|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
309-883 |
0e+00 |
|
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: 784.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 309 LYTLLNCRGAIANSLTCVQLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIA 387
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 388 TTLPTVKMivEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA-----QICKPCNPDTLAYLDFSV 462
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 463 STTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAV 542
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 543 SQYKVRDTFCSYSVMELCTKGLGSQTESLKARGLDLSRVRTCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGCRV 622
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 623 NLAICLqphrlwtlaeQGTSGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHL 702
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 703 GEIWVHSAHNASGYFTIYGDESLQSDHFNS-RLSFGDTQTIWARTGYLGFLRRTELTDANGERHDALYVVGALDEAMELR 781
Cdd:cd05905 389 GEIWVNSPANASGYFLLDGETNDTFKVFPStRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 782 GMRYHPIDIETSVIRAHKSVTECAVFTWTNLLVVVVELD-GSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDIGVIPINS 860
Cdd:cd05905 469 GLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNP 548
|
570 580
....*....|....*....|...
gi 767959951 861 RGEKQRMHLRDGFLADQLDPIYV 883
Cdd:cd05905 549 LGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1-233 |
3.71e-95 |
|
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: 310.43 E-value: 3.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 1 MHGLTYGVIRVDSEEKLSVLTVQDVGLVMPGAIMCSVKPDGVPqLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEVFP 80
Cdd:cd05905 339 MRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 81 MTSSGAPISEYPFIRTGLLGFVGPG----------GLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPmkfvYRGRIAV 150
Cdd:cd05905 418 STRLSTGITNNSYARTGLLGFLRPTkctdlnveehDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAV 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 151 FSVTvlhdERIVIVAEQRPDStEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHP 230
Cdd:cd05905 494 FSIT----GLVVVVAEQPPGS-EEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHP 568
|
...
gi 767959951 231 CNV 233
Cdd:cd05905 569 IYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
299-841 |
4.10e-71 |
|
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: 244.84 E-value: 4.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 299 WRAQTTPDHILYTLLNCRGAIANSLTCVQLHKRAEKIAVMLmeRGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITV 378
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 379 RPPHPqniATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKPcNPDTLAYL 458
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSP-DPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 459 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALW 538
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 539 LLAVSQYkvRDTFcsySVM-----ELCTKglgsQTESLKARGLDLSRVRTCVVVAEeRPRIALTQSFSKLFKDLGLHPRA 613
Cdd:cd05931 235 LRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGAE-PVRPATLRRFAEAFAPFGFRPEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 614 VSTSFGcrvnlaiclqphrlwtLAEQ------GTSGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGVRII 687
Cdd:cd05931 305 FRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 688 IANPETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRLSFGDtqTIWARTGYLGFLrrteltdANGErhda 767
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVRGPSVASGYW---GRPEATAETFGALAATDE--GGWLRTGDLGFL-------HDGE---- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 768 LYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTE--CAVFTW----TNLLVVVVELDGSeQEALDLVPLVTNV---VL 838
Cdd:cd05931 432 LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIraaVA 510
|
...
gi 767959951 839 EEH 841
Cdd:cd05931 511 REH 513
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
297-781 |
4.36e-58 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 204.85 E-value: 4.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 297 LQWRAQTTPDHILYTllncrGAIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPI 376
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 377 TVRPphpqniATTLPTVKMIVEVSRSACLMTTQlICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICK-------- 448
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDD-ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAkpadvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 449 ---PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCE----LYPSREVAICLDPYCGLGFVLWCLCSVYSGH 521
Cdd:pfam00501 148 pppPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 522 QSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSVMELCtkglgsqTESLKARGLDLSRVRTCVVVAeERPRIALTQSFS 601
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 602 KLFkdlglhPRAVSTSFGcrvnlaiclqphrlwtLAEqgTSGPdptTVYVDMRALRHDRVRLVergsphslplmesGKIL 681
Cdd:pfam00501 299 ELF------GGALVNGYG----------------LTE--TTGV---VTTPLPLDEDLRSLGSV-------------GRPL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 682 PGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDAN 761
Cdd:pfam00501 339 PGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DED 401
|
490 500
....*....|....*....|
gi 767959951 762 GErhdaLYVVGALDEAMELR 781
Cdd:pfam00501 402 GY----LEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
454-828 |
5.20e-38 |
|
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: 145.12 E-value: 5.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 454 TLAYLDFSVSTTGMLAGVKMSH---AATSAFCRSIKlqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSe 530
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrnlLAAAAALAASG----GLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 531 letNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPrIALTQSFSKLfkdlglh 610
Cdd:cd04433 76 ---DPEAALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEA------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 611 pravstsFGCRVnlaiclqpHRLWTLAEqgtSGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVRIIIAN 690
Cdd:cd04433 138 -------PGIKL--------VNGYGLTE---TGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 691 PETkGPLGDSHLGEIWVHSAHNASGYFTiygdeslqsdhfNSRLSFGDTQTIWARTGYLGFLrrteltDANGErhdaLYV 770
Cdd:cd04433 184 PDG-GELPPGEIGELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL------DEDGY----LYI 240
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767959951 771 VGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAVF-----TWTNLLVVVVELDGSEQEALD 828
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
293-881 |
9.80e-36 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 147.62 E-value: 9.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 293 LSEVLQWRAQTTPDHILYTLLNCRGAIANSLTCVQLHKRAEKIAVMLMERGHLqdGDHVALVYPPGIDLIAAFYGCLYAG 372
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 373 CV------PITVRPPHPQNIATtlptvkmIVEVSRSACLMTTQLICKLLRSREAAAAVDVrtwPLILDTDDLPKKRPAQI 446
Cdd:PRK05691 89 VIavpaypPESARRHHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPALAEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 447 CKP-CNPDTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsiklqCELYPSREVAICLDP----------YCGLGFVLWCLC 515
Cdd:PRK05691 159 QEPaLQPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 516 SVYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGsqtESLKARgLDLSRVRtcVVVAEERP-RI 594
Cdd:PRK05691 231 PIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVS---ESALER-LDLSRWR--VAYSGSEPiRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 595 ALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQ------GTSGPDPTTVYVDMRALRHDRVRLVErGS 668
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYG----------------LAEAtlfvsgGRRGQGIPALELDAEALARNRAEPGT-GS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 669 phslPLMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgDTQTiWARTGY 748
Cdd:PRK05691 368 ----VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGY---WRNPEASAKTFVEH----DGRT-WLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 749 LGFLRRTEltdangerhdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTE--CAVFTWTNL----LVVVVELDGS 822
Cdd:PRK05691 436 LGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKgrVAAFAVNHQgeegIGIAAEISRS 504
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767959951 823 EQEAL---DLVPLVTNVVLEEHYLIVGVVVVVDIGVIPINSRGEKQRMHLRDGFLADQLDPI 881
Cdd:PRK05691 505 VQKILppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDSY 566
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
296-837 |
1.40e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 137.00 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 296 VLQWRAQTTPDHILYTLLNCR---GAIANSLTCVQLHKRAEKIAVMLmeRGHLQDGDHVALVYPPGIDLIAAFYGCLYAG 372
Cdd:PRK05850 6 LLRERASLQPDDAAFTFIDYEqdpAGVAETLTWSQLYRRTLNVAEEL--RRHGSTGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 373 CVPITVRPPH----------------PQNIATTLPTVKMIVEVSRSACLMTTQLIckllrsreaaAAVDVrtwpLILDTD 436
Cdd:PRK05850 84 LIAVPLSVPQggahdervsavlrdtsPSVVLTTSAVVDDVTEYVAPQPGQSAPPV----------IEVDL----LDLDSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 437 DLPKKRPAQIckpcnPDTlAYLDFSVSTTGMLAGVKMSHAATSAFCRsiKLQCELYPSREVAICLD-------P-YCGLG 508
Cdd:PRK05850 150 RGSDARPRDL-----PST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 509 FVLWCLCSVYSGHQSILIPPSELETNPALW--LLAVSQYkvrdtfcSYSV-----MELCTKglgsQTESLKARGLDLSRV 581
Cdd:PRK05850 222 LVLGVCAPILGGCPAVLTSPVAFLQRPARWmqLLASNPH-------AFSAapnfaFELAVR----KTSDDDMAGLDLGGV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 582 RTcVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAE------QGTSGPDPTTVYVDMRA 655
Cdd:PRK05850 291 LG-IISGSERVHPATLKRFADRFAPFNLRETAIRPSYG----------------LAEatvyvaTREPGQPPESVRFDYEK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 656 LRHDRVR---------LVERGSPHSlplmesgkilPGVRIIiaNPETKGPLGDSHLGEIWVHSAHNASGYFTiyGDESLQ 726
Cdd:PRK05850 354 LSAGHAKrcetgggtpLVSYGSPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAAGYWQ--KPEETE 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 727 SDhFNSRL---SFGDTQTIWARTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVirahKSVT- 802
Cdd:PRK05850 420 RT-FGATLvdpSPGTPEGPWLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATI----QEITg 483
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 767959951 803 -ECAVFT----WTNLLVVVVEL---DGSEQEALDLVPLVTNVV 837
Cdd:PRK05850 484 gRVAAISvpddGTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
293-830 |
7.23e-31 |
|
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: 126.85 E-value: 7.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 293 LSEVLQWRAQTTPDHILYTLLNCRgaiansLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 372
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 373 CVPITVrpphpqNIATTLPTVKMIVEVSRSACLMTtqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnp 452
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 453 dtlAYLDFSvS-TTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPpsel 531
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP---- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 532 ETNPALWLLAVSQYKVrdTFCSYS---VMELCtkglgsqtESLKARGLDLSRVRTCVVVAEerpriALTQSFSKLFKDLg 608
Cdd:COG0318 175 RFDPERVLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 609 lhpravstsFGCRVnlaiclqpHRLWTLAEqgtSGPDPTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVRIII 688
Cdd:COG0318 239 ---------FGVRI--------VEGYGLTE---TSPVVTVNPEDPGERRPGSV----------------GRPLPGVEVRI 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 689 ANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLqsdhfnSRLSFGDTqtiWARTGYLGFLrrteltDANGErhdaL 768
Cdd:COG0318 283 VDEDGR-ELPPGEVGEIVVRGPNVMKGY---WNDPEA------TAEAFRDG---WLRTGDLGRL------DEDGY----L 339
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767959951 769 YVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLVVVVEL-DGSEQEALDLV 830
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELR 406
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
320-801 |
2.40e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 112.14 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 320 ANSLTCVQLHKRAEKIAVMLMErgHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNIATTLPTVkmiVEV 399
Cdd:PRK12476 66 AVELTWTQLGVRLRAVGARLQQ--VAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHAERLDTA---LRD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 400 SRSACLMTTQLICKLLRSREAAAAVDVRtwPLILDTDDLPKkRPAQICKPCNPDT--LAYLDFSVSTTGMLAGVKMSHAA 477
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPD-SAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 478 TSA----FCRSIKLqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHqSILIPPSELETNPALWLLAVSQ-YKVRDTFC 552
Cdd:PRK12476 218 VGTnlvqMILSIDL---LDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVVT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 553 SYS--VMELCT-KGLGSQTEslkarGLDLSRVrtCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclq 629
Cdd:PRK12476 294 AAPnfAYEWAAqRGLPAEGD-----DIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG---------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 630 phrlwtLAEQ----GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHLG 703
Cdd:PRK12476 357 ------IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 704 EIWVHSAHNASGYFTiYGDESLQSDH--FNSRLSFG------DTQTIWARTGYLGFLRrteltdaNGErhdaLYVVGALD 775
Cdd:PRK12476 431 EIWLHGDNIGRGYWG-RPEETERTFGakLQSRLAEGshadgaADDGTWLRTGDLGVYL-------DGE----LYITGRIA 498
|
490 500
....*....|....*....|....*.
gi 767959951 776 EAMELRGMRYHPIDIETSVIRAHKSV 801
Cdd:PRK12476 499 DLIVIDGRNHYPQDIEATVAEASPMV 524
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
293-816 |
3.81e-25 |
|
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: 110.83 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 293 LSEVLQWRAQTTPDHILYTllncrgaIANSLTCV-----QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYG 367
Cdd:cd05906 12 LLELLLRAAERGPTKGITY-------IDADGSEEfqsyqDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 368 CLYAGCVPITVRPPHP-QNIATTLPTVKMIVEVSRSA-CLMTTQLICKLLRSREAA--AAVDVRTWPLILDTDDLPKKRP 443
Cdd:cd05906 84 CVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPvVLTDAELVAEFAGLETLSglPGIRVLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 444 AQickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSiKLQCELYPSREVA---ICLDPYCGLGFVlwCLCSVYSG 520
Cdd:cd05906 164 SR------PDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 521 HQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSvmeLCTKgLGSQTESLKARGLDLSRVRtCVVVAEERPRIALTQSF 600
Cdd:cd05906 235 CQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 601 SKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQGtSGpdpTTVYVDMRALRHdrvrlvergsPHSLPLMESGKI 680
Cdd:cd05906 310 LRLLEPYGLPPDAIRPAFG----------------MTETC-SG---VIYSRSFPTYDH----------SQALEFVSLGRP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 681 LPGVRIIIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltda 760
Cdd:cd05906 360 IPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFLD------- 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767959951 761 NGErhdaLYVVGALDEAMELRGMRYHPIDIETSV----IRAHKSVTECAVF---TWTNLLVVV 816
Cdd:cd05906 421 NGN----LTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRdpgAETEELAIF 479
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
283-826 |
1.02e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 109.71 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 283 DNDQARK---FLFLSEVLQWRAQTTPDHILYTLlncRGAIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGI 359
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFYDR---RGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 360 DLIAAFYGCLYAGCVPITVrpPHPQNI---ATTLPTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTD 436
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV-----NEATHGNPLLHVLSHA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 437 DLpKKRPAQICK--PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQ-CELYPSREVAICLDPYCGLGFVlWC 513
Cdd:PRK09192 159 WF-KALPEADVAlpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGLV-GF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 514 LCSVYSGHQSI-LIPPSELETNPALWLLAVSqyKVRDTFcSYSV---MELCTKGLGSQTESlkarGLDLSRVRTCVVVAE 589
Cdd:PRK09192 237 LLTPVATQLSVdYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIGAD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 590 E-RPRIalTQSFSKLFKDLGLHPRAVSTSFG-CRVNLAICLQPHrlwtlaEQGtsgpdpttvyvdMRALRHDRVRLVERG 667
Cdd:PRK09192 310 MiRPDV--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSFSPL------GSG------------IVVEEVDRDRLEYQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 668 spHSLPLMES----------GKILPGVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESlqsdhfnsrlsfg 737
Cdd:PRK09192 370 --KAVAPGAEtrrvrtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYF---RDEE------------- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 738 DTQTI----WARTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSV-----IRAHksvtECAVFT 808
Cdd:PRK09192 431 SQDVLaadgWLDTGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAeqepeLRSG----DAAAFS 495
|
570 580
....*....|....*....|..
gi 767959951 809 WTN----LLVVVVELDGSEQEA 826
Cdd:PRK09192 496 IAQengeKIVLLVQCRISDEER 517
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
297-801 |
1.21e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.82 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 297 LQWRAQTTPDHILYTLLNC---RGAIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAGC 373
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDFsteRDGVARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 374 VPITVRPPHPQNIATTLPTVkmIVEVSRSACLMTT---QLICKLLRSREAAAAvdvrtwPLILDTDDLPKKRPAQICKP- 449
Cdd:PRK07769 105 IAVPLFDPAEPGHVGRLHAV--LDDCTPSAILTTTdsaEGVRKFFRARPAKER------PRVIAVDAVPDEVGATWVPPe 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 450 CNPDTLAYLDFSVSTTGMLAGVKMSH--AATSAF--CRSIKLQcelYPSREVAiCLDPYCGLGFVLWCLCSVYSGHQSIL 525
Cdd:PRK07769 177 ANEDTIAYLQYTSGSTRIPAGVQITHlnLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLPALLGHYITFM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 526 IPPSELEtNPALWLLAVSQyKVRDTFCSYSV-----MELCT-KGLGSQTESlkarGLDLSRVRtCVVVAEERPRIALTQS 599
Cdd:PRK07769 253 SPAAFVR-RPGRWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKDGEP----PLDLSNVK-GLLNGSEPVSPASMRK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 600 FSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQ----GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLP 673
Cdd:PRK07769 326 FNEAFAPYGLPPTAIKPSYG----------------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 674 LMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYG--DESLQSDH--FNSRLSFGDTQ-----TIWA 744
Cdd:PRK07769 390 QVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGY---WGkpEETAATFQniLKSRLSESHAEgapddALWV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 767959951 745 RTGYLGflrrtelTDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSV 801
Cdd:PRK07769 467 RTGDYG-------VYFDGE----LYITGRVKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
37-224 |
6.27e-24 |
|
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: 106.94 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 37 VKPDGVpQLCRTDEIGELCVC--AVATGtsYYGLSGMTKNTFEVFpmtssgAPISEYPFIRTGLLGFVGPGGLvFVVGKM 114
Cdd:cd05931 369 VDPETG-RELPDGEVGEIWVRgpSVASG--YWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRL 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 115 DGLMVVSGRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVG 194
Cdd:cd05931 439 KDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVA 516
|
170 180 190
....*....|....*....|....*....|
gi 767959951 195 VYCLALVPANTLPKTPLGGIHLSETKQLFL 224
Cdd:cd05931 517 PADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
327-806 |
1.04e-22 |
|
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: 101.57 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 327 QLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITvrPPHPQN-IATtlptvkmIVEVSRSA 403
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAayVPLD--PAYPAErLAF-------ILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 404 CLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAqickPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCR 483
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDA----PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 484 SIklqCELYPSREVAICLDpYCGLGF------VLWCLcsvYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVM 557
Cdd:TIGR01733 151 WL---ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 558 ELCtkglgsqtesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLglhpravstsfgcrvnlaiclqphRLWTla 637
Cdd:TIGR01733 224 ALL----------AAALPPALASLRL-VILGGEALTPALVDRWRARGPGA------------------------RLIN-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 638 eqgTSGPDPTTVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYF 717
Cdd:TIGR01733 267 ---LYGPTETTVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGYL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 718 tiyGDESLQSDHFNSRLSFGDTQTIWARTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRA 797
Cdd:TIGR01733 335 ---NRPELTAERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLR 400
|
....*....
gi 767959951 798 HKSVTECAV 806
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
322-807 |
4.92e-22 |
|
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: 100.75 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 322 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVpitVRPPHPQNIATTL--------PTV 393
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGI---FSAANPIYTADELahqlkiskPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 394 kMIVEVSrsaCLMTTQLICK---------LLRSREAAAA--VDVRTWPLILDTDDLPkkrpaqICKPCNPDTLAYLDFSV 462
Cdd:cd05911 86 -IFTDPD---GLEKVKEAAKelgpkdkiiVLDDKPDGVLsiEDLLSPTLGEEDEDLP------PPLKDGKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 463 STTGMLAGVKMSHaatSAFCRSIKLQC----ELYPSREVAICLDPY---CGLgfvLWCLCSVYSGHQSILIPpselETNP 535
Cdd:cd05911 156 GTTGLPKGVCLSH---RNLIANLSQVQtflyGNDGSNDVILGFLPLyhiYGL---FTTLASLLNGATVIIMP----KFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 536 ALWLLAVSQYKVRDTFCSYSVMELctkgLGSQTESLKArglDLSRVRTCVVVAEerpriALTQSFSKLFKdlglhpravs 615
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGGA-----PLSKELQELLA---------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 616 tsfgCRVNLAICLQphrLWTLAEqgTSGPDPTTVYVDmralrhdrvrlVERGSphslplmeSGKILPGVRIIIANPETKG 695
Cdd:cd05911 284 ----KRFPNATIKQ---GYGMTE--TGGILTVNPDGD-----------DKPGS--------VGRLLPNVEAKIVDDDGKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 696 PLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDANGErhdaLYVVGALD 775
Cdd:cd05911 336 SLGPNEPGEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYF------DEDGY----LYIVDRKK 394
|
490 500 510
....*....|....*....|....*....|..
gi 767959951 776 EAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 807
Cdd:cd05911 395 ELIKYKGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
320-809 |
5.67e-19 |
|
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: 91.28 E-value: 5.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 320 ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPItvrpphPQNIATTLPTVKMIVEV 399
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 400 SRSACLMTTQLICKLLRSREAAAAVDVRT----------WPLILDTDDLPKKRPAQICKPCNPDTLAYLDFSVSTTGMLA 469
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 470 GVKMSHAatsafcrSIKLQCELYPSREVAICLDPYC----------GLGFVLWCLCSVysGHQSILIPpsELETnPALWL 539
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMP--ERPT-PAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 540 LAVSQYKvRDTFcsYSVMELCTKGLGSqtESLKARglDLSRVRTCVVVAEerpriALTQSFSKLFKDLglhpravstsFG 619
Cdd:cd05959 248 KRIRRYR-PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGE-----ALPAEVGERWKAR----------FG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 620 CRVnlaiclqphrlwtlaEQGTSGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVRIIIANpETKGPLGD 699
Cdd:cd05959 306 LDI---------------LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGDVAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 700 SHLGEIWVHSAHNASGYFTIYGDeslqsdhfnSRLSFgdtQTIWARTGYlGFLRrteltDANGerhdALYVVGALDEAME 779
Cdd:cd05959 356 GEPGELYVRGPSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADDMLK 413
|
490 500 510
....*....|....*....|....*....|
gi 767959951 780 LRGMRYHPIDIEtSVIRAHKSVTECAVFTW 809
Cdd:cd05959 414 VSGIWVSPFEVE-SALVQHPAVLEAAVVGV 442
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
46-214 |
2.04e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 86.92 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 46 CRTDEIGELCVCA--VATGtsYYGLSGMTKNTFE---VFPmtSSGAPISeyPFIRTGLLGFVGPGGLvFVVGKMDGLMVV 120
Cdd:PRK05850 392 CPAGTVGEIWVHGdnVAAG--YWQKPEETERTFGatlVDP--SPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIV 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 121 SGRRHNADDIVATalavepMKFVYRGRIAVFSVTVLHDERIVIVAE-QRPDSTEEDSFQWM----SRVLQAIDSIHQVGV 195
Cdd:PRK05850 465 DGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSV 538
|
170
....*....|....*....
gi 767959951 196 YCLALVPANTLPKTPLGGI 214
Cdd:PRK05850 539 ADLVLVAPGSIPITTSGKI 557
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
322-829 |
6.26e-17 |
|
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: 84.50 E-value: 6.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 322 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSR 401
Cdd:cd05930 12 SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE------RLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 402 SACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 481
Cdd:cd05930 85 AKLVLTD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 482 CRSIKlqcELYP--SREVAICLDPYcglGF------VLWCLCsvySGHQsILIPPSELETNPALWLLAVSQYKVRDTFCS 553
Cdd:cd05930 122 LLWMQ---EAYPltPGDRVLQFTSF---SFdvsvweIFGALL---AGAT-LVVLPEEVRKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 554 YSVMELCTKGLGSQteslkarglDLSRVRTcVVVAEERPRIALTQSFSKLFKDlglhpravstsfgcrvnlaiclqpHRL 633
Cdd:cd05930 192 PSLLRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPG------------------------ARL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 634 WTLaeqgtSGPDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNA 713
Cdd:cd05930 238 VNL-----YGPTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 714 SGYftiYGDESLQSDHFNsRLSFGDTQTIWaRTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIETs 793
Cdd:cd05930 303 RGY---LNRPELTAERFV-PNPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA- 366
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 767959951 794 VIRAHKSVTECAVFTWTN------LLVVVVELDGSEQEALDL 829
Cdd:cd05930 367 ALLAHPGVREAAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
39-230 |
6.64e-16 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 82.10 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 39 PDGvpqlcrtdEIGELCVCAVATGTSYYGLSGMTKNTFEV-----FPMTS--SGAPISEyPFIRTGLLGFVGPGGLvFVV 111
Cdd:PRK12476 425 PDG--------EVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDG-TWLRTGDLGVYLDGEL-YIT 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 112 GKMDGLMVVSGRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIH 191
Cdd:PRK12476 495 GRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRH 572
|
170 180 190
....*....|....*....|....*....|....*....
gi 767959951 192 QVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHP 230
Cdd:PRK12476 573 GLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
327-806 |
5.46e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 75.57 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 327 QLHKRAEKIAVMLMERGhlqDGDHVALVYPPGIDLIAAFYGCLYAG----CVPITVRPPHPQNIA-TTLptvkmivevSR 401
Cdd:PRK05851 36 EVHGRAENVAARLLDRD---RPGAVGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWAdATL---------TR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 402 SACLMTTQLIC-----KLLRSREAAAAV-DVRTWPlildtddlPKKRPAQIcKPCNPDTLAYLDFSVSTTGMLAGVKMSH 475
Cdd:PRK05851 104 FAGIGVRTVLShgshlERLRAVDSSVTVhDLATAA--------HTNRSASL-TPPDSGGPAVLQGTAGSTGTPRTAILSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 476 AATSAFCRSIKLQCELYPSREVAICLDPY---CGLGFVLwclCSVYSGHQSILIPPSELETNPALWLLAVSQykVRDTFC 552
Cdd:PRK05851 175 GAVLSNLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSD--SRATLT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 553 SYSVMELCTKGLGSQteslKARGLDLSRVRTCVVVAEerP-RIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqph 631
Cdd:PRK05851 250 AAPNFAYNLIGKYAR----RVSDVDLGALRVALNGGE--PvDCDGFERFATAMAPFGFDAGAAAPSYG------------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 632 rlwtLAEQ--GTSGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVRIIIANPETKGPLGDSHLGEIWVHS 709
Cdd:PRK05851 312 ----LAEStcAVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 710 AHNASGYFtiyGDESLQSDHfnsrlsfgdtqtiWARTGYLGFlrrteLTDangerhDALYVVGALDEAMELRGMRYHPID 789
Cdd:PRK05851 380 ASMMSGYL---GQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTE 432
|
490
....*....|....*..
gi 767959951 790 IETSVIRAhKSVTECAV 806
Cdd:PRK05851 433 IERVAAQV-RGVREGAV 448
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
39-228 |
1.73e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 74.38 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 39 PDGvpqlcrtdEIGELCVCAVATGTSYYGLSGMTKNTFE------VFPMTSSGAPiSEYPFIRTGLLGFVGPGGLvFVVG 112
Cdd:PRK07769 414 PDG--------QIGEIWLHGNNIGTGYWGKPEETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITG 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 113 KMDGLMVVSGRRHNADDIVATALavEPMKFVYRGRIAVFSV-------TVLHD-------------ERIVIVAEQRPDST 172
Cdd:PRK07769 484 RVKDLVIIDGRNHYPQDLEYTAQ--EATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAH 561
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767959951 173 EEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSL 228
Cdd:PRK07769 562 KLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
451-791 |
5.22e-13 |
|
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: 72.52 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 451 NPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSE 530
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 531 LETNPALWLLAVSQYKVRDTFCSysvmELCTKGLGSQTESLKARGLDLSRVRTCVVVAEErprIA--LTQSFSKLFKDLG 608
Cdd:cd05908 184 FIRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 609 LHPRAVSTSFGcrvnlaiclqphrlwtLAEQ--GTSGPDP----TTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKIL 681
Cdd:cd05908 257 LKRNAILPVYG----------------LAEAsvGASLPKAqspfKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 682 PGVRIIIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltdaN 761
Cdd:cd05908 321 DETDIRICDEDNKI-LPDGYIGHIQIRGKNVTPGY---YNNPEATAKVF--------TDDGWLKTGDLGFIR-------N 381
|
330 340 350
....*....|....*....|....*....|
gi 767959951 762 GErhdaLYVVGALDEAMELRGMRYHPIDIE 791
Cdd:cd05908 382 GR----LVITGREKDIIFVNGQNVYPHDIE 407
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
293-527 |
4.62e-12 |
|
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: 69.13 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 293 LSEVLQWRAQTTPDHilyTLLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 372
Cdd:cd05936 1 LADLLEEAARRFPDK---TALIFMGR---KLTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 373 CVPITVRPphpqniattlptvkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQickpcNP 452
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVAL-----TP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 453 DTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsIKLQC-----ELYPSREVAICLDP-YCGLGFVLWCLCSVYSGHQSILI 526
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 767959951 527 P 527
Cdd:cd05936 201 P 201
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
322-806 |
6.36e-12 |
|
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: 68.80 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 322 SLTCVQLHKRAEKIAVMLMERGHLQdGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPphpqniATTLPTVKMIVEVSR 401
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 402 SACLMTT-QLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKP-CNPDTLAYLDFSVSTTGMLAGVKMSH---- 475
Cdd:cd05904 105 AKLAFTTaELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVvIKQDDVAALLYSSGTTGRSKGVMLTHrnli 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 476 AATSAFCRSIKLQCElypSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPSELETnpalWLLAVSQYKVRDTFCSY 554
Cdd:cd05904 185 AMVAQFVAGEGSNSD---SEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVTHLPVVP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 555 SVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPRiALTQSFSKLFKDlglhpravstsfgcrVNLaicLQPHRLW 634
Cdd:cd05904 258 PIVLALVK-------SPIVDKYDLSSLRQIMSGAAPLGK-ELIEAFRAKFPN---------------VDL---GQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 635 TLAEQGTSGPDPTtvyvdmralrHDRVRlveRGSphslplmeSGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNAS 714
Cdd:cd05904 312 ESTGVVAMCFAPE----------KDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 715 GYFtiyGDESlqsdhfnsrlsfgDTQ-TI----WARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPID 789
Cdd:cd05904 371 GYL---NNPE-------------ATAaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQVAPAE 424
|
490
....*....|....*..
gi 767959951 790 IEtSVIRAHKSVTECAV 806
Cdd:cd05904 425 LE-ALLLSHPEILDAAV 440
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
301-832 |
3.53e-11 |
|
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: 66.50 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 301 AQTTPDHILYTllnCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITV 378
Cdd:cd05945 1 AAANPDRPAVV---EGGR---TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 379 RPPHPQniattlptVKMIVEVSRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYL 458
Cdd:cd05945 74 SSPAER--------IREILDAAKPALLIAD-------------------------------------------GDDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 459 DFSVSTTGMLAGVKMSHAATSAFCRSIkLQCELYPSREVAICLDPYcglGF---VLWCLCSVYSGhQSILIPPSELETNP 535
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPF---SFdlsVMDLYPALASG-ATLVPVPRDATADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 536 ALWLLAVSQYKVRDTFCSYSVMELCTkGLGSQTESLkargldLSRVRTCVVVAEERPrIALTQSFSKLFkdlglhPravs 615
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPES------LPSLRHFLFCGEVLP-HKTARALQQRF------P---- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 616 tsfGCRV-NlaiclqphrlwtlaeqgTSGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVRIIIANPETK 694
Cdd:cd05945 240 ---DARIyN-----------------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILDEDGR 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 695 gPLGDSHLGEIWVHSAHNASGYFtiyGDEslqsDHFNSRLSFGDTQTiWARTGYLGFLrrteltDANGErhdaLYVVGAL 774
Cdd:cd05945 292 -PVPPGEKGELVISGPSVSKGYL---NNP----EKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRL 352
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767959951 775 DEAMELRGMRYHPIDIETSViRAHKSVTECAVFTWTNL-----LVVVVELDGSEqEALDLVPL 832
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
301-806 |
9.29e-11 |
|
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: 65.06 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 301 AQTTPDHILytlLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG--CVPITV 378
Cdd:cd17651 5 AARTPDAPA---LVAEGR---RLTYAELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 379 RPPhPQNIAttlptvkMIVEVSRSACLMTTQlickllrsREAAAAVDVRTWPLILDTDDLPKKRPAQICKPCNPDTLAYL 458
Cdd:cd17651 78 AYP-AERLA-------FMLADAGPVLVLTHP--------ALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 459 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF--VLWCLCSVYSGHQSILIPPSELETNPA 536
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTL----QFAGLGFdvSVQEIFSTLCAGATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 537 LWLLAVSQYKVRDTFCSYSVME-LCtkglgsqtESLKARGLDLSRVRtCVVVAEERprialtqsfsklfkdLGLHPRavs 615
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGEQ---------------LVLTED--- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 616 tsfgcrvnlaiclqpHRLWTLAEQG-----TSGPDPTTVyVDMRALRHDRVRlveRGSPHSLplmesGKILPGVRIIIAN 690
Cdd:cd17651 271 ---------------LREFCAGLPGlrlhnHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 691 PETKgPLGDSHLGEIWVHSAHNASGYFTIYG--DESLQSDHF--NSRLSfgdtqtiwaRTGYLGflRRteltDANGErhd 766
Cdd:cd17651 327 AALR-PVPPGVPGELYIGGAGLARGYLNRPEltAERFVPDPFvpGARMY---------RTGDLA--RW----LPDGE--- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 767959951 767 aLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 806
Cdd:cd17651 388 -LEFLGRADDQVKIRGFRIELGEIE-AALARHPGVREAVV 425
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
96-230 |
3.58e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.49 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 96 TGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATAlavEPMKFVYRGRIAVFSVTVLHDERIVIVAEQRPdSTEED 175
Cdd:PRK09192 443 TGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWIA---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEER 517
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767959951 176 SFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKTPLGGIHLSETKQLFLEGSLHP 230
Cdd:PRK09192 518 RGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
300-829 |
6.17e-10 |
|
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: 63.34 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 300 RAQTTPDHIlytllncrgAI---ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--V 374
Cdd:COG1020 485 QAARTPDAV---------AVvfgDQSLTYAELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 375 PITvrPPHPQN-IAttlptvkMIVEVSRSACLMTTQlickLLRSREAAAAVDVrtwpLILDTDDLPKKRPAQICKPCNPD 453
Cdd:COG1020 555 PLD--PAYPAErLA-------YMLEDAGARLVLTQS----ALAARLPELGVPV----LALDALALAAEPATNPPVPVTPD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 454 TLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF------VLWCLCsvySGHQSILIP 527
Cdd:COG1020 618 DLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL----QFASLSFdasvweIFGALL---SGATLVLAP 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 528 PsELETNPALWLLAVSQYKVrdtfcsySVMELcTKGLGSQTesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDL 607
Cdd:COG1020 691 P-EARRDPAALAELLARHRV-------TVLNL-TPSLLRAL--LDAAPEALPSLRL-VLVGGEALPPELVRRWRARLPGA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 608 GLHpravstsfgcrvNLAiclqphrlwtlaeqgtsGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVRII 687
Cdd:COG1020 759 RLV------------NLY-----------------GPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVY 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 688 IAnpetkgplgDSHL--------GEIWVHSAHNASGYFtiyGDESLQSDHF--NsrlSFGDTQTIWARTGYLGflRRTel 757
Cdd:COG1020 801 VL---------DAHLqpvpvgvpGELYIGGAGLARGYL---NRPELTAERFvaD---PFGFPGARLYRTGDLA--RWL-- 861
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767959951 758 tdANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVFTWTN-----LLVVVVELDGSEQEALDL 829
Cdd:COG1020 862 --PDGN----LEFLGRADDQVKIRGFRIELGEIE-AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAAL 931
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
322-547 |
1.22e-09 |
|
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: 61.52 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 322 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPhPQNIATTLptvkmiveV 399
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARREAIL--------A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 400 SRSACLMTTQLICkllrSREAAAAVDVRTWPLILD-TDDLPKKRPAQickpcnPDTLAYLDFSVSTTGMLAGVKMSHAAT 478
Cdd:cd12114 82 DAGARLVLTDGPD----AQLDVAVFDVLILDLDALaAPAPPPPVDVA------PDDLAYVIFTSGSTGTPKGVMISHRAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767959951 479 SAFCRSIKLQCELYPSREVaICLDPycgLGFVLwclcSVY------SGHQSILIPPSELETNPALWLLAVSQYKV 547
Cdd:cd12114 152 LNTILDINRRFAVGPDDRV-LALSS---LSFDL----SVYdifgalSAGATLVLPDEARRRDPAHWAELIERHGV 218
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
299-806 |
1.37e-09 |
|
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: 61.52 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 299 WRAQT--TPDH--ILYTllncrgaiANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 374
Cdd:cd17646 4 VAEQAarTPDApaVVDE--------GRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 375 PITVRPPHPQniattlPTVKMIVEVSRSACLMTTQlickllRSREAAAAVDVRTWPLILDTDDLPKKRPAQickPCNPDT 454
Cdd:cd17646 75 YLPLDPGYPA------DRLAYMLADAGPAVVLTTA------DLAARLPAGGDVALLGDEALAAPPATPPLV---PPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 455 LAYLDFSVSTTGMLAGVKMSHAatsAFCRSIKLQCELYP--SREVAICLDPycgLGF------VLWCLCsvySGhQSILI 526
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHA---GIVNRLLWMQDEYPlgPGDRVLQKTP---LSFdvsvweLFWPLV---AG-ARLVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 527 PPSELETNPALWLLAVSQYKVrdTFCSY--SVMELCtkglgsqteslkargLDLSRVRTC-----VVVAEErpriALTQS 599
Cdd:cd17646 210 ARPGGHRDPAYLAALIREHGV--TTCHFvpSMLRVF---------------LAEPAAGSCaslrrVFCSGE----ALPPE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 600 FSKLFKDLglhpravstsFGCRVnlaiclqpHRLWtlaeqgtsGPDPTTVYVDmralrHDRVRlvERGSPHSLPLmesGK 679
Cdd:cd17646 269 LAARFLAL----------PGAEL--------HNLY--------GPTEAAIDVT-----HWPVR--GPAETPSVPI---GR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 680 ILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHF-------NSRLSfgdtqtiwaRTGYLGfl 752
Cdd:cd17646 313 PVPNTRLYVLDDALR-PVPVGVPGELYLGGVQLARGY---LGRPALTAERFvpdpfgpGSRMY---------RTGDLA-- 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 767959951 753 RRTeltdANGerhdALYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAV 806
Cdd:cd17646 378 RWR----PDG----ALEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTHAVV 422
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
322-823 |
1.50e-09 |
|
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: 61.15 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 322 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSR 401
Cdd:cd12116 12 SLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 402 SACLMTTQlickllrSREAAAAVDVRTWPLILDTDDLPkkrPAQICKPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 481
Cdd:cd12116 85 PALVLTDD-------ALPDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 482 CRSIklqcelypsREvaicldpycglgfvlwclcsvysghqsilippsELETNPALWLLAVSQYkvrdTFcSYSVMEL-- 559
Cdd:cd12116 155 LHSM---------RE---------------------------------RLGLGPGDRLLAVTTY----AF-DISLLELll 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 560 ----------CTKGLGSQTESLKARgldLSRVRTCVVVAeerprialTQSFSKLFKDLGLHPRAvstsfGCRV------- 622
Cdd:cd12116 188 pllagarvviAPRETQRDPEALARL---IEAHSITVMQA--------TPATWRMLLDAGWQGRA-----GLTAlcggeal 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 623 --NLA--ICLQPHRLWTLaeqgtSGPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVRIIIANPETKgPLG 698
Cdd:cd12116 252 ppDLAarLLSRVGSLWNL-----YGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVLDAALR-PVP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 699 DSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWARTGYLgfLRRteltDANGErhdaLYVVGALDEAM 778
Cdd:cd12116 314 PGVPGELYIGGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR----RADGR----LEYLGRADGQV 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 767959951 779 ELRGMRYHPIDIETsVIRAHKSVTECAVFTWTN----LLVVVVELDGSE 823
Cdd:cd12116 380 KIRGHRIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
297-827 |
1.70e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.99 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 297 LQWRAQTTPDHILYTLLNCRGAIAN----SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 372
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGADGKlaydELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 373 CVPITVRP-------------PHPQ--------NIATTL-----PTVKMIVEVSRSACLMTTQLIcKLLRSREAAAAvdv 426
Cdd:PRK09274 91 AVPVLVDPgmgiknlkqclaeAQPDafigipkaHLARRLfgwgkPSVRRLVTVGGRLLWGGTTLA-TLLRDGAAAPF--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 427 rtwplildtddlpkkrpaqICKPCNPDTLAYLDFSVSTTGMLAGVKMSHaatSAFCRSIKLQCELYPSR--EVAIC---- 500
Cdd:PRK09274 167 -------------------PMADLAPDDMAAILFTSGSTGTPKGVVYTH---GMFEAQIEALREDYGIEpgEIDLPtfpl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 501 ---LDPYCGlgfvlwcLCSVysghqsilIPPSEL----ETNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKA 573
Cdd:PRK09274 225 falFGPALG-------MTSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGR-------YGEA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 574 RGLDLSRVRTcVVVAEERPRIALTQSFSKLfkdlgLHPRA-VSTSFGCRVNLAICLqphrlwtlaeqgtsgpdpttvyVD 652
Cdd:PRK09274 283 NGIKLPSLRR-VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS----------------------IE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 653 MRALRHDRVRLVERGSPHSLplmesGKILPGVRI-IIA---NP-----ETKgPLGDSHLGEIWVHSAHNASGYFtiygde 723
Cdd:PRK09274 335 SREILFATRAATDNGAGICV-----GRPVDGVEVrIIAisdAPipewdDAL-RLATGEIGEIVVAGPMVTRSYY------ 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 724 slQSDHFN--SRLSFGDTQtIWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSV 801
Cdd:PRK09274 403 --NRPEATrlAKIPDGQGD-VWHRMGDLGYL------DAQGR----LWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGV 468
|
570 580
....*....|....*....|....*.
gi 767959951 802 TECAvftwtnllVVVVELDGSEQEAL 827
Cdd:PRK09274 469 KRSA--------LVGVGVPGAQRPVL 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
323-831 |
4.33e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 323 LTCVQLHKRAEKIAVMLMERGHLQDGdHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRS 402
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEV-LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGA 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 403 ACLMTTQLICKLLRSREAAAAVDV---RTWplildtDDLPKKRPAqicKPCNPDTLAYLDFSVSTTGMLAGVKMSHAATS 479
Cdd:PRK12316 4650 ALLLTQSHLLQRLPIPDGLASLALdrdEDW------EGFPAHDPA---VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV 4720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 480 AFCRSIKLQCELYPSREVaICLDPYCGLGFVL---WCLCSvysgHQSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSV 556
Cdd:PRK12316 4721 NHLHATGERYELTPDDRV-LQFMSFSFDGSHEglyHPLIN----GASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVY 4794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 557 MELCTKGlgsqteslKARGLDLSRVRTCVVVAEERPRIALTQSFSKlfkdlglhpravstsfgcrvnlaicLQPHRLWTl 636
Cdd:PRK12316 4795 LQQLAEH--------AERDGEPPSLRVYCFGGEAVAQASYDLAWRA-------------------------LKPVYLFN- 4840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 637 aeqgTSGPDPTTVYVDMRALRhdrvrlveRGSPHSLPLMESGKILPGVRIII----ANPETKGPLGDSHLGEIWVhsahn 712
Cdd:PRK12316 4841 ----GYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVldgqLNPLPVGVAGELYLGGEGV----- 4903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 713 ASGYFTiygDESLQSDHFNSRlSFGDTQTIWARTGYLGFLRRTELTDangerhdalyVVGALDEAMELRGMRYHPIDIET 792
Cdd:PRK12316 4904 ARGYLE---RPALTAERFVPD-PFGAPGGRLYRTGDLARYRADGVID----------YLGRVDHQVKIRGFRIELGEIEA 4969
|
490 500 510
....*....|....*....|....*....|....*....
gi 767959951 793 SvIRAHKSVTECavftwtnlLVVVVELDGSEQEALDLVP 831
Cdd:PRK12316 4970 R-LREHPAVREA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
327-494 |
9.82e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 327 QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLM 406
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 407 T-TQLICKLLRSREAAAavdvrtwpLILDTD----DLPKKRPAQickPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 481
Cdd:PRK12316 2106 TqRHLLERLPLPAGVAR--------LPLDRDaewaDYPDTAPAV---QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170
....*....|...
gi 767959951 482 CRSIKLQCELYPS 494
Cdd:PRK12316 2175 CQAAGERYELSPA 2187
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
322-806 |
2.72e-07 |
|
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: 53.85 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 322 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPHPQNIAttlptvkmIVEV 399
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERIAF--------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 400 SRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATS 479
Cdd:cd17643 83 SGPSLLLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 480 AFCRSIKLQCELYPSREVAICldPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAVSQYKVrdtfcsySVMel 559
Cdd:cd17643 120 ALFAATQRWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV-------TVL-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 560 ctkglgSQT--------ESLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDlgLHPRAvstsfgcrVNLaiclqph 631
Cdd:cd17643 189 ------NQTpsafyqlvEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQL--------VNM------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 632 rlwtlaeqgtSGPDPTTVYVDMRALRHDRVRLVErGSPhslplmeSGKILPGVRIIIANpETKGPLGDSHLGEIWVHSAH 711
Cdd:cd17643 245 ----------YGITETTVHVTFRPLDAADLPAAA-ASP-------IGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 712 NASGYFtiyGDESLQSDHFNSrLSFGDTQTIWARTGYLGflRRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIE 791
Cdd:cd17643 306 VARGYL---GRPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE 371
|
490
....*....|....*
gi 767959951 792 tSVIRAHKSVTECAV 806
Cdd:cd17643 372 -AALATHPSVRDAAV 385
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
295-475 |
3.67e-07 |
|
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: 53.87 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 295 EVLQWRAQTTPDHIlytllncrgAIA---NSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYA 371
Cdd:cd17655 1 ELFEEQAEKTPDHT---------AVVfedQTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 372 GC--VPITvrPPHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLRSREAAaavdvrtwpLILDTDDLPKKRPAQICKP 449
Cdd:cd17655 71 GGayLPID--PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPV 133
|
170 180
....*....|....*....|....*.
gi 767959951 450 CNPDTLAYLDFSVSTTGMLAGVKMSH 475
Cdd:cd17655 134 SKSDDLAYVIYTSGSTGKPKGVMIEH 159
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
295-840 |
5.50e-07 |
|
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: 52.97 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 295 EVLQWRAQTTPDHILytlLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 374
Cdd:cd12117 1 ELFEEQAARTPDAVA---VVYGDR---SLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 375 PITVRPPHPQNiattlpTVKMIVEVSRSACLMTtqlickllrSREAAAAVDVRTWPLILDTDDLPKKRPAQICkPCNPDT 454
Cdd:cd12117 74 YVPLDPELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGLEVAVVIDEALDAGPAGNPAV-PVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 455 LAYLDFSVSTTGMLAGVKMSHAATSAFCRS---IKLQcelypSREVAICLDPYC--GLGFVLWclCSVYSGHQSILIPPS 529
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGVVRLVKNtnyVTLG-----PDDRVLQTSPLAfdASTFEIW--GALLNGARLVLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 530 ELETNPALwLLAVSQYKVrdtfcsySVMELcTKGLGSQteslkargldlsrvrtcvvVAEERPrialtQSFSKLfkdlgl 609
Cdd:cd12117 211 TLLDPDAL-GALIAEEGV-------TVLWL-TAALFNQ-------------------LADEDP-----ECFAGL------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 610 hpRAVSTSfGCRVNLAIClqphRLWTLAEQGTS-----GPDPTTVYvdmrALRHdrvrLVERG--SPHSLPLmesGKILP 682
Cdd:cd12117 252 --RELLTG-GEVVSPPHV----RRVLAACPGLRlvngyGPTENTTF----TTSH----VVTELdeVAGSIPI---GRPIA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 683 GVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWaRTGYLGFLRrteltdANG 762
Cdd:cd12117 314 NTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGY---LNRPALTAERF-VADPFGPGERLY-RTGDLARWL------PDG 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767959951 763 ErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAvftwtnllVVVVELDGSEQEaldlvpLVTNVVLEE 840
Cdd:cd12117 382 R----LEFLGRIDDQVKIRGFRIELGEIEA-ALRAHPGVREAV--------VVVREDAGGDKR------LVAYVVAEG 440
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
297-830 |
6.37e-07 |
|
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: 52.61 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 297 LQWRAQTTPDHilyTLLNCRGaiaNSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPi 376
Cdd:cd17631 1 LRRRARRHPDR---TALVFGG---RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVF- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 377 tvrppHPQNIATTLPTVKMIVEVSRSACLMttqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnpDTLA 456
Cdd:cd17631 73 -----VPLNFRLTPPEVAYILADSGAKVLF----------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 457 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELyPSREVAICLDPYC---GLGfvLWCLCSVYSGHQSILIPpselET 533
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILR----KF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 534 NPALWLLAVSQYKVRDTFCSYSVME-LCTKGlgsqteslKARGLDLSRVRtCVVVAEERPRIALTQSFSKlfkdlglhpr 612
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRALQA---------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 613 avstsFGCRvnlaiclqphrLWTLAEQGTSGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVRIIIANPE 692
Cdd:cd17631 236 -----RGVK-----------FVQGYGMTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPD 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 693 TKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDhfnsrlSFGDTqtiWARTGYLGFLrrteltDANGerhdALYVVG 772
Cdd:cd17631 284 GR-EVPPGEVGEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVD 340
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767959951 773 ALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLV-VVVELDGSEQEALDLV 830
Cdd:cd17631 341 RKKDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
7-226 |
7.93e-07 |
|
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: 52.67 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 7 GVI--RVDSEEKLS-VLTVQDVGLVMPGAIMCSVKPDGvpQLCRTDEIGELCVCavatGTS----YYGLSGMTKNTFevf 79
Cdd:cd05906 335 GVIysRSFPTYDHSqALEFVSLGRPIPGVSMRIVDDEG--QLLPEGEVGRLQVR----GPVvtkgYYNNPEANAEAF--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 80 pmTSSGapiseypFIRTGLLGFVGPGGLVFvVGKMDGLMVVSGRRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHD- 158
Cdd:cd05906 406 --TEDG-------WFRTGDLGFLDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAe 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767959951 159 -ERIVIVAeqrpdSTEEDSFQWMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLGGIHLSETKQLFLEG 226
Cdd:cd05906 473 tEELAIFF-----VPEYDLQDALSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
93-258 |
1.56e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.48 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 93 FIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATAlaVEPMKFVYRGRIAVFSVTVLHDERIVIVAE-----Q 167
Cdd:PRK05691 430 WLRTGDLGFLRDGEL-FVTGRLKDMLIVRGHNLYPQDIEKTV--EREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 168 RPDSTEEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLhpcnvlmcphTCVTNLPKP 247
Cdd:PRK05691 507 KILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPAL 572
|
170
....*....|.
gi 767959951 248 RQKQPEIGPAS 258
Cdd:PRK05691 573 QAVEAAQTAAS 583
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
25-228 |
2.01e-06 |
|
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: 51.35 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 25 VGLVMPGAIMCSVKPDGVPqlCRTDEIGELCVC--AVATGtsYYGLSGMTKNTFEVfpmtssgapiseyPFIRTGLLGFV 102
Cdd:COG0318 271 VGRPLPGVEVRIVDEDGRE--LPPGEVGEIVVRgpNVMKG--YWNDPEATAEAFRD-------------GWLRTGDLGRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 103 GPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMKfvyrgRIAVFSVTV-LHDERIV--IVAEQRPDSTEEDSFQW 179
Cdd:COG0318 334 DEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGVPDeKWGERVVafVVLRPGAELDAEELRAF 408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767959951 180 MSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGIHLSETKQLFLEGSL 228
Cdd:COG0318 409 LRERLARYKVPRRV-------EFVDELPRTASGKIDRRALRERYAAGAL 450
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
449-806 |
4.39e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 50.38 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 449 PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYC-GLGFVLWCLCSVYSGHQSILIP 527
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 528 PSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGSQTESlkaRGLDLSRVRtCVVVAEERPRIALTQSFSKLFKDL 607
Cdd:PRK07768 228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 608 GLHPRAVSTSFG-CRVNLAICLQPhrlwtlaeqgtSGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPG--V 684
Cdd:PRK07768 304 GLRPEAILPAYGmAEATLAVSFSP-----------CGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGleV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 685 RIIIANPEtkgPLGDSHLGEIWVHSAHNASGYFTIYGDESLQSDHfnsrlsfGdtqtiWARTGYLGFLrrTEltdaNGEr 764
Cdd:PRK07768 372 RVVDEDGQ---VLPPRGVGVIELRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TE----EGE- 429
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767959951 765 hdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTECAV 806
Cdd:PRK07768 430 ---VVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
251-477 |
5.26e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.43 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 251 QPEIGPASVmvgNLVSGKRIAQasgrdLGQIEDNDQARKFLFLSEVLQWRAQTTPDhilytllncRGAIA---NSLTCVQ 327
Cdd:PRK10252 426 DPALLCGDV---DILLPGEYAQ-----LAQVNATAVEIPETTLSALVAQQAAKTPD---------APALAdarYQFSYRE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 328 LHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLMT 407
Cdd:PRK10252 489 MREQVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLIT 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 408 TQlickLLRSREAAAAVDVRTWPLILDTDdlPKKRPAQICKPCNPdtlAYLDFSVSTTGMLAGVKMSHAA 477
Cdd:PRK10252 562 TA----DQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHT---AYIIFTSGSTGRPKGVMVGQTA 622
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
293-382 |
1.87e-05 |
|
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: 48.22 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 293 LSEVLQWRAQTTPDHIlytllncrgAI---ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCL 369
Cdd:COG1021 27 LGDLLRRRAERHPDRI---------AVvdgERRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALF 96
|
90
....*....|...
gi 767959951 370 YAGCVPITVRPPH 382
Cdd:COG1021 97 RAGAIPVFALPAH 109
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
293-481 |
1.92e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 48.36 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 293 LSEVLQWRAQTTPDHIlytllncrgAIA---NSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCL 369
Cdd:PRK07656 7 LPELLARAARRFGDKE---------AYVfgdQRLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 370 YAGCVPITVRPPH-PQNIATTLPT--VKMI--------VEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDl 438
Cdd:PRK07656 77 KAGAVVVPLNTRYtADEAAYILARgdAKALfvlglflgVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGD- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767959951 439 PKKRPAQIckpcNPDTLAYLDFSVSTTGMLAGVKMSHAAT-SAF 481
Cdd:PRK07656 156 PAERAPEV----DPDDVADILFTSGTTGRPKGAMLTHRQLlSNA 195
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
295-482 |
2.48e-05 |
|
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: 47.55 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 295 EVLQWRAQTTPDHILYTLlncRGaiaNSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCV 374
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD---RG---QSLTYKQLNEKANQLARHLRGKGVKPD-DQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 375 PITVRPPHPQniattlptvkmivevsrsaclmttQLICKLLRSREAAaavdvrtwpLILDtddlpkkrpaqickpcNPDT 454
Cdd:cd17645 75 YVPIDPDYPG------------------------ERIAYMLADSSAK---------ILLT----------------NPDD 105
|
170 180
....*....|....*....|....*...
gi 767959951 455 LAYLDFSVSTTGMLAGVKMSHAATSAFC 482
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1-212 |
2.64e-05 |
|
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: 47.82 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 1 MHGLTYGVIR---VDSEEKLSVLTvqDVGLVMPGAIMCSVKPDGvpQLCRTDEIGELcvcaVATGTSYYgLSGMTKNTFE 77
Cdd:cd05922 263 MYGQTEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDG--TPTPPGEPGEI----VHRGPNVM-KGYWNDPPYR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 78 VFPMTSSGApiseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfvyrGRIAVFSVTVLH 157
Cdd:cd05922 334 RKEGRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPL 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767959951 158 DERIVIVAEqRPDSTEEDSfqwMSRVLQAIDSIHQVGVYClalVPANTLPKTPLG 212
Cdd:cd05922 402 GEKLALFVT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
301-476 |
8.59e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.04 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 301 AQTTPDHILYtllNCRGAianSLTCVQLHKRAEKIAVMLMERgHLQDGDHVaLVY----PpgiDLIAAFYGCLYAGC--V 374
Cdd:PRK04813 12 AQTQPDFPAY---DYLGE---KLTYGQLKEDSDALAAFIDSL-KLPDKSPI-IVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 375 PITVRPPhpqniattLPTVKMIVEVSRSACLMTTqlickllrSREAAAAVDVRTwpLILD--TDDLPKKRPAQICKPCNP 452
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIAT--------EELPLEILGIPV--ITLDelKDIFATGNPYDFDHAVKG 142
|
170 180
....*....|....*....|....
gi 767959951 453 DTLAYLDFSVSTTGMLAGVKMSHA 476
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHD 166
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
301-806 |
1.70e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.54 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 301 AQTTPDHILYTLLNCRgaiansLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP 380
Cdd:PRK12467 522 ARQHPERPALVFGEQV------LSYAELNRQANRLAHVLIAAGVGPD-VLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 381 PHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTDDLPKKRPAQICKPCNPDTLAYLDF 460
Cdd:PRK12467 595 EYPQD------RLAYMLDDSGVRLLLTQSHLLAQL-----PVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIY 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 461 SVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAIcLDPYCGLGFVLWCLCSVYSGHQSILIPPSEletnpalwll 540
Cdd:PRK12467 664 TSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLM-VSTFAFDLGVTELFGALASGATLHLLPPDC---------- 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 541 avsqykVRDTFCSYSVMelCTKGLG--SQTES-----LKARGLDLSRVRTCVVVAEErpriALTQSFSKLFKDLGLhpra 613
Cdd:PRK12467 733 ------ARDAEAFAALM--ADQGVTvlKIVPShlqalLQASRVALPRPQRALVCGGE----ALQVDLLARVRALGP---- 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 614 vstsfGCrvnlaiclqphRLWTLaeqgtSGPDPTTVYVDMRALRHDRVrlVERGSPHSLPLMESgkilpGVRIIIA--NP 691
Cdd:PRK12467 797 -----GA-----------RLINH-----YGPTETTVGVSTYELSDEER--DFGNVPIGQPLANL-----GLYILDHylNP 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 692 ETKGPLGDSHLGeiwvhSAHNASGYftiYGDESLQSDHFNSRLSFGDTQTIWaRTGYLGflRRTeltdANGErhdaLYVV 771
Cdd:PRK12467 849 VPVGVVGELYIG-----GAGLARGY---HRRPALTAERFVPDPFGADGGRLY-RTGDLA--RYR----ADGV----IEYL 909
|
490 500 510
....*....|....*....|....*....|....*
gi 767959951 772 GALDEAMELRGMRYHPIDIETSvIRAHKSVTECAV 806
Cdd:PRK12467 910 GRMDHQVKIRGFRIELGEIEAR-LLAQPGVREAVV 943
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
304-475 |
1.73e-04 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. 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: 341311 [Multi-domain] Cd Length: 479 Bit Score: 45.16 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 304 TPDHILYTLLNCrgaianSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAG--CVPITvrpP 381
Cdd:cd17656 1 TPDAVAVVFENQ------KLTYRELNERSNQLARFLREKGVKKD-SIVAIMMERSAEMIVGILGILKAGgaFVPID---P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 382 HpqniattLPTVKMIVEVSRSAC-LMTTQLICKLLRSREAAaaVDVRTWPLILDTDDlpkkrpAQICKPCNPDTLAYLDF 460
Cdd:cd17656 71 E-------YPEERRIYIMLDSGVrVVLTQRHLKSKLSFNKS--TILLEDPSISQEDT------SNIDYINNSDDLLYIIY 135
|
170
....*....|....*
gi 767959951 461 SVSTTGMLAGVKMSH 475
Cdd:cd17656 136 TSGTTGKPKGVQLEH 150
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
319-547 |
4.74e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 43.87 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 319 IANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP------------------ 380
Cdd:PRK06710 46 LGKDITFSVFHDKVKRFANYLQKLG-VEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPlytereleyqlhdsgakv 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 381 --------PHPQNIATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKPCNP 452
Cdd:PRK06710 125 ilcldlvfPRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 453 DT-LAYLDFSVSTTGMLAGVKMSHA-ATSAFCRSIKLQCELYPSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPS 529
Cdd:PRK06710 205 ENdLALLQYTGGTTGFPKGVMLTHKnLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVyGMTAVMNLSIMQGYKMVLIPKF 284
|
250
....*....|....*...
gi 767959951 530 ELEtnpaLWLLAVSQYKV 547
Cdd:PRK06710 285 DMK----MVFEAIKKHKV 298
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
96-223 |
4.85e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 43.83 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 96 TGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPmkfVYRGRIAVFSVTVLHD-ERIVIVAEQRPDSTEE 174
Cdd:PRK07768 418 TGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEG---VRPGNAVAVRLDAGHSrEGFAVAVESNAFEDPA 494
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767959951 175 DSFQWMSRVLQAIDSihQVGV--YCLALVPANTLPKTPLGGIHLSETKQLF 223
Cdd:PRK07768 495 EVRRIRHQVAHEVVA--EVGVrpRNVVVLGPGSIPKTPSGKLRRANAAELV 543
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
25-214 |
1.19e-03 |
|
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: 41.89 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 25 VGLVMPGAIMCSVKPDGVPqlCRTDEIGELCVcavatgTSYYGLSGMTKNTFEVFPMTSSGapiseypFIRTGLLGFVGP 104
Cdd:cd04433 170 VGRPVPGVEVRIVDPDGGE--LPPGEIGELVV------RGPSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 105 GGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMKfvyrgRIAVFSVTvlhDER------IVIVAEQRPDSTEEDSFQ 178
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVA-----EAAVVGVP---DPEwgervvAVVVLRPGADLDAEELRA 306
|
170 180 190
....*....|....*....|....*....|....*.
gi 767959951 179 WMSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGI 214
Cdd:cd04433 307 HVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
293-476 |
1.35e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 42.44 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 293 LSEVLQWRAQTTPDHILYTLLNCRgaiansLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 372
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVFGGTR------WTYAEAARAAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 373 CVPItvrpphPQNIATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAA----------AVDVRTWPLILDTDDLPkkr 442
Cdd:PRK06155 96 AIAV------PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDlplpavwlldAPASVSVPAGWSTAPLP--- 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 767959951 443 PAQICKPCNP----DTLAYLDFSvSTTGMLAGVKMSHA 476
Cdd:PRK06155 167 PLDAPAPAAAvqpgDTAAILYTS-GTTGPSKGVCCPHA 203
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
678-820 |
1.75e-03 |
|
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: 41.66 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 678 GKILPGVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFTIYGDEsLQSDHFNSRLsfgdtqtiwaRTGYLGFLrrtel 757
Cdd:cd05922 289 GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL----------HTGDLARR----- 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767959951 758 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSvIRAHKSVTECAVF----TWTNLLVVVVELD 820
Cdd:cd05922 352 -DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLIIEAAAVglpdPLGEKLALFVTAP 412
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
678-806 |
1.88e-03 |
|
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: 41.48 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 678 GKILPGVRIIIANPETKGPLGDSHlGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLRrtel 757
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767959951 758 tdangeRHDALYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 806
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
683-807 |
2.08e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 41.80 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 683 GVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLrrteltDANG 762
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL---GDPTITAANFTDG---------WLRTGDLGSL------SAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767959951 763 ErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 807
Cdd:PRK05852 423 D----LSIRGRIKELINRGGEKISPERVE-GVLASHPNVMEAAVF 462
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
678-806 |
5.64e-03 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 40.35 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 678 GKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYFTIYGDESLQSDhfnsrlsfgdtQTIWARTGYLGFLrrtel 757
Cdd:PLN02330 364 GFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTID-----------EDGWLHTGDIGYI----- 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767959951 758 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 806
Cdd:PLN02330 428 -DDDGD----IFIVDRIKELIKYKGFQVAPAELE-AILLTHPSVEDAAV 470
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
758-807 |
7.05e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 39.64 E-value: 7.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767959951 758 TDANGERHD-ALYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 807
Cdd:PRK07824 238 TDDLGALDDgVLTVLGRADDAISTGGLTVLPQVVE-AALATHPAVADCAVF 287
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
318-475 |
7.12e-03 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 39.83 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 318 AIANSLTCVQLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPphpqnIATTLPTVKMIV 397
Cdd:PLN02574 62 STGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP-----SSSLGEIKKRVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959951 398 EVSRSACLMTTQLICKLLRSR-------------EAAAAVDVRTWPLILDTDDLPKkrpaqicKPCNPDTLAYLDFSVST 464
Cdd:PLN02574 137 DCSVGLAFTSPENVEKLSPLGvpvigvpenydfdSKRIEFPKFYELIKEDFDFVPK-------PVIKQDDVAAIMYSSGT 209
|
170
....*....|.
gi 767959951 465 TGMLAGVKMSH 475
Cdd:PLN02574 210 TGASKGVVLTH 220
|
|
| |
