP--VRQ 812
Cdd:PRK05691 1335 PLITGCRLVLAGPGEH-RDPQRIAELVQQYGVTtlHFVPP-------LLQLFIDEPLAAACTSLRRLFSGGEALPaeLRN 1406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 813 KTLKRfveltrpfgLSQEVMAPGYGLAENCVFVS---C--AYGKKKPIlvdwqGR----ICCgyvdpndadvdiRIVDAD 883
Cdd:PRK05691 1407 RVLQR---------LPQVQLHNRYGPTETAINVThwqCqaEDGERSPI-----GRplgnVLC------------RVLDAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 884 tgLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKLQNYPGRKYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNI 962
Cdd:PRK05691 1461 --LNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRArWNADGALEYLGRLDQQVKLRGFRV 1538
|
....*.
gi 1917948728 963 YSADVE 968
Cdd:PRK05691 1539 EPEEIQ 1544
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
491-729 |
5.08e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 51.97 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 491 PTLDCYLKHWAAQEITQnkalyTWINEGGAVGCQ---RTYAELDSNASCVAHKLLTSRKPtikPGDRVLLVHVPGLDFID 567
Cdd:PRK12582 49 RSIPHLLAKWAAEAPDR-----PWLAQREPGHGQwrkVTYGEAKRAVDALAQALLDLGLD---PGRPVMILSGNSIEHAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 568 AFFGCLRAKVIPIPVLPPDPLQRGGQAltKIENIAKLCNAVAILSTVG--YHAAVRAglvknlISFTGKSVKS-TGQWPN 644
Cdd:PRK12582 121 MTLAAMQAGVPAAPVSPAYSLMSHDHA--KLKHLFDLVKPRVVFAQSGapFARALAA------LDLLDVTVVHvTGPGEG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 645 LPWLHTDSWIkSSKVLPASNIAFQSESqPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLM---RRRYRSTSNTVLVSW 721
Cdd:PRK12582 193 IASIAFADLA-ATPPTAAVAAAIAAIT-PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQeqlRPREPDPPPPVSLDW 270
|
....*...
gi 1917948728 722 LPQYHDMG 729
Cdd:PRK12582 271 MPWNHTMG 278
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
22-96 |
5.91e-06 |
|
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213540 [Multi-domain] Cd Length: 462 Bit Score: 51.38 E-value: 5.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728 22 TRIGIVGGGPSGLSAAYALAKLGYR---DITVMEKHKSVGGMCESVEIEGKVYDLGGQVLAANSaPVIFHLAKESGTE 96
Cdd:TIGR00562 3 KHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERK-KSAPDLVKDLGLE 79
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
21-103 |
7.45e-06 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 50.32 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 21 DTRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGG-------MCESVEIegkVYDLG-GQVLAANSAPV---IFHL 89
Cdd:COG0654 3 RTDVLIVGGGPAGLALALALARAGIR-VTVVERAPPPRPdgrgialSPRSLEL---LRRLGlWDRLLARGAPIrgiRVRD 78
|
90
....*....|....
gi 1917948728 90 AkESGTELEEMDLH 103
Cdd:COG0654 79 G-SDGRVLARFDAA 91
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
16-60 |
1.15e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 50.54 E-value: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1917948728 16 PCLPLDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:PRK13984 278 EPEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGV 321
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1087-1187 |
1.61e-05 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 49.36 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1087 LTRSFTTGTCREGKTPRSHLAKSSLAPSPKLSNRNIVEFLKQLISEQTGISIQNISATESLVSYGIDSIGVVRAAQKLSD 1166
Cdd:COG3433 185 LLLALKVVARAAPALAAAEALLAAASPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRK 264
|
90 100
....*....|....*....|.
gi 1917948728 1167 fLGVPVGAVDIFTATCIADLA 1187
Cdd:COG3433 265 -AGLDVSFADLAEHPTLAAWW 284
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
673-751 |
1.70e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 50.12 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVK-LMRRRYRSTSNTVLVSWLPQYHDMGLIGGlfTAMACGGSAILF-SPL 750
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAgVMTVVPKLGKNDVYLAYLPLAHILELAAE--SVMAAVGAAIGYgSPL 326
|
.
gi 1917948728 751 T 751
Cdd:PLN02387 327 T 327
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
679-1064 |
1.82e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 49.95 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 679 LQFTSGSTSDAKGVMITHGGLIHNvklmrrryrSTSNTVlvSW-----------LPQYHdmgLIGGLF--TAMACGGSAI 745
Cdd:PRK08162 187 LNYTSGTTGNPKGVVYHHRGAYLN---------ALSNIL--AWgmpkhpvylwtLPMFH---CNGWCFpwTVAARAGTNV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 746 lfspltFIR--NPLMWLQTISDYKATHSAGPNFAFELVIRRLEADKAKarnydLSSMIFFMIAAEP----VRQKTLKRFV 819
Cdd:PRK08162 253 ------CLRkvDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAG-----IDHPVHAMVAGAAppaaVIAKMEEIGF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 820 ELTRPFGLSqEVmapgYGLAencvfVSCAygkKKPilvDW-----------QGRICCGYVdpndADVDIRIVDADTGLEV 888
Cdd:PRK08162 322 DLTHVYGLT-ET----YGPA-----TVCA---WQP---EWdalplderaqlKARQGVRYP----LQEGVTVLDPDTMQPV 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 889 DEDGKE-GEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrkYTRTGDLG-WVIQGNLFITGRIKDLIIVAGRNIYSAD 966
Cdd:PRK08162 382 PADGETiGEIMFRGNIVMKGYLKNPKATEEAFAGG--------WFHTGDLAvLHPDGYIKIKDRSKDIIISGGENISSIE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 967 VEKTvessseLLR-PGccavigvpeeVLSAKGISLPDAS-DEVGLVVIaELRDSKLVNK-DIIKQIESRVAeehGVTVAs 1043
Cdd:PRK08162 454 VEDV------LYRhPA----------VLVAAVVAKPDPKwGEVPCAFV-ELKDGASATEeEIIAHCREHLA---GFKVP- 512
|
410 420
....*....|....*....|.
gi 1917948728 1044 vKLIRPRTISKTTSGKIKRFE 1064
Cdd:PRK08162 513 -KAVVFGELPKTSTGKIQKFV 532
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
853-1061 |
2.25e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 853 KPILVDWQGRICCGYVDPNDADvDIRIVDADTGLE---------------VDEDGKEgeiwisSPSAGIG--YWGKEELS 915
Cdd:PRK13390 287 KHAMIDWLGPIVYEYYSSTEAH-GMTFIDSPDWLAhpgsvgrsvlgdlhiCDDDGNE------LPAGRIGtvYFERDRLP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 916 -------QKTFRNKLQNYPgrKYTRTGDLGWVIQ-GNLFITGRIKDLIIVAGRNIYSADVEKTVEssselLRPGC--CAV 985
Cdd:PRK13390 360 frylndpEKTAAAQHPAHP--FWTTVGDLGSVDEdGYLYLADRKSFMIISGGVNIYPQETENALT-----MHPAVhdVAV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 986 IGVPEevlsakgislPDASDEVGLVV--IAELRDSKLVNKDIIKQIESRVAeeHGVTVASVKLIR--PRT-ISKTTSGKI 1060
Cdd:PRK13390 433 IGVPD----------PEMGEQVKAVIqlVEGIRGSDELARELIDYTRSRIA--HYKAPRSVEFVDelPRTpTGKLVKGLL 500
|
.
gi 1917948728 1061 K 1061
Cdd:PRK13390 501 R 501
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
5-97 |
2.57e-05 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 49.63 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 5 KSVEDQFsklhPCLPLDTRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIE----GKVYDLGGQVLAA 80
Cdd:PLN03000 172 QAIKDKF----PAQSSKSSVVIVGAGLSGLAAARQLMRFGFK-VTVLEGRKRPGGRVYTKKMEanrvGAAADLGGSVLTG 246
|
90
....*....|....*..
gi 1917948728 81 NSAPVIFHLAKESGTEL 97
Cdd:PLN03000 247 TLGNPLGIIARQLGSSL 263
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
22-96 |
2.74e-05 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 49.08 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 22 TRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMCESVEIEgkvyDLG-----GQ--VLAANSApvIFHLAKESG 94
Cdd:COG3349 4 PRVVVVGGGLAGLAAAVELAEAGFR-VTLLEARPRLGGRARSFPDP----DTGlpidnGQhvLLGCYRN--TLDLLRRIG 76
|
..
gi 1917948728 95 TE 96
Cdd:COG3349 77 AA 78
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
21-59 |
3.23e-05 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 48.71 E-value: 3.23e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1917948728 21 DTRIGIVGGGPSGLSAAYALAKLGyRDITVMEKHKSVGG 59
Cdd:COG2072 6 HVDVVVIGAGQAGLAAAYHLRRAG-IDFVVLEKADDVGG 43
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
674-954 |
3.35e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 49.20 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 674 DDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRS-----TSNTVLVSWLPQYHDMGLigGLFTAMACGGSAILF- 747
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDligppEEDETYCSYLPLAHIMEF--GVTNIFLARGALIGFg 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 748 SPLT----FIR--------NPLMWL------QTISdyKATHSAGP----------NFAFELVIRRLEADK---------- 789
Cdd:PTZ00216 342 SPRTltdtFARphgdltefRPVFLIgvprifDTIK--KAVEAKLPpvgslkrrvfDHAYQSRLRALKEGKdtpywnekvf 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 790 AKARNYDLSSMIFFMIAAEPVRQKTlKRFVELTrpFGLsqevMAPGYGLAENCvfvsCAYGKKKPilvdwqGRICCGYVD 869
Cdd:PTZ00216 420 SAPRAVLGGRVRAMLSGGGPLSAAT-QEFVNVV--FGM----VIQGWGLTETV----CCGGIQRT------GDLEPNAVG 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 870 PNDADVDIRIVDADTGLEVDEDGKEGEIWISSPSAGIGYWGKEELSQKTFRNKlqnypgrKYTRTGDLGWV-IQGNLFIT 948
Cdd:PTZ00216 483 QLLKGVEMKLLDTEEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDED-------GWFHTGDVGSIaANGTLRII 555
|
....*.
gi 1917948728 949 GRIKDL 954
Cdd:PTZ00216 556 GRVKAL 561
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
23-110 |
3.44e-05 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 48.69 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYR-DITVMEKHKSVGGMCESVEIEGKVYDLGgqvlaansaPVIFHLAKESGTELeemd 101
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGPDaDITLLEASDRLGGKIQTVRKDGFPIELG---------PESFLARKPSAPAL---- 68
|
....*....
gi 1917948728 102 LHKLALIDS 110
Cdd:PRK11883 69 VKELGLEDE 77
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
21-94 |
3.57e-05 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 48.86 E-value: 3.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917948728 21 DTRIGIVGGGPSGLSAAYALAKLGYRDITVMEKHKSVGGMCESVEIEGKVYDLGgqvlaANS---APVIFHLAKESG 94
Cdd:PLN02576 12 SKDVAVVGAGVSGLAAAYALASKHGVNVLVTEARDRVGGNITSVSEDGFIWEEG-----PNSfqpSDPELTSAVDSG 83
|
|
| LbH_wcaF_like |
cd05825 |
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ... |
1352-1434 |
4.18e-05 |
|
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.
Pssm-ID: 100063 [Multi-domain] Cd Length: 107 Bit Score: 44.52 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1352 WFEMLGAR--IGSSVLLDTVDitdpsLVSIGDGAVIAEGALL--QSHEVRNSILRL--QPIRIGRNCSVGPYAVVQKGSV 1425
Cdd:cd05825 2 WNLTIGDNswIGEGVWIYNLA-----PVTIGSDACISQGAYLctGSHDYRSPAFPLitAPIVIGDGAWVAAEAFVGPGVT 76
|
....*....
gi 1917948728 1426 LREGAEVPA 1434
Cdd:cd05825 77 IGEGAVVGA 85
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1354-1432 |
4.69e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 48.57 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1354 EMLGARIGSSVLLDTVDITDPSLVSIGDGAV------------------IAEGALLQSH-EVRNSIL----------RLQ 1404
Cdd:PRK14356 241 ELLRARIVEKHLESGVLIHAPESVRIGPRATiepgaeiygpceiygasrIARGAVIHSHcWLRDAVVssgatihsfsHLE 320
|
90 100
....*....|....*....|....*...
gi 1917948728 1405 PIRIGRNCSVGPYAVVQKGSVLREGAEV 1432
Cdd:PRK14356 321 GAEVGDGCSVGPYARLRPGAVLEEGARV 348
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
661-770 |
5.32e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 48.33 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 661 PASNIAFQSESQPDDLCFLQFTSGSTSDAKGVMITH----------GGLIhnvklmrrryRSTSNTVLVSWLPQYHDMGL 730
Cdd:PRK08279 186 PTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHmrwlkamggfGGLL----------RLTPDDVLYCCLPLYHNTGG 255
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1917948728 731 IGGLFTAMACGGSAIL---FSPLTFirnplmWLQtISDYKATH 770
Cdd:PRK08279 256 TVAWSSVLAAGATLALrrkFSASRF------WDD-VRRYRATA 291
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
23-60 |
6.40e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 48.19 E-value: 6.40e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGM 231
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
874-1068 |
7.43e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 47.85 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 874 DVDIRIVDADtGLEVdEDGKEGEIWISSPSAGIGYWGKEELSQKTfrnklqnyPGRKYTRTGDLGWVIQ-GNLFITGRIK 952
Cdd:PRK07638 315 NVQVRICNEA-GEEV-QKGEIGTVYVKSPQFFMGYIIGGVLAREL--------NADGWMTVRDVGYEDEeGFIYIVGREK 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 953 DLIIVAGRNIYSADVEKTVESSSELLRpgcCAVIGVPEEVLSAKGISLPDASDEVglvviaelrdsklvnkdiiKQIESR 1032
Cdd:PRK07638 385 NMILFGGINIFPEEIESVLHEHPAVDE---IVVIGVPDSYWGEKPVAIIKGSATK-------------------QQLKSF 442
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1917948728 1033 VAEEhgvtVASVKliRPR------TISKTTSGKIKRFECLKQ 1068
Cdd:PRK07638 443 CLQR----LSSFK--IPKewhfvdEIPYTNSGKIARMEAKSW 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
473-746 |
8.68e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 48.23 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 473 ETGLKTLSETSGVVFPNLPTLDCYLKHWAAQEITQNKALYT-------WIN-------EGGAVGC---QRTYAELDSNAS 535
Cdd:PRK12467 3052 DRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPserlvhqLIEaqvartpEAPALVFgdqQLSYAELNRRAN 3131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 536 CVAHKLLTsrkptIKPGDRVLL-VHVP-GLDFIDAFFGCLRAKVIPIPVLPPDPLQRggqALTKIENiaklcNAVAILST 613
Cdd:PRK12467 3132 RLAHRLIA-----IGVGPDVLVgVAVErSVEMIVALLAVLKAGGAYVPLDPEYPRER---LAYMIED-----SGVKLLLT 3198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 614 VGyHAAVRAGLVKNLISFTGKSVKSTGQWPNLPWLHTDswiksskvlpasniafqsesqPDDLCFLQFTSGSTSDAKGVM 693
Cdd:PRK12467 3199 QA-HLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVM---------------------GENLAYVIYTSGSTGKPKGVG 3256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1917948728 694 ITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDmGLIGGLFTAMACGGSAIL 746
Cdd:PRK12467 3257 VRHGALANHLCWIAEAYELDANDRVLLFMSFSFD-GAQERFLWTLICGGCLVV 3308
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
672-840 |
9.08e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 48.04 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 672 QPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAILF-SPL 750
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYpSPL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 751 TFIRNPLMwlqtISDYKATHSAGPNFaFelvirrLEADKAKARNYDLSSMIFFMIAAEPVRQKTLKRFVEltrPFGLSqe 830
Cdd:PRK06814 871 HYRIIPEL----IYDTNATILFGTDT-F------LNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTWME---KFGIR-- 934
|
170
....*....|
gi 1917948728 831 vMAPGYGLAE 840
Cdd:PRK06814 935 -ILEGYGVTE 943
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
1607-1686 |
1.48e-04 |
|
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.
Pssm-ID: 100053 [Multi-domain] Cd Length: 109 Bit Score: 43.21 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1607 KVGRYCSIRAINPIADPRMVSIGAGVHLGDFSRIITGFYS--------QSGYIQGNVDIKDNSVTGSQSLILPGSVVEKD 1678
Cdd:cd04647 3 SIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82
|
....*...
gi 1917948728 1679 VILGAISV 1686
Cdd:cd04647 83 AVVGAGSV 90
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
1341-1432 |
1.71e-04 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 46.56 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1341 VHLRGTVFLKHwfemlGARIGS-SVLLDTVditdpslvsIGDGAVIaegalLQSHeVRNSIlrlqpirIGRNCSVGPYAV 1419
Cdd:COG1207 279 VILEGKTVIGE-----GVVIGPnCTLKDST---------IGDGVVI-----KYSV-IEDAV-------VGAGATVGPFAR 331
|
90
....*....|...
gi 1917948728 1420 VQKGSVLREGAEV 1432
Cdd:COG1207 332 LRPGTVLGEGVKI 344
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
23-178 |
2.12e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 46.22 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKH---KSVG---GMCESVEIEGKVYDLGGQVLAANSAPVIFHLAKESGTE 96
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGH-EVKVFEKNesvKEVGagiGIGDNVIKKLGNHDLAKGIKNAGQILSTMNLLDDKGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 97 LEEM---------DLHKLALIDSFTGEYHDinvaedymSLVSLTLEIQDKAKDSNHIGIHaVSDIASDLTPAYLEAHGIK 167
Cdd:PRK06753 81 LNKVklksntlnvTLHRQTLIDIIKSYVKE--------DAIFTGKEVTKIENETDKVTIH-FADGESEAFDLCIGADGIH 151
|
170
....*....|....*....
gi 1917948728 168 SV------PKS-VQY-GYT 178
Cdd:PRK06753 152 SKvrqsvnADSkVRYqGYT 170
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
18-60 |
2.20e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.39 E-value: 2.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1917948728 18 LPLDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:COG1148 137 VPVNKRALVIGGGIAGMTAALELAEQGY-EVYLVEKEPELGGR 178
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
23-264 |
2.22e-04 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 46.26 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKlgYRDITVMEKHKSVGGMCESVEIegkvyDLGGQVLAANSA---------PVIFHLAKES 93
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSR--RHDVTLFEANDRLGGHTHTVDV-----DLDGRTVPVDTGfivfnertyPNLTALFAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 94 GTELEEMDLhklalidSF------TG-EY--HDINvaedymslvslTLEIQdkakDSN-----HIGI---------HAVS 150
Cdd:COG2907 78 GVPTQPSDM-------SFsvsldgGGlEYagSNLN-----------GLFAQ----RRNllrprFWRMlrdilrfnrEAPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 151 DIASDLTP-----AYLEAHGIksvPKSVQYGY-----TA---SGYGFVQDMPYAYIHEFTRT----SMAGKI--RRMKGG 211
Cdd:COG2907 136 LLEAGSDDdltlgEFLDRNGY---SEAFRDHYllpmgAAiwsCPPDDMLDFPARFFVRFFHNhgllSVTDRPqwRTVKGG 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1917948728 212 ---YMslwKKISKSLLIKVCCNTEVQAVRRDGSdvNVDITNSSGETEHkeFDKIII 264
Cdd:COG2907 213 sreYV---RRLTAGLKDRIRLNTPVRSVRRDAD--GVEVRTADGEEER--FDHVVF 261
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
21-60 |
2.57e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 46.10 E-value: 2.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1917948728 21 DTRIGIVGGGPSGLSAAYALAKLGYR--DITVMEKHKSVG-GM 60
Cdd:COG4529 5 RKRIAIIGGGASGTALAIHLLRRAPEplRITLFEPRPELGrGV 47
|
|
| NRPS_term_dom |
TIGR02353 |
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ... |
2103-2302 |
3.00e-04 |
|
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.
Pssm-ID: 274093 [Multi-domain] Cd Length: 695 Bit Score: 46.28 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2103 LQTIVPYFLLGLIIY---FPLNLLLHCknarnMPVhwtfpFFWVSTGILAalTCAAAKYILVGKKKEdETVHIWsrGVFM 2179
Cdd:TIGR02353 16 LQWLAPLLGYNWLYEaldDVSWLYLRA-----VAL-----VFAVPVGRLG--FAIAAKWLLVGRWKP-GTYPIW--GSTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 2180 DTIWQAIRTV--FGDYFVemtSGSALFLMWMKLMGssVELDKGTYVDSMGAALNpEMVEVEGGGSVEREALLFGhvYDGE 2257
Cdd:TIGR02353 81 LRFWTVKRLVdaAPTVLL---SGSPLYSLYLRALG--AKIGKGVDIGSLPPVCT-DLLTIGAGTIVRKEVMLLG--YRAE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1917948728 2258 GGAVKFGKIVVGEGGFVGSRAVAMPG--VESGGSLSALSLAMKGEAI 2302
Cdd:TIGR02353 153 RGRLHTGPVTLGRDAFIGTRSTLDIDtsIGDGAQLGHGSALQGGQSI 199
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
23-59 |
3.65e-04 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 45.54 E-value: 3.65e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGG 59
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAGH-KVTVFERADRIGG 180
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
526-744 |
4.69e-04 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 45.52 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 526 TYAELDSNASCVAHKLLTSRkpTIKPGDRVLLVHVPGLDFIDAFFGCLRAKVIPIPVLPPDPLQRGGQALTKIE------ 599
Cdd:cd17632 69 TYAELWERVGAVAAAHDPEQ--PVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEprllav 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 600 NIAKLCNAVAILSTVG---------YHAAV---RAGLVKNLISFTGKSVKSTgqwpnlpwLHTDSWIKSSKVLPASniAF 667
Cdd:cd17632 147 SAEHLDLAVEAVLEGGtpprlvvfdHRPEVdahRAALESARERLAAVGIPVT--------TLTLIAVRGRDLPPAP--LF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 668 QSESQPDDLCFLQFTSGSTSDAKGVMITHggliHNVKLMRRRYRST-----SNTVLVSWLPQYHDMGLIgGLFTAMACGG 742
Cdd:cd17632 217 RPEPDDDPLALLIYTSGSTGTPKGAMYTE----RLVATFWLKVSSIqdirpPASITLNFMPMSHIAGRI-SLYGTLARGG 291
|
..
gi 1917948728 743 SA 744
Cdd:cd17632 292 TA 293
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
22-55 |
4.95e-04 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 45.01 E-value: 4.95e-04
10 20 30
....*....|....*....|....*....|....
gi 1917948728 22 TRIGIVGGGPSGLSAAYALAKLGYRdITVMEKHK 55
Cdd:PRK12409 2 SHIAVIGAGITGVTTAYALAQRGYQ-VTVFDRHR 34
|
|
| LbH_MAT_like |
cd04647 |
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ... |
1371-1432 |
5.56e-04 |
|
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.
Pssm-ID: 100053 [Multi-domain] Cd Length: 109 Bit Score: 41.67 E-value: 5.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1371 ITDPSLVSIGDGAVIAEGALLQSH--------EVRNSILRLQPIRIGRNCSVGPYAVVQKGSVLREGAEV 1432
Cdd:cd04647 16 ISAGGGITIGDNVLIGPNVTIYDHnhdiddpeRPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVV 85
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
1356-1420 |
5.73e-04 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 42.17 E-value: 5.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917948728 1356 LGARIGSSVLLDTVDITDPSLVSIGDGAVIAEGAllqshevrnSILRLQPIRIGRNCSVGPYAVV 1420
Cdd:COG0110 7 FGARIGDGVVIGPGVRIYGGNITIGDNVYIGPGV---------TIDDPGGITIGDNVLIGPGVTI 62
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
888-1082 |
5.74e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 45.27 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 888 VDEDGKE--GE------IWISSPSAGIGYWGKEELSQKTFRNKLQNY--PGRKYTRTGDlgwviqGNLFITGRIKDLIIV 957
Cdd:PLN02654 468 VDEKGKEieGEcsgylcVKKSWPGAFRTLYGDHERYETTYFKPFAGYyfSGDGCSRDKD------GYYWLTGRVDDVINV 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 958 AGRNIYSADVEktvesSSELLRPGC--CAVIGVPEEVlsaKGislpdasdeVGLVVIAELRDSKLVNKDIIKQIESRVAE 1035
Cdd:PLN02654 542 SGHRIGTAEVE-----SALVSHPQCaeAAVVGIEHEV---KG---------QGIYAFVTLVEGVPYSEELRKSLILTVRN 604
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1917948728 1036 EHGVTVASVKLIRPRTISKTTSGKIKRfECLKQFVD------GNLNTVPDPIV 1082
Cdd:PLN02654 605 QIGAFAAPDKIHWAPGLPKTRSGKIMR-RILRKIASrqldelGDTSTLADPGV 656
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
673-729 |
8.58e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 44.48 E-value: 8.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1917948728 673 PDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNT--VLVSWLPQYHDMG 729
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFG 266
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
23-59 |
1.10e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 43.54 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGG 59
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGL-SVTLLERGDDPGS 36
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
20-55 |
1.26e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 43.69 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1917948728 20 LDTRIGIVGGGPSGLSAAYALAKLGYrDITVMEKHK 55
Cdd:PRK06185 5 ETTDCCIVGGGPAGMMLGLLLARAGV-DVTVLEKHA 39
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
879-1062 |
1.33e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 43.98 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 879 IVDaDTGLEVdEDGKEGEIWISSPSAGI--GYWGKEELSQKTFRNKlqnYPGRKYTrtGDlgWVIQ---GNLFITGRIKD 953
Cdd:PRK00174 437 VVD-EEGNPL-EGGEGGNLVIKDPWPGMmrTIYGDHERFVKTYFST---FKGMYFT--GD--GARRdedGYYWITGRVDD 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 954 LIIVAGRNIYSADVEKTV---ESSSEllrpgcCAVIGVPEEVlsaKGISLpdasdeVGLVViaeLRDSKLVNKDIIKQIE 1030
Cdd:PRK00174 508 VLNVSGHRLGTAEIESALvahPKVAE------AAVVGRPDDI---KGQGI------YAFVT---LKGGEEPSDELRKELR 569
|
170 180 190
....*....|....*....|....*....|....*..
gi 1917948728 1031 SRVAEEHGvTVASVKLIR-----PrtisKTTSGKIKR 1062
Cdd:PRK00174 570 NWVRKEIG-PIAKPDVIQfapglP----KTRSGKIMR 601
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
24-59 |
1.59e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 42.46 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1917948728 24 IGIVGGGPSGLSAAYALAKLGYRDITVMEKHKSVGG 59
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLAKNRGLKVAIIERSVSPGG 55
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
21-54 |
1.74e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 42.97 E-value: 1.74e-03
10 20 30
....*....|....*....|....*....|....
gi 1917948728 21 DTRIGIVGGGPSGLSAAYALAKLGyRDITVMEKH 54
Cdd:COG0665 2 TADVVVIGGGIAGLSTAYHLARRG-LDVTVLERG 34
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
675-752 |
1.75e-03 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 43.50 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 675 DLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRYRSTSNTVLVSWLPQYHDMGLIGGLFTAMACGGSAIL---FSPLT 751
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASN 161
|
.
gi 1917948728 752 F 752
Cdd:cd05940 162 F 162
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
23-60 |
2.16e-03 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 42.67 E-value: 2.16e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGGM 60
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGY-EVHVYDKLPEPGGL 56
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
26-61 |
2.33e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 42.84 E-value: 2.33e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1917948728 26 IVGGGPSGLSAAYALAKLGYRdITVMEKHKSVGGMC 61
Cdd:PRK05249 10 VIGSGPAGEGAAMQAAKLGKR-VAVIERYRNVGGGC 44
|
|
| LbH_GlmU_C |
cd03353 |
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ... |
1341-1432 |
2.62e-03 |
|
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.
Pssm-ID: 100044 [Multi-domain] Cd Length: 193 Bit Score: 41.25 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1341 VHLRGTVFLKHwfemlGARIGS-SVLLDTVditdpslvsIGDGAVIAEGallqSHeVRNSIlrlqpirIGRNCSVGPYAV 1419
Cdd:cd03353 28 VILEGKTVIGE-----DCVIGPnCVIKDST---------IGDGVVIKAS----SV-IEGAV-------IGNGATVGPFAH 81
|
90
....*....|...
gi 1917948728 1420 VQKGSVLREGAEV 1432
Cdd:cd03353 82 LRPGTVLGEGVHI 94
|
|
| LbH_LpxD |
cd03352 |
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ... |
1606-1698 |
3.35e-03 |
|
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
Pssm-ID: 100043 [Multi-domain] Cd Length: 205 Bit Score: 41.24 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917948728 1606 AKVGRYCSIRAinpiadprMVSIGAGVHLGDFSRiitgfysqsgyIQGNVDIKDNSVTGSQSLILPGSVVEKDVILGAis 1685
Cdd:cd03352 2 AKIGENVSIGP--------NAVIGEGVVIGDGVV-----------IGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGD-- 60
|
90
....*....|...
gi 1917948728 1686 vapvNSVLQSGGV 1698
Cdd:cd03352 61 ----RVIIHSGAV 69
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
23-59 |
4.11e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.42 E-value: 4.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEKHKSVGG 59
Cdd:PRK12778 433 KVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGG 468
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
26-58 |
4.24e-03 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 41.54 E-value: 4.24e-03
10 20 30
....*....|....*....|....*....|...
gi 1917948728 26 IVGGGPSGLSAAYALAKLGYRdITVMEKHKSVG 58
Cdd:TIGR02032 5 VVGAGPAGASAAYRLADKGLR-VLLLEKKSFPR 36
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|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
29-58 |
4.83e-03 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 41.49 E-value: 4.83e-03
10 20 30
....*....|....*....|....*....|
gi 1917948728 29 GGPSGLSAAYALAKLGYrDITVMEKHKSVG 58
Cdd:COG0644 1 AGPAGSAAARRLARAGL-SVLLLEKGSFPG 29
|
|
| NAD_binding_9 |
pfam13454 |
FAD-NAD(P)-binding; |
25-60 |
5.57e-03 |
|
FAD-NAD(P)-binding;
Pssm-ID: 433222 [Multi-domain] Cd Length: 155 Bit Score: 39.57 E-value: 5.57e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1917948728 25 GIVGGGPSGLSAAYALAKLGYR---DITVMEKHKSVGGM 60
Cdd:pfam13454 1 AIVGGGPSGLALLERLLARAPKrplEITLFDPSPPGAGG 39
|
|
| PRK08401 |
PRK08401 |
L-aspartate oxidase; Provisional |
21-51 |
7.09e-03 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236259 [Multi-domain] Cd Length: 466 Bit Score: 41.33 E-value: 7.09e-03
10 20 30
....*....|....*....|....*....|.
gi 1917948728 21 DTRIGIVGGGPSGLSAAYALAKLGYrDITVM 51
Cdd:PRK08401 1 MMKVGIVGGGLAGLTAAISLAKKGF-DVTII 30
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
661-710 |
7.39e-03 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 41.23 E-value: 7.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1917948728 661 PASNIAFQSE--------SQPDDLCFLQFTSGSTSDAKGVMITHGGLIHNVKLMRRRY 710
Cdd:cd17648 73 PDERIQFILEdtgarvviTNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERY 130
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
23-58 |
7.43e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 41.16 E-value: 7.43e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1917948728 23 RIGIVGGGPSGLSAAYALAKLGYrDITVMEK-HKSVG 58
Cdd:PRK12831 142 KVAVIGSGPAGLTCAGDLAKMGY-DVTIFEAlHEPGG 177
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
22-61 |
8.45e-03 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 41.00 E-value: 8.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1917948728 22 TRIGIVGGGPSGLSAAYALAKLGyRDITVMEKhKSVGGMC 61
Cdd:PRK07845 2 TRIVIIGGGPGGYEAALVAAQLG-ADVTVIER-DGLGGAA 39
|
|
|