|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
29-522 |
0e+00 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain] Cd Length: 449 Bit Score: 575.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 29 KDVPFLIRRTESKDTIVSYADAADEIQVLMNFLRKNGVPDEAGIALRVTeHTPASSLMILAILNNKCHFFPTDKMMLSQD 108
Cdd:cd17654 1 PDRPALIIDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCD-RGTESPVAILAILFLGAAYAPIDPASPEQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 109 LYSQMSTAGVDYLVANKHLTVAPLYFTflgsilvfkedcrlyrvklksaDETVQSKKPLPANMCYTISTTGTTGKPKLIH 188
Cdd:cd17654 80 SLTVMKKCHVSYLLQNKELDNAPLSFT----------------------PEHRHFNIRTDECLAYVIHTSGTTGTPKIVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 189 VPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRdspskVLSALFPDNLAT-PGIT 267
Cdd:cd17654 138 VPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVK-----VLPSKLADILFKrHRIT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 268 VLQMTPSLFRQFGASSIKDRVLSGSSSLRVLLLGGEPFPSNVELVTWMHpsVLMQKHICNIYGITEISCWSLLHIVQSLQ 347
Cdd:cd17654 213 VLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRG--KGNRTRIFNIYGITEVSCWALAYKVPEED 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 348 SPVPLGTPIEedtVLRIESEDNET-SQQGELFLGSVKRRCYIPEVDDQANAsqddsgiCFRATGDLVTRqQDGTLFYSER 426
Cdd:cd17654 291 SPVQLGSPLL---GTVIEVRDQNGsEGTGQVFLGGLNRVCILDDEVTVPKG-------TMRATGDFVTV-KDGELFFLGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 427 SNDVVKRAGNRISLGLITRKIQKCLPssELTTCLWLEDLQKLICCIRTLESKTRVQQRVQTFDilskVSIAEQPDRFVYL 506
Cdd:cd17654 360 KDSQIKRRGKRINLDLIQQVIESCLG--VESCAVTLSDQQRLIAFIVGESSSSRIHKELQLTL----LSSHAIPDTFVQI 433
|
490
....*....|....*.
gi 665407183 507 QHFPCNVHGKLDKQQL 522
Cdd:cd17654 434 DKLPLTSHGKVDKSEL 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
168-522 |
2.09e-44 |
|
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: 167.32 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRD 247
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 248 SPSKVLSAlfpdnLATPGITVLQMTPSLFRQFGASSIKDRVlsgsSSLRVLLLGGEPFPsnVELVTWMHpSVLMQKHICN 327
Cdd:cd05930 172 DPEALADL-----LAEEGITVLHLTPSLLRLLLQELELAAL----PSLRLVLVGGEALP--PDLVRRWR-ELLPGARLVN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 328 IYGITEISCWSLLHIVQS---LQSPVPLGTPIeEDTVLRIESEDNET---SQQGELFLGSV-KRRCYI--PEVDDQA-NA 397
Cdd:cd05930 240 LYGPTEATVDATYYRVPPddeEDGRVPIGRPI-PNTRVYVLDENLRPvppGVPGELYIGGAgLARGYLnrPELTAERfVP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 398 SQDDSGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKcLPSSELTTCLWLED---LQKLICCIRT 474
Cdd:cd05930 319 NPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLA-HPGVREAAVVAREDgdgEKRLVAYVVP 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 665407183 475 LESKTRVQQRVQTFdiLSK------VsiaeqPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd05930 398 DEGGELDEEELRAH--LAErlpdymV-----PSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
46-443 |
6.44e-36 |
|
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: 141.25 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 46 SYADAADEIQVLMNFLRKNGV--PDEAgIALRVtEHTPASSLMILAILNNKCHFFPTDKMMLSQDLYSQMSTAGVDYLVA 123
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGvgPGDR-VAVLL-ERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 124 NKHLTVAPLYFTFLGSILVFKEDCRLYRvklkSADETVQSKKPLPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQ 203
Cdd:TIGR01733 79 DSALASRLAGLVLPVILLDPLELAALDD----APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 204 KLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRDSPSKVLSALfpdnLATPGITVLQMTPSLFRQfgass 283
Cdd:TIGR01733 155 RYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAAL----IAEHPVTVLNLTPSLLAL----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 284 IKDRVLSGSSSLRVLLLGGEPFPSNVeLVTWMHPSVlmQKHICNIYGITEISCWSLLHIVQ----SLQSPVPLGTPIeED 359
Cdd:TIGR01733 226 LAAALPPALASLRLVILGGEALTPAL-VDRWRARGP--GARLINLYGPTETTVWSTATLVDpddaPRESPVPIGRPL-AN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 360 TVLRIESEDNETS---QQGELFLGSVKR-RCYI--PEVDDQ---ANASQDDSGICFRATGDLVTRQQDGTLFYSERSNDV 430
Cdd:TIGR01733 302 TRLYVLDDDLRPVpvgVVGELYIGGPGVaRGYLnrPELTAErfvPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQ 381
|
410
....*....|...
gi 665407183 431 VKRAGNRISLGLI 443
Cdd:TIGR01733 382 VKIRGYRIELGEI 394
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
39-522 |
1.79e-30 |
|
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: 126.25 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 39 ESKDTIVSYADAADEIQVLMNFLRKNGVP--DEAGIALRVTEHTPASslmILAILNNKCHFFPTDK--------MMLSQd 108
Cdd:cd12116 7 RDDDRSLSYAELDERANRLAARLRARGVGpgDRVAVYLPRSARLVAA---MLAVLKAGAAYVPLDPdypadrlrYILED- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 109 lysqmstAGVDYLvankhLTVAPLYFTFLGSILVFkedcrLYRVKLKSADETVQSKKPLPANMCYTISTTGTTGKPKLIH 188
Cdd:cd12116 83 -------AEPALV-----LTDDALPDRLPAGLPVL-----LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 189 VPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATL-LTSRHSMRDsPSKvLSALfpdnLATPGIT 267
Cdd:cd12116 146 VSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVvIAPRETQRD-PEA-LARL----IEAHSIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 268 VLQMTPSLFRQFGASSIKDRvlsgsSSLRvLLLGGEPFPSNV--ELVTwmHPSVLMqkhicNIYGITEISCWSLLHIVQS 345
Cdd:cd12116 220 VMQATPATWRMLLDAGWQGR-----AGLT-ALCGGEALPPDLaaRLLS--RVGSLW-----NLYGPTETTIWSTAARVTA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 346 LQSPVPLGTPIEEDTVLRIESEDN--ETSQQGELFLGSVK------RRcyiPEVDDQ---ANASQDDSGICFRaTGDLVT 414
Cdd:cd12116 287 AAGPIPIGRPLANTQVYVLDAALRpvPPGVPGELYIGGDGvaqgylGR---PALTAErfvPDPFAGPGSRLYR-TGDLVR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 415 RQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKCLPSSELTTCLWLEDLQKLICCIRTLESKT-----RVQQRVQTFD 489
Cdd:cd12116 363 RRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAapdaaALRAHLRATL 442
|
490 500 510
....*....|....*....|....*....|...
gi 665407183 490 ILSKVsiaeqPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd12116 443 PAYMV-----PSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
45-535 |
2.09e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 130.67 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 45 VSYADAADEIQVLMNFLRKNGV-PDE-AGIALrvtEHTPASSLMILAILNNKCHFFPTDKMMLSQDLYSQMSTAGVDYLV 122
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVgPDVlVGIAV---ERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 123 ANKHLtVAPLYFTFLGSILVFKEDCRLYRVKLKSADETVQSkkplPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLS 202
Cdd:PRK12467 615 TQSHL-LAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVALD----PDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 203 QKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATL-LTSRHSMRDSPSkvlsalFPDNLATPGITVLQMTPSLFRQFga 281
Cdd:PRK12467 690 ERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLhLLPPDCARDAEA------FAALMADQGVTVLKIVPSHLQAL-- 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 282 ssIKDRVLSGSSSLRVLLLGGEPFPSNVeLVTWMhpSVLMQKHICNIYGITEISCWSLLHIVQSLQSP---VPLGTPIEE 358
Cdd:PRK12467 762 --LQASRVALPRPQRALVCGGEALQVDL-LARVR--ALGPGARLINHYGPTETTVGVSTYELSDEERDfgnVPIGQPLAN 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 359 DTVLRIESEDNETSQQ--GELFLGSVK-RRCYI--PEVDDQ---ANASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDV 430
Cdd:PRK12467 837 LGLYILDHYLNPVPVGvvGELYIGGAGlARGYHrrPALTAErfvPDPFGADGGRLYR-TGDLARYRADGVIEYLGRMDHQ 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 431 VKRAGNRISLGLITRKIQKcLPSSELTTCLWLE---DLQKLICCIRTLESKTRVQQrvQTFDILSKVSIAEQPD-----R 502
Cdd:PRK12467 916 VKIRGFRIELGEIEARLLA-QPGVREAVVLAQPgdaGLQLVAYLVPAAVADGAEHQ--ATRDELKAQLRQVLPDymvpaH 992
|
490 500 510
....*....|....*....|....*....|...
gi 665407183 503 FVYLQHFPCNVHGKLDKQQLLKmciPLAQPAQQ 535
Cdd:PRK12467 993 LLLLDSLPLTPNGKLDRKALPK---PDASAVQA 1022
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
168-522 |
2.37e-30 |
|
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: 125.50 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYEciapNIVGL----SQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRH 243
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHA----NVLALfaatQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 244 SMRDSPSKvlsalFPDNLATPGITVLQMTPSLFRQFGASSikDRVLSGSSSLRVLLLGGEPFPSNVeLVTWMHPSVLMQK 323
Cdd:cd17643 168 EVARSPED-----FARLLRDEGVTVLNQTPSAFYQLVEAA--DRDGRDPLALRYVIFGGEALEAAM-LRPWAGRFGLDRP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 324 HICNIYGITEISCWSLLHIVQ----SLQSPVPLGTPIEeDTVLRIESEDNE---TSQQGELFLGSVK-RRCYI--PEVDD 393
Cdd:cd17643 240 QLVNMYGITETTVHVTFRPLDaadlPAAAASPIGRPLP-GLRVYVLDADGRpvpPGVVGELYVSGAGvARGYLgrPELTA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 394 QANASQDDSGICFRA--TGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKClPSSELTTCLWLEDL---QKL 468
Cdd:cd17643 319 ERFVANPFGGPGSRMyrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATH-PSVRDAAVIVREDEpgdTRL 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 469 ICCIRTLESKTRVQQRVQTFdilskvsIAE------QPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd17643 398 VAYVVADDGAAADIAELRAL-------LKEllpdymVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
168-441 |
2.85e-29 |
|
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: 126.51 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATL-LTSRHSMR 246
Cdd:COG1020 616 PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLvLAPPEARR 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 247 DSPskVLSALfpdnLATPGITVLQMTPSLFRQFGassikDRVLSGSSSLRVLLLGGEPFPsnVELVTWMHpSVLMQKHIC 326
Cdd:COG1020 696 DPA--ALAEL----LARHRVTVLNLTPSLLRALL-----DAAPEALPSLRLVLVGGEALP--PELVRRWR-ARLPGARLV 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 327 NIYGITEISCWSLLHIV---QSLQSPVPLGTPIeEDTVLRIESEDnetsQQ-------GELFLGSVKR-RCYI--PEVDD 393
Cdd:COG1020 762 NLYGPTETTVDSTYYEVtppDADGGSVPIGRPI-ANTRVYVLDAH----LQpvpvgvpGELYIGGAGLaRGYLnrPELTA 836
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 665407183 394 Q---ANASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVK-RaGNRISLG 441
Cdd:COG1020 837 ErfvADPFGFPGARLYR-TGDLARWLPDGNLEFLGRADDQVKiR-GFRIELG 886
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
168-525 |
2.57e-27 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 116.87 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATL-LTSRHSMR 246
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLcIPSEEDRL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 247 DSPSKVLSALfpdnlatpGITVLQMTPSLFRQFGASSIkdrvlsgsSSLRVLLLGGEPFPSNVeLVTWMHPSVLMqkhic 326
Cdd:cd05918 185 NDLAGFINRL--------RVTWAFLTPSVARLLDPEDV--------PSLRTLVLGGEALTQSD-VDTWADRVRLI----- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 327 NIYGITEISCWSLLHIVQSLQSPVPLGTPIeeDTVLRIESEDNETS-----QQGELFL-GSVKRRCYI--PE------VD 392
Cdd:cd05918 243 NAYGPAECTIAATVSPVVPSTDPRNIGRPL--GATCWVVDPDNHDRlvpigAVGELLIeGPILARGYLndPEktaaafIE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 393 DQANASQDDSGICFRA--TGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKCLPSS-----ELTTCLWLEDL 465
Cdd:cd05918 321 DPAWLKQEGSGRGRRLyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAkevvvEVVKPKDGSSS 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665407183 466 QKLICCI--------RTLESKTRVQQRVQTFDILSKVSIAEQ--------PDRFVYLQHFPCNVHGKLDKQQLLKM 525
Cdd:cd05918 401 PQLVAFVvldgsssgSGDGDSLFLEPSDEFRALVAELRSKLRqrlpsymvPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
46-605 |
4.66e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.60 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 46 SYADAADEIQVLMNFLRKNGVPDEAGIALRVtEHTPASSLMILAILNNKCHFFPTDKMMLSQDLYSQMSTAGVDYLVANK 125
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAV-ERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS 3162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 126 HLTVAplyftflgsilvfkEDCRLYRVKLKSADETVQSKKP----LPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGL 201
Cdd:PRK12316 3163 HLRLP--------------LAQGVQVLDLDRGDENYAEANPairtMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWM 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 202 SQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRDSPskvlsALFPDNLATPGITVLQMTPSLFRQFGA 281
Cdd:PRK12316 3229 QQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDP-----ALLVELINSEGVDVLHAYPSMLQAFLE 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 282 SSIKDRVlsgsSSLRVLLLGGEPFPSNvelvtwMHPSVLMQKHICNIYGITEISCWSLLH-IVQSLQSPVPLGTPIEEDT 360
Cdd:PRK12316 3304 EEDAHRC----TSLKRIVCGGEALPAD------LQQQVFAGLPLYNLYGPTEATITVTHWqCVEEGKDAVPIGRPIANRA 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 361 --VLRIESEDNETSQQGELFLGSVK-RRCYIPEVDDQANASQDD---SGICFRATGDLVTRQQDGTLFYSERSNDVVKRA 434
Cdd:PRK12316 3374 cyILDGSLEPVPVGALGELYLGGEGlARGYHNRPGLTAERFVPDpfvPGERLYRTGDLARYRADGVIEYIGRVDHQVKIR 3453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 435 GNRISLGLITRKIQKCLPSSEltTCLWLEDLQKLICCIRTLESKTRVQqrvqtfDILSKVSIAEQPD-----RFVYLQHF 509
Cdd:PRK12316 3454 GFRIELGEIEARLLEHPWVRE--AVVLAVDGRQLVAYVVPEDEAGDLR------EALKAHLKASLPEymvpaHLLFLERM 3525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 510 PCNVHGKLDKQQLLKMCIPLAQPAQQILKSYLHDRLecveepddsASKKQRLDDAAPCGYDLSFRQAGGTSFHAITI--- 586
Cdd:PRK12316 3526 PLTPNGKLDRKALPRPDAALLQQDYVAPVNELERRL---------AAIWADVLKLEQVGLTDNFFELGGDSIISLQVvsr 3596
|
570
....*....|....*....
gi 665407183 587 CREIGLQMCIDDeqrhLFE 605
Cdd:PRK12316 3597 ARQAGIRFTPKD----LFQ 3611
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
168-605 |
9.91e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.44 E-value: 9.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRD 247
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHR 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 248 SPSKvlsalFPDNLATPGITVLQMTPSLFRQFgassIKDRVLSGSSSLRVLLLGGEPFPSN-VELVTWMHPsvlmQKHIC 326
Cdd:PRK12316 734 DPAK-----LVELINREGVDTLHFVPSMLQAF----LQDEDVASCTSLRRIVCSGEALPADaQEQVFAKLP----QAGLY 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 327 NIYGITE----ISCWSLlhiVQSLQSPVPLGTPIEEDTVLRIESEDNETSQQ--GELFL-GSVKRRCYIPEVDDQAN--- 396
Cdd:PRK12316 801 NLYGPTEaaidVTHWTC---VEEGGDSVPIGRPIANLACYILDANLEPVPVGvlGELYLaGRGLARGYHGRPGLTAErfv 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 397 ASQDDSGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKcLPSSELTTCLWLEDLQKLICCIrtLE 476
Cdd:PRK12316 878 PSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAVLAVDGKQLVGYVV--LE 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 477 SKTRVQQRVQTFDILSKVSIAEQPDRFVYLQHFPCNVHGKLDKQQLLKmciPLAQPAQQilkSYLHDRLEcVEEPddSAS 556
Cdd:PRK12316 955 SEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA---PEASVAQQ---GYVAPRNA-LERT--LAA 1025
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 665407183 557 KKQRLDDAAPCGYDLSFRQAGGTSFHAITI---CREIGLQMciddEQRHLFE 605
Cdd:PRK12316 1026 IWQDVLGVERVGLDDNFFELGGDSIVSIQVvsrARQAGIQL----SPRDLFQ 1073
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
39-522 |
1.12e-25 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 111.25 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 39 ESKDTIVSYADAADEIQVLMNFLRKNGVPDEAGIALrVTEHTPASSLMILAILNNKCHFFPTDKMMLSQDLYSQMSTAGv 118
Cdd:cd17653 17 ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPL-LSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 119 dylvankhltvaplyftflGSILVFkedcrlyrvkLKSADETVqskkplpanmcYTISTTGTTGKPKLIHVPYECIApNI 198
Cdd:cd17653 95 -------------------ATLLLT----------TDSPDDLA-----------YIIFTSGSTGIPKGVMVPHRGVL-NY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 199 VGLSQ-KLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLtsrhsMRDSpskvlsalfPDNLATPG--ITVLQMTPSL 275
Cdd:cd17653 134 VSQPPaRLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLV-----LADP---------SDPFAHVArtVDALMSTPSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 276 FrqfgaSSIKDRVLsgsSSLRVLLLGGEPFPSNVeLVTWMHPSVLMqkhicNIYGITEISCWSLLhivQSLQ--SPVPLG 353
Cdd:cd17653 200 L-----STLSPQDF---PNLKTIFLGGEAVPPSL-LDRWSPGRRLY-----NAYGPTECTISSTM---TELLpgQPVTIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 354 TPIEEDTVLRIESEDNETS--QQGELFLGSVK-RRCYIPevDDQANAS-----QDDSGICFRATGDLVTRQQDGTLFYSE 425
Cdd:cd17653 263 KPIPNSTCYILDADLQPVPegVVGEICISGVQvARGYLG--NPALTASkfvpdPFWPGSRMYRTGDYGRWTEDGGLEFLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 426 RSNDVVKRAGNRISLGLITRKIQKCLPSSELTTCLWLEDlqkLICCIRTLES--KTRVQQRVQTfdILSKVSIaeqPDRF 503
Cdd:cd17653 341 REDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNG---RLVAFVTPETvdVDGLRSELAK--HLPSYAV---PDRI 412
|
490
....*....|....*....
gi 665407183 504 VYLQHFPCNVHGKLDKQQL 522
Cdd:cd17653 413 IALDSFPLTANGKVDRKAL 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
173-522 |
1.18e-24 |
|
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: 108.49 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 173 YTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRDSPskv 252
Cdd:cd05945 101 YIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADP--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 253 lsALFPDNLATPGITVLQMTPSlfrqFGASSIKDRVLSGSS--SLRVLLLGGEPFPSNvELVTWMhpSVLMQKHICNIYG 330
Cdd:cd05945 178 --KQLFRFLAEHGITVWVSTPS----FAAMCLLSPTFTPESlpSLRHFLFCGEVLPHK-TARALQ--QRFPDARIYNTYG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 331 ITE--ISCwSLLHIVQSLQS---PVPLGTPIEeDTVLRIESEDNETSQ---QGELFLG--SVKRRCYIPEVDDQANASQD 400
Cdd:cd05945 249 PTEatVAV-TYIEVTPEVLDgydRLPIGYAKP-GAKLVILDEDGRPVPpgeKGELVISgpSVSKGYLNNPEKTAAAFFPD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 401 DSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKCLPSSELTTCLW--LEDLQKLICCI------ 472
Cdd:cd05945 327 EGQRAYR-TGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKykGEKVTELIAFVvpkpga 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 665407183 473 ---RTLESKTRVQQRVQTFDIlskvsiaeqPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd05945 406 eagLTKAIKAELAERLPPYMI---------PRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-605 |
8.84e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 109.28 E-value: 8.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 42 DTIVSYADAADEIQVLMNFLRKNGVPDEA--GIALRVTEhtpasSLMI--LAILNNKCHFFPTDKMMLSQDLYSQMSTAG 117
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRARGVGPEVrvAIAAERSF-----ELVValLAVLKAGGAYVPLDPNYPAERLAYMLEDSG 2100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 118 VDYLVANKHLTVAPLYFTFLGSILVFKEDcrlyrvKLKSADETVQSKKPLPANMCYTISTTGTTGKPKLIHVPYECIAPN 197
Cdd:PRK12316 2101 AALLLTQRHLLERLPLPAGVARLPLDRDA------EWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 198 IVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRDsPSKVLsalfpDNLATPGITVLQMTPSLFR 277
Cdd:PRK12316 2175 CQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWD-PEQLY-----DEMERHGVTILDFPPVYLQ 2248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 278 QFGASSIKDRvlsGSSSLRVLLLGGEPFPSNVELVTWmhpSVLMQKHICNIYGITE----ISCWSLLHIVQSLQSPVPLG 353
Cdd:PRK12316 2249 QLAEHAERDG---RPPAVRVYCFGGEAVPAASLRLAW---EALRPVYLFNGYGPTEavvtPLLWKCRPQDPCGAAYVPIG 2322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 354 TPIEEDTVLRIESEDNETSQQ--GELFLGSVK-RRCYIPE--------VDDQANASqddSGICFRaTGDLVTRQQDGTLF 422
Cdd:PRK12316 2323 RALGNRRAYILDADLNLLAPGmaGELYLGGEGlARGYLNRpgltaerfVPDPFSAS---GERLYR-TGDLARYRADGVVE 2398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 423 YSERSNDVVKRAGNRISLGLITRKIQKcLPSSELTTCLWLEDL--QKLICCIRTLESKTRVQQRVQTFdILSKVSIAEQP 500
Cdd:PRK12316 2399 YLGRIDHQVKIRGFRIELGEIEARLQA-HPAVREAVVVAQDGAsgKQLVAYVVPDDAAEDLLAELRAW-LAARLPAYMVP 2476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 501 DRFVYLQHFPCNVHGKLDKQQLLKMCIPLAQPAQQILKSYLHDRLecveepddsASKKQRLDDAAPCGYDLSFRQAGGTS 580
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRL---------AAIWQAVLKVEQVGLDDHFFELGGHS 2547
|
570 580
....*....|....*....|....*
gi 665407183 581 FHAITICREIGLQMCIDDEQRHLFE 605
Cdd:PRK12316 2548 LLATQVVSRVRQDLGLEVPLRILFE 2572
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
166-443 |
2.96e-23 |
|
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: 104.66 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 166 PLPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSM 245
Cdd:cd17646 135 PRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 246 RDSPSkVLSALfpdnLATPGITVLQMTPSLFRQFgassIKDRVLSGSSSLRVLLLGGEPFPsnVELVTWMH--PSVLMQk 323
Cdd:cd17646 215 HRDPA-YLAAL----IREHGVTTCHFVPSMLRVF----LAEPAAGSCASLRRVFCSGEALP--PELAARFLalPGAELH- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 324 hicNIYGITEISCWSLLHIVQSLQ--SPVPLGTPIEEDT--VLrieseDNETSQQ-----GELFLGSVK-RRCYIPEVDD 393
Cdd:cd17646 283 ---NLYGPTEAAIDVTHWPVRGPAetPSVPIGRPVPNTRlyVL-----DDALRPVpvgvpGELYLGGVQlARGYLGRPAL 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 665407183 394 QAN---ASQDDSGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLI 443
Cdd:cd17646 355 TAErfvPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEI 407
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
168-434 |
4.23e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 103.16 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTiSttGTTGKPKLIHVPYECIAPNIVGLSQ----KLNVSMADIIYLGTPITFD-PFVVEFFLALQNGATLLTSR 242
Cdd:pfam00501 157 LAYIIYT-S--GTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDfGLSLGLLGPLLAGATVVLPP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 243 HSMRDSPskvlsALFPDNLATPGITVLQMTPSLFRQFGASSIKDRVLSgsSSLRVLLLGGEPFPsnVELVTWMHpsVLMQ 322
Cdd:pfam00501 234 GFPALDP-----AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALL--SSLRLVLSGGAPLP--PELARRFR--ELFG 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 323 KHICNIYGITEISCWSLLHI--VQSLQSPVPLGTPIEeDTVLRIESEDN----ETSQQGELFLGSvkrrcyiPEV----- 391
Cdd:pfam00501 303 GALVNGYGLTETTGVVTTPLplDEDLRSLGSVGRPLP-GTEVKIVDDETgepvPPGEPGELCVRG-------PGVmkgyl 374
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 665407183 392 -DDQANASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRA 434
Cdd:pfam00501 375 nDPELTAEAFDEDGWYR-TGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
57-522 |
4.63e-23 |
|
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: 103.95 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 57 LMNFLRKNGV-PDE-AGIalrVTEHTPASSLMILAILNNKCHFFPTD--------KMMLSQdlysqmstAGVDYLVANKH 126
Cdd:cd17655 35 LARTLREKGVgPDTiVGI---MAERSLEMIVGILGILKAGGAYLPIDpdypeeriQYILED--------SGADILLTQSH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 127 LtVAPLYFTflGSILVFKEDcrlyrvklKSADETVQSKKPL--PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQK 204
Cdd:cd17655 104 L-QPPIAFI--GLIDLLDED--------TIYHEESENLEPVskSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 205 LNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSmRDSPSKVLSALFPDNlatpGITVLQMTPSLFrqfgaSSI 284
Cdd:cd17655 173 IYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKE-TVLDGQALTQYIRQN----RITIIDLTPAHL-----KLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 285 KDRVLSGSSSLRVLLLGGEPFPSnvELVT-WMHPSVLmQKHICNIYGITE--ISCWSLLHIVQSLQSP-VPLGTPIEE-- 358
Cdd:cd17655 243 DAADDSEGLSLKHLIVGGEALST--ELAKkIIELFGT-NPTITNAYGPTEttVDASIYQYEPETDQQVsVPIGKPLGNtr 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 359 ----DTVLRIESedneTSQQGELFLG--SVKRRcYI--PEVDDQA--NASQDDSGICFRaTGDLVTRQQDGTLFYSERSN 428
Cdd:cd17655 320 iyilDQYGRPQP----VGVAGELYIGgeGVARG-YLnrPELTAEKfvDDPFVPGERMYR-TGDLARWLPDGNIEFLGRID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 429 DVVKRAGNRISLGLITRKIQKcLPSSELTTCLWLEDLQ--KLICC-------IRTLESKTRVQQRVQTFDIlskvsiaeq 499
Cdd:cd17655 394 HQVKIRGYRIELGEIEARLLQ-HPDIKEAVVIARKDEQgqNYLCAyivsekeLPVAQLREFLARELPDYMI--------- 463
|
490 500
....*....|....*....|...
gi 665407183 500 PDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd17655 464 PSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
42-443 |
5.41e-23 |
|
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: 103.82 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 42 DTIVSYADAADEIQVLMNFLRKNGVPDEAGIALRVtEHTPASSLMILAILNNKCHFFPTD--------KMMLSQdlysqm 113
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLA-ERSPELVVALLAVLKAGAAYVPLDpelpaerlAFMLAD------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 114 stAGVDYLVANKHLTVAPlyftflgsilvfkeDCRLYRVKLKSADETVQSKKPL----PANMCYTISTTGTTGKPKLIHV 189
Cdd:cd12117 93 --AGAKVLLTDRSLAGRA--------------GGLEVAVVIDEALDAGPAGNPAvpvsPDDLAYVMYTSGSTGRPKGVAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 190 PYECIA-----PNIVGLSqklnvsmADIIYLGT-PITFDPFVVEFFLALQNGATL-LTSRHSMRDSPSkvLSALfpdnLA 262
Cdd:cd12117 157 THRGVVrlvknTNYVTLG-------PDDRVLQTsPLAFDASTFEIWGALLNGARLvLAPKGTLLDPDA--LGAL----IA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 263 TPGITVLQMTPSLFRQfgassIKDRVLSGSSSLRVLLLGGEPF-PSNVELVTWMHPSVlmqkHICNIYGITEISCWSLLH 341
Cdd:cd12117 224 EEGVTVLWLTAALFNQ-----LADEDPECFAGLRELLTGGEVVsPPHVRRVLAACPGL----RLVNGYGPTENTTFTTSH 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 342 IVQSL---QSPVPLGTPIEEDTVLRIesedNETSQQ------GELF-------LGSVKRrcyiPEVDDQ---ANASQDDS 402
Cdd:cd12117 295 VVTELdevAGSIPIGRPIANTRVYVL----DEDGRPvppgvpGELYvggdglaLGYLNR----PALTAErfvADPFGPGE 366
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 665407183 403 GIcFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLI 443
Cdd:cd12117 367 RL-YR-TGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEI 405
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
168-522 |
4.26e-22 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 100.52 E-value: 4.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLtsrhsMRD 247
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVV-----LRP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 248 SPskvlSALFPDNLATP----GITVLQMTPSLFRQFgASSIKDRVLSGSSSLRVLLLGGEPFPsnVELVT-WMHPSVLMq 322
Cdd:cd17649 168 DE----LWASADELAEMvrelGVTVLDLPPAYLQQL-AEEADRTGDGRPPSLRLYIFGGEALS--PELLRrWLKAPVRL- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 323 khiCNIYGITEISCWSLLHIVQS----LQSPVPLGTPIEEDTVLRIESEDNETSQ--QGELFLGSVK-RRCYI--PEVDD 393
Cdd:cd17649 240 ---FNAYGPTEATVTPLVWKCEAgaarAGASMPIGRPLGGRSAYILDADLNPVPVgvTGELYIGGEGlARGYLgrPELTA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 394 QA---NASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKcLPS--SELTTCLWLEDLQKL 468
Cdd:cd17649 317 ERfvpDPFGAPGSRLYR-TGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLE-HPGvrEAAVVALDGAGGKQL 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 665407183 469 ICCI--RTLESKTRVQQRVQTfDILSKVSIAEQPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd17649 395 VAYVvlRAAAAQPELRAQLRT-ALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
46-448 |
6.06e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 103.32 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 46 SYADAADEIQVLMNFLRKNGVPDEA--GIALrvtehtPASSLMI---LAILNNKCHFFPTDKMMLSQDLYSQMSTAGVDY 120
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVlvGIAV------ERSLEMVvglLAILKAGGAYVPLDPEYPRERLAYMIEDSGIEL 1674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 121 LVANKHLTVAPLYFTFLGSILVFKEDcrlyrVKLKSADETVQSKKPLPANMCYTISTTGTTGKPKLIHVPYECIAPNIVG 200
Cdd:PRK12467 1675 LLTQSHLQARLPLPDGLRSLVLDQED-----DWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCA 1749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 201 LSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRDSPSKVLsalfpDNLATPGITVLQMTPSLFRQFG 280
Cdd:PRK12467 1750 TQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLI-----QLIERQQVTTLHFVPSMLQQLL 1824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 281 ASsikDRVLSGSSSLRVLLLGGEPFPSNVELVTWmhpSVLMQKHICNIYGITE----ISCWSLLHIVQSLQSPVPLGTPI 356
Cdd:PRK12467 1825 QM---DEQVEHPLSLRRVVCGGEALEVEALRPWL---ERLPDTGLFNLYGPTEtavdVTHWTCRRKDLEGRDSVPIGQPI 1898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 357 EEdtvLRIESEDNETSQQ-----GELFLGSVK-RRCYI--PEVDDQ---ANASQDDSGICFRaTGDLVTRQQDGTLFYSE 425
Cdd:PRK12467 1899 AN---LSTYILDASLNPVpigvaGELYLGGVGlARGYLnrPALTAErfvADPFGTVGSRLYR-TGDLARYRADGVIEYLG 1974
|
410 420
....*....|....*....|...
gi 665407183 426 RSNDVVKRAGNRISLGLITRKIQ 448
Cdd:PRK12467 1975 RIDHQVKIRGFRIELGEIEARLR 1997
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
168-522 |
1.33e-21 |
|
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: 99.73 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIApNIVG-LSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMR 246
Cdd:cd17651 135 ADDLAYVIYTSGSTGRPKGVVMPHRSLA-NLVAwQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 247 DSPSKvLSALfpdnLATPGITVLQMTPSLFRQFGASSikDRVLSGSSSLRVLLLGGEPFPSNVELVTWM--HPSVLmqkh 324
Cdd:cd17651 214 TDPPA-LAAW----LDEQRISRVFLPTVALRALAEHG--RPLGVRLAALRYLLTGGEQLVLTEDLREFCagLPGLR---- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 325 ICNIYGITE---ISCWSLLHIVQSLQSPVPLGTPIEeDTVLRIESEDNE---TSQQGELFLG--SVKR-RCYIPE----- 390
Cdd:cd17651 283 LHNHYGPTEthvVTALSLPGDPAAWPAPPPIGRPID-NTRVYVLDAALRpvpPGVPGELYIGgaGLARgYLNRPEltaer 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 391 -VDDQANASQddsgICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKClPSSELTTCLWLEDLQK-- 467
Cdd:cd17651 362 fVPDPFVPGA----RMYR-TGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARH-PGVREAVVLAREDRPGek 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665407183 468 -----LIC----CIRTLESKTRVQQRVQTFDIlskvsiaeqPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd17651 436 rlvayVVGdpeaPVDAAELRAALATHLPEYMV---------PSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
168-605 |
2.64e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.19 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLtsrhsMRD 247
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVV-----IRD 4767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 248 sPSKVLSALFPDNLATPGITVLQMTPSLFRQFGASsikDRVLSGSSSLRVLLLGGEPFPSNVELVTWmhpSVLMQKHICN 327
Cdd:PRK12316 4768 -DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEH---AERDGEPPSLRVYCFGGEAVAQASYDLAW---RALKPVYLFN 4840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 328 IYGITE----ISCWSLLHIVQSLQSPVPLGTPIEEDT--VLRIESEDNETSQQGELFLGS-VKRRCYIPEVDDQA----- 395
Cdd:PRK12316 4841 GYGPTEttvtVLLWKARDGDACGAAYMPIGTPLGNRSgyVLDGQLNPLPVGVAGELYLGGeGVARGYLERPALTAerfvp 4920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 396 NASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKcLPSSELTTCLWLEDL--QKLICCI- 472
Cdd:PRK12316 4921 DPFGAPGGRLYR-TGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLRE-HPAVREAVVIAQEGAvgKQLVGYVv 4998
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 473 ----RTLESKTRVQQRVQTFDILSKVSIAEQ--PDRFVYLQHFPCNVHGKLDKQQLLKMCIPLAQPAQQILKSYLHDRLE 546
Cdd:PRK12316 4999 pqdpALADADEAQAELRDELKAALRERLPEYmvPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVA 5078
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 665407183 547 CVEEpddSASKKQRLddaapcGYDLSFRQAGGTSFHAITICREIGLQMCIDDEQRHLFE 605
Cdd:PRK12316 5079 AIWA---EVLQLERV------GLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQ 5128
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
168-522 |
7.88e-20 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 93.47 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIaPNIVG-LSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLtsrhsMR 246
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGL-ANLAAaQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLV-----LA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 247 DSPSKVLSALFPDNLATPGITVLQMTPSLFRQFGASSIKDrvlsgsssLRVLLLGGEPFPSnvELV-TWMhPSVLMqkhi 325
Cdd:cd17652 166 PAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPD--------LRTLVVAGEACPA--ELVdRWA-PGRRM---- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 326 CNIYGITEISCWSLLHIVQSLQSPVPLGTPIEEDTVLRIESEDNET--SQQGELFLGSVK-RRCYI--PEVDDQ---ANA 397
Cdd:cd17652 231 INAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVppGVPGELYIAGAGlARGYLnrPGLTAErfvADP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 398 SQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKCLPSSELTTCLWLEDL--QKLICCIrTL 475
Cdd:cd17652 311 FGAPGSRMYR-TGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPgdKRLVAYV-VP 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 665407183 476 ESKTRV---QQRVQTFDILSKVSIaeqPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd17652 389 APGAAPtaaELRAHLAERLPGYMV---PAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
168-522 |
1.97e-19 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 92.50 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRD 247
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 248 SPSKvlsalFPDNLATPGITVLQMTPSLFRQFgASSIKDRVLSGSSSLRVLLLGGEPF-PSNVElvTWMhpSVLMQKHIC 326
Cdd:cd17644 185 SLED-----FVQYIQQWQLTVLSLPPAYWHLL-VLELLLSTIDLPSSLRLVIVGGEAVqPELVR--QWQ--KNVGNFIQL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 327 -NIYGITEISCWSLLHIVQSLQSP----VPLGTPIEEDTVLRIEsednETSQQ------GELFLGSVK-RRCYI--PEVD 392
Cdd:cd17644 255 iNVYGPTEATIAATVCRLTQLTERnitsVPIGRPIANTQVYILD----ENLQPvpvgvpGELHIGGVGlARGYLnrPELT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 393 DQ---ANASQDDSGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKcLPSSELTTCLWLED---LQ 466
Cdd:cd17644 331 AEkfiSHPFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQ-HNDVKTAVVIVREDqpgNK 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 665407183 467 KLICCIRTLESKTRVQQRVQTFdILSKVSIAEQPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd17644 410 RLVAYIVPHYEESPSTVELRQF-LKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
169-525 |
3.65e-19 |
|
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: 91.80 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 169 ANMCYTistTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFD-PFVVEFFLALQNGATL-LTSRHSmr 246
Cdd:COG0318 103 ALILYT---SGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLvLLPRFD-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 247 dsPSKVLsalfpDNLATPGITVLQMTPSLFRQFGASSIKDRVLSgsSSLRVLLLGGEPFPSNV--ELVTWMHPsvlmqkH 324
Cdd:COG0318 178 --PERVL-----ELIERERVTVLFGVPTMLARLLRHPEFARYDL--SSLRLVVSGGAPLPPELleRFEERFGV------R 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 325 ICNIYGITEISCWSLLHIVQSLQS-PVPLGTPIeEDTVLRIESEDNE---TSQQGELFLGSvkrrcyiPEV------DDQ 394
Cdd:COG0318 243 IVEGYGLTETSPVVTVNPEDPGERrPGSVGRPL-PGVEVRIVDEDGRelpPGEVGEIVVRG-------PNVmkgywnDPE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 395 ANASQDDSGiCFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKC----------LPSSELTtclwled 464
Cdd:COG0318 315 ATAEAFRDG-WLR-TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHpgvaeaavvgVPDEKWG------- 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665407183 465 lQKLICCIRTLESKTRVQQRVQTFdILSKVSIAEQPDRFVYLQHFPCNVHGKLDKQQLLKM 525
Cdd:COG0318 386 -ERVVAFVVLRPGAELDAEELRAF-LRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
151-522 |
9.26e-19 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 90.54 E-value: 9.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 151 RVKLKSADETVQSKKPLPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMAD---IIYLGTPItFDPFVVE 227
Cdd:cd17648 76 RIQFILEDTGARVVITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGdeaVLFFSNYV-FDFFVEQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 228 FFLALQNGATLLTSRHSMRDSPSKvlsalFPDNLATPGITVLQMTPSLFRQFGASSIkdrvlsgsSSLRVLLLGGEPFps 307
Cdd:cd17648 155 MTLALLNGQKLVVPPDEMRFDPDR-----FYAYINREKVTYLSGTPSVLQQYDLARL--------PHLKRVDAAGEEF-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 308 nvelvtwmHPSVLMQKH------ICNIYGITEIScwsllhiVQSLQSPVP--------LGTPIEEDT--VLRIESEDNET 371
Cdd:cd17648 220 --------TAPVFEKLRsrfaglIINAYGPTETT-------VTNHKRFFPgdqrfdksLGRPVRNTKcyVLNDAMKRVPV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 372 SQQGELFLGSVK-RRCYI--PEVDDQ-------ANASQDDSGICFR--ATGDLVTRQQDGTLFYSERSNDVVKRAGNRIS 439
Cdd:cd17648 285 GAVGELYLGGDGvARGYLnrPELTAErflpnpfQTEQERARGRNARlyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 440 LGLITRK------IQKCLPSSELTTCLWLEDLQKLICCIRTLESKTRVQQRVQTFdILSKVSIAEQPDRFVYLQHFPCNV 513
Cdd:cd17648 365 PGEVEAAlasypgVRECAVVAKEDASQAQSRIQKYLVGYYLPEPGHVPESDLLSF-LRAKLPRYMVPARLVRLEGIPVTI 443
|
....*....
gi 665407183 514 HGKLDKQQL 522
Cdd:cd17648 444 NGKLDVRAL 452
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
168-439 |
2.26e-18 |
|
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: 87.73 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTistTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRhsmRD 247
Cdd:cd04433 2 PALILYT---SGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 248 SPSKVLSAlfpdnLATPGITVLQMTPSLFRQF-GASSIKDRVLsgsSSLRVLLLGGEPFPsnVELVTWMH---PSVLMqk 323
Cdd:cd04433 76 DPEAALEL-----IEREKVTILLGVPTLLARLlKAPESAGYDL---SSLRALVSGGAPLP--PELLERFEeapGIKLV-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 324 hicNIYGITE-----ISCWSLLHIVQslqsPVPLGTPIeEDTVLRIESEDNETSQQGE----------LFLGSVKRRcyi 388
Cdd:cd04433 144 ---NGYGLTEtggtvATGPPDDDARK----PGSVGRPV-PGVEVRIVDPDGGELPPGEigelvvrgpsVMKGYWNNP--- 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 665407183 389 pevddqANASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRIS 439
Cdd:cd04433 213 ------EATAAVDEDGWYR-TGDLGRLDEDGYLYIVGRLKDMIKSGGENVY 256
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
168-522 |
3.89e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 88.53 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYEciapNIVGL---------SQKLNVSMAdiiylGTPITFDPFVVEFFLALQNGATL 238
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHR----NAAAFlqwaaaafsAEELAGVLA-----STSICFDLSVFELFGPLATGGKV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 239 LtsrhsMRDSpskVLSalFPDNLATPGITVLQMTPSLFRQFgassIKDRVLsgSSSLRVLLLGGEPFPSnvELVTWMHpS 318
Cdd:cd12115 175 V-----LADN---VLA--LPDLPAAAEVTLINTVPSAAAEL----LRHDAL--PASVRVVNLAGEPLPR--DLVQRLY-A 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 319 VLMQKHICNIYGITEISCWSLLHIV-QSLQSPVPLGTPIEEDTVLRIESEDNETSQ--QGELFL-GSVKRRCYIPEVDDQ 394
Cdd:cd12115 236 RLQVERVVNLYGPSEDTTYSTVAPVpPGASGEVSIGRPLANTQAYVLDRALQPVPLgvPGELYIgGAGVARGYLGRPGLT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 395 AN----ASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGlitrKIQKCLPS----------------- 453
Cdd:cd12115 316 AErflpDPFGPGARLYR-TGDLVRWRPDGLLEFLGRADNQVKVRGFRIELG----EIEAALRSipgvreavvvaigdaag 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665407183 454 ---------SELTTCLWLEDLQKliccirtlesktRVQQRVQTFDIlskvsiaeqPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd12115 391 errlvayivAEPGAAGLVEDLRR------------HLGTRLPAYMV---------PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
166-455 |
2.42e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 87.79 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 166 PLPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSR-HS 244
Cdd:PRK10252 595 SQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEpEA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 245 MRDsPSKvLSALFPDNlatpGITVLQMTPSLFRQFGASSIKDRVLSGSSSLRVLLLGGEPFPSnvELVTWMHPSVLMQKH 324
Cdd:PRK10252 675 HRD-PLA-MQQFFAEY----GVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPA--DLCREWQQLTGAPLH 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 325 icNIYGITE----ISCW----SLLHIVQSlqSPVPLGTPIeEDTVLRIesEDNETSQQ-----GELFLGSVK-RRCYIPE 390
Cdd:PRK10252 747 --NLYGPTEaavdVSWYpafgEELAAVRG--SSVPIGYPV-WNTGLRI--LDARMRPVppgvaGDLYLTGIQlAQGYLGR 819
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665407183 391 VDDQANASQDD---SGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKcLPSSE 455
Cdd:PRK10252 820 PDLTASRFIADpfaPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQA-LPDVE 886
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
168-522 |
2.72e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.91 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRD 247
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWD 3315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 248 sPSKVLSALFPDnlatpGITVLQMTPSLFRQFGAssikDRVLSGSSSLRVLLLGGEPFP-SNVELVTwmhpSVLMQKHIC 326
Cdd:PRK12467 3316 -PEELWQAIHAH-----RISIACFPPAYLQQFAE----DAGGADCASLDIYVFGGEAVPpAAFEQVK----RKLKPRGLT 3381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 327 NIYGITE----ISCWSLLHIVQSLQSPVPLGTPIEEDT--VLRIESEDNETSQQGELFLGSV------KRRcyiPEVDDQ 394
Cdd:PRK12467 3382 NGYGPTEavvtVTLWKCGGDAVCEAPYAPIGRPVAGRSiyVLDGQLNPVPVGVAGELYIGGVglargyHQR---PSLTAE 3458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 395 ---ANASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKCLPSSE-------------LTT 458
Cdd:PRK12467 3459 rfvADPFSGSGGRLYR-TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREavvlardgaggkqLVA 3537
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665407183 459 CLWLEDLQKliccirTLESKTRVQQRVQTFDILskvsiaeQPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:PRK12467 3538 YVVPADPQG------DWRETLRDHLAASLPDYM-------VPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
57-522 |
8.69e-17 |
|
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: 84.45 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 57 LMNFLRKNGVPDEAGIALrVTEHTPASSLMILAILNNKCHFFPTDKMMLSQDLYSQMSTAGVDYLVANKHLTVaPLYFTF 136
Cdd:cd17656 26 LARFLREKGVKKDSIVAI-MMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRHLKS-KLSFNK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 137 lgsILVFKEDCRLYRVKLKSADETVQSKkplpaNMCYTISTTGTTGKPKLIHVPYECIApNIVGL--SQKLNVSMADIIY 214
Cdd:cd17656 104 ---STILLEDPSISQEDTSNIDYINNSD-----DLLYIIYTSGTTGKPKGVQLEHKNMV-NLLHFerEKTNINFSDKVLQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 215 LGTPiTFDPFVVEFFLALQNGATL-LTSRHSMRDSPSkvlsaLFpDNLATPGITVLQMtPSLFRQFGASSiKDRVLSGSS 293
Cdd:cd17656 175 FATC-SFDVCYQEIFSTLLSGGTLyIIREETKRDVEQ-----LF-DLVKRHNIEVVFL-PVAFLKFIFSE-REFINRFPT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 294 SLRVLLLGGEPFPSNVELVTWMHPSvlmQKHICNIYGITEISCWSLLHIVQSLQSPV--PLGTPIEEDTVLRIESEDNET 371
Cdd:cd17656 246 CVKHIITAGEQLVITNEFKEMLHEH---NVHLHNHYGPSETHVVTTYTINPEAEIPElpPIGKPISNTWIYILDQEQQLQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 372 SQQ--GELFL-GSVKRRCYI--PEV-DDQANASQDDSGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITR 445
Cdd:cd17656 323 PQGivGELYIsGASVARGYLnrQELtAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 446 KIQKCLPSSELTTCLWLEDL-QKLICCIRTLEsktrvqQRVQTFDILSKvsIAEQ------PDRFVYLQHFPCNVHGKLD 518
Cdd:cd17656 403 QLLNHPGVSEAVVLDKADDKgEKYLCAYFVME------QELNISQLREY--LAKQlpeymiPSFFVPLDQLPLTPNGKVD 474
|
....
gi 665407183 519 KQQL 522
Cdd:cd17656 475 RKAL 478
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
151-522 |
9.81e-15 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 77.59 E-value: 9.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 151 RVKLKSADETVQSKKPLPANMCYTISTTGTTGKPKLIHVPYEciapNIVGLSQ----KLNVSMADIIYLGTPITFDPFVV 226
Cdd:cd17645 86 RIAYMLADSSAKILLTNPDDLAYVIYTSGSTGLPKGVMIEHH----NLVNLCEwhrpYFGVTPADKSLVYASFSFDASAW 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 227 EFFLALQNGATLltsrHSMrDSPSKVLSALFPDNLATPGITVLQMTPSLFRQFGASSikdrvlsgSSSLRVLLLGGEPFP 306
Cdd:cd17645 162 EIFPHLTAGAAL----HVV-PSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLD--------NQSLRVLLTGGDKLK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 307 SNVElvtwmhpsvlMQKHICNIYGITEISCWSLLHIVQSLQSPVPLGTPIEEDTVLrIESEDNETSQQ---GELFL-GSV 382
Cdd:cd17645 229 KIER----------KGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVY-ILDEALQLQPIgvaGELCIaGEG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 383 KRRCYIPEVDDQAN---ASQDDSGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKcLPSSELTTC 459
Cdd:cd17645 298 LARGYLNRPELTAEkfiVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMN-HPLIELAAV 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665407183 460 LWLEDL--QKLICCIRTLESKTRVQQRVQTF-DILSKVSIaeqPDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd17645 377 LAKEDAdgRKYLVAYVTAPEEIPHEELREWLkNDLPDYMI---PTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-522 |
2.36e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 47 YADAADEIQVLMNFLRKNGVPDEAGIALRVtEHTPASSLMILAILNNKCHFFPTDKMMLSQDLYSQMSTAGVDYLVANKH 126
Cdd:PRK05691 1159 YAELHAQANRLAHYLRDKGVGPDVCVAIAA-ERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSH 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 127 LtvaplyftfLGSILVFKEDCRLYRVKLKSADETVQSkkplPA------NMCYTISTTGTTGKPKLIHVPYECIAPNIVG 200
Cdd:PRK05691 1238 L---------LERLPQAEGVSAIALDSLHLDSWPSQA----PGlhlhgdNLAYVIYTSGSTGQPKGVGNTHAALAERLQW 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 201 LSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRDSPSKVLSAlfpdnLATPGITVLQMTPSLFRQFg 280
Cdd:PRK05691 1305 MQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAEL-----VQQYGVTTLHFVPPLLQLF- 1378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 281 assIKDRVLSGSSSLRVLLLGGEPFPSNV-ELVTWMHPSVlmQKHicNIYGITE----ISCWSlLHIVQSLQSPV--PLG 353
Cdd:PRK05691 1379 ---IDEPLAAACTSLRRLFSGGEALPAELrNRVLQRLPQV--QLH--NRYGPTEtainVTHWQ-CQAEDGERSPIgrPLG 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 354 TPIEEdtVLRIESEDNETSQQGELFLGSVK-RRCYI--PEVDDQ---ANASQDDSGICFRaTGDLVTRQQDGTLFYSERS 427
Cdd:PRK05691 1451 NVLCR--VLDAELNLLPPGVAGELCIGGAGlARGYLgrPALTAErfvPDPLGEDGARLYR-TGDRARWNADGALEYLGRL 1527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 428 NDVVKRAGNRISLGlitrKIQKCL---PSSELTTCLWLEDL--QKLICCIrTLESktrvQQRVQTFDILSKVSiAEQPD- 501
Cdd:PRK05691 1528 DQQVKLRGFRVEPE----EIQARLlaqPGVAQAAVLVREGAagAQLVGYY-TGEA----GQEAEAERLKAALA-AELPEy 1597
|
490 500
....*....|....*....|....*
gi 665407183 502 ----RFVYLQHFPCNVHGKLDKQQL 522
Cdd:PRK05691 1598 mvpaQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
732-978 |
5.20e-13 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 69.74 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 732 DGCLYGFNPQTGNIVFRVGIGGliKSQPMLTADGRRIIVcsyADDYN-VYCLSAERQEVLWCLRIGEkPIFASPLelPRE 810
Cdd:pfam13360 2 DGVVTALDAATGAELWRVDLET--GLGGGVAVDGGRLFV---ATGGGqLVALDAATGKLLWRQTLSG-EVLGAPL--VAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 811 QSLIVCTLDGSYSRVAITDGSVEWTQKFREP--VFSTPVLLESVSNIFLSAEVAGRVHACHVGNGKILA----TFSTEGN 884
Cdd:pfam13360 74 GRVFVVAGDGSLIALDAADGRRLWSYQRSGEplALRSSGSPAVVGDTVVAGFSSGKLVALDPATGKVRWeaplAAPRGTN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 885 IFSSLV-VKTPPTFMGHS-FAI-----FGCIDQHlyclrckTGpggksvelELHWKVDVGAPiyatptlLTVQPNGLLVW 957
Cdd:pfam13360 154 ELERLVdITGTPVVAGGRvFASayqgrLVAFDAA-------TG--------RRLWTREISGP-------NGPILDGDLLY 211
|
250 260
....*....|....*....|.
gi 665407183 958 CAATDGRVMLINFRNGEIQWS 978
Cdd:pfam13360 212 VVSDDGELYALDRATGAVVWK 232
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
175-440 |
1.57e-11 |
|
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: 67.85 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 175 ISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSrhsmrdsPSKVLS 254
Cdd:cd05922 123 LYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLT-------NDGVLD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 255 ALFPDNLATPGITVLQMTPSLFRQFGASSIKDrvlSGSSSLRVLLLGGEPFPSNV--ELVTWMhpsVLMQKHIcnIYGIT 332
Cdd:cd05922 196 DAFWEDLREHGATGLAGVPSTYAMLTRLGFDP---AKLPSLRYLTQAGGRLPQETiaRLRELL---PGAQVYV--MYGQT 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 333 EISCW-SLLHIVQSLQSPVPLGTPIEEDTVLrIESEDNETSQQGELflGSVKRR---CYIPEVDDQANASQDDSGICFRA 408
Cdd:cd05922 268 EATRRmTYLPPERILEKPGSIGLAIPGGEFE-ILDDDGTPTPPGEP--GEIVHRgpnVMKGYWNDPPYRRKEGRGGGVLH 344
|
250 260 270
....*....|....*....|....*....|..
gi 665407183 409 TGDLVTRQQDGTLFYSERSNDVVKRAGNRISL 440
Cdd:cd05922 345 TGDLARRDEDGFLFIVGRRDRMIKLFGNRISP 376
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
166-522 |
1.59e-11 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 67.79 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 166 PLPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPIT-FDPFVVEFFLALQNGATLltsrHS 244
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAhQTGFVYGFTLPLLLGAPV----VL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 245 MRD-SPSKVLSALFPDNL-----ATPGITVLQMTPslfrqfgassikDRVLSGSSSLRVLLLGGEPFPSNVElvtwMHPS 318
Cdd:cd05903 166 QDIwDPDKALALMREHGVtfmmgATPFLTDLLNAV------------EEAGEPLSRLRTFVCGGATVPRSLA----RRAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 319 VLMQKHICNIYGITEIScwsllHIVQSLQSPVPL------GTP-------IEEDT--VLRIESEDNETSQQGELFLGSVK 383
Cdd:cd05903 230 ELLGAKVCSAYGSTECP-----GAVTSITPAPEDrrlytdGRPlpgveikVVDDTgaTLAPGVEGELLSRGPSVFLGYLD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 384 RrcyiPEvddqaNASQDDSGICFRaTGDLVTRQQDGTLFYSERSNDVVKRAGNRISlgliTRKIQKCL---PSSELTTCL 460
Cdd:cd05903 305 R----PD-----LTADAAPEGWFR-TGDLARLDEDGYLRITGRSKDIIIRGGENIP----VLEVEDLLlghPGVIEAAVV 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 461 WLED--LQKLICCIRTLESKTRVqqrvqTFD----ILSKVSIAEQ--PDRFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd05903 371 ALPDerLGERACAVVVTKSGALL-----TFDelvaYLDRQGVAKQywPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
167-449 |
4.67e-11 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 66.34 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 167 LPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLG-TPITFDPFVVEFFLALQNGATLLTSRHSM 245
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQmASFSFDVFAGDFARSLLNGGTLVICPDEV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 246 RDSPskvlsALFPDNLATPGITVLQMTPSLFRqfGASSIKDRVLSGSSSLRVLLLGGEPFPsnVELVTWMHPSVLMQKHI 325
Cdd:cd17650 171 KLDP-----AALYDLILKSRITLMESTPALIR--PVMAYVYRNGLDLSAMRLLIVGSDGCK--AQDFKTLAARFGQGMRI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 326 CNIYGITEISCWSLLHIVQSLQSP----VPLGTPIEEDTVLRIESEDN--ETSQQGELFLGSVK-RRCYIPEVDDQANAS 398
Cdd:cd17650 242 INSYGVTEATIDSTYYEEGRDPLGdsanVPIGRPLPNTAMYVLDERLQpqPVGVAGELYIGGAGvARGYLNRPELTAERF 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 665407183 399 QDD---SGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQK 449
Cdd:cd17650 322 VENpfaPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLAR 375
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
168-546 |
4.83e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRD 247
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAH 3947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 248 SPSKVLSalfpdNLATPGITVLQMTPSLFRQFGASsikDRvlSGSSSLRVLLLGGEPFPSnvELVT-WM--HPSVlmqkH 324
Cdd:PRK05691 3948 DPQGLLA-----HVQAQGITVLESVPSLIQGMLAE---DR--QALDGLRWMLPTGEAMPP--ELARqWLqrYPQI----G 4011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 325 ICNIYGITEIS---CWSLLHIVQSLQSPVPLGTPIEEDTvLRIESEDNETSQQ---GELFL-GSVKRRCYI--PEVDDQA 395
Cdd:PRK05691 4012 LVNAYGPAECSddvAFFRVDLASTRGSYLPIGSPTDNNR-LYLLDEALELVPLgavGELCVaGTGVGRGYVgdPLRTALA 4090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 396 NASQDDSGICFR--ATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRK-------------IQKCLPSSELTTCL 460
Cdd:PRK05691 4091 FVPHPFGAPGERlyRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARlheqaevreaavaVQEGVNGKHLVGYL 4170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 461 WLEDlqkliCCIRTLESKTRVQQRVQtfdilskvsiAEQPDRFV-----YLQHFPCNVHGKLDKQQLlkmciPLAQPAQQ 535
Cdd:PRK05691 4171 VPHQ-----TVLAQGALLERIKQRLR----------AELPDYMVplhwlWLDRLPLNANGKLDRKAL-----PALDIGQL 4230
|
410
....*....|.
gi 665407183 536 ILKSYLHDRLE 546
Cdd:PRK05691 4231 QSQAYLAPRNE 4241
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
45-522 |
6.19e-10 |
|
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: 62.67 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 45 VSYADAADEIQVLMNFLRKNGV-PDEA-GIALRvteHTPASSLMILAILNNKCHFFPTDKMMLSQDLYSQMSTAGVDYLV 122
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVrPGDLvAVTLP---KGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 123 ANKHLTVA-PLYFTFLGSILVFKEdcrlyrvklksADETVQSKKPLPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGL 201
Cdd:cd12114 90 TDGPDAQLdVAVFDVLILDLDALA-----------APAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 202 SQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRDSPskvlsALFPDNLATPGITVLQMTPSLFR---Q 278
Cdd:cd12114 159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDP-----AHWAELIERHGVTLWNSVPALLEmllD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 279 FGASSIKDrvlsgSSSLRVLLLGGEPFPsnVELVTWMHPsVLMQKHICNIYGITEISCWSLLHIVQSLQ---SPVPLGTP 355
Cdd:cd12114 234 VLEAAQAL-----LPSLRLVLLSGDWIP--LDLPARLRA-LAPDARLISLGGATEASIWSIYHPIDEVPpdwRSIPYGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 356 IEEDTVlRIESEDNETSQQ---GELFLGSVK-RRCYI--PEVDDQANASQDDSGICFRaTGDLVTRQQDGTLFYSERSND 429
Cdd:cd12114 306 LANQRY-RVLDPRGRDCPDwvpGELWIGGRGvALGYLgdPELTAARFVTHPDGERLYR-TGDLGRYRPDGTLEFLGRRDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 430 VVKRAGNRISLGLITRKIQKcLPSSELTTCLWLED-----LQKLICCIR---TLESKTRVQQRVQTFDilskvSIAeQPD 501
Cdd:cd12114 384 QVKVRGYRIELGEIEAALQA-HPGVARAVVVVLGDpggkrLAAFVVPDNdgtPIAPDALRAFLAQTLP-----AYM-IPS 456
|
490 500
....*....|....*....|.
gi 665407183 502 RFVYLQHFPCNVHGKLDKQQL 522
Cdd:cd12114 457 RVIALEALPLTANGKVDRAAL 477
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
132-439 |
5.18e-08 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 56.36 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 132 LYFTFLGSILV----------FKEDCRLYRVKLKSADETVQS----KKPLPANMCYTISTTGTTGKPK-LIHVPYECIAP 196
Cdd:cd05969 38 LYFSMLGIGKIgavicplfsaFGPEAIRDRLENSEAKVLITTeelyERTDPEDPTLLHYTSGTTGTPKgVLHVHDAMIFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 197 NIVGlSQKLNVSMADIIYlgtpITFDP-----FVVEFFLALQNGATLLTsrHSMRDSPSKVLSalfpdNLATPGITVLQM 271
Cdd:cd05969 118 YFTG-KYVLDLHPDDIYW----CTADPgwvtgTVYGIWAPWLNGVTNVV--YEGRFDAESWYG-----IIERVKVTVWYT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 272 TPSLFRQFGASSIKDRVLSGSSSLRVLLLGGEPFpsNVELVTWMHPSVLMQKHicNIYGITEISCWSLLHIVQSLQSPVP 351
Cdd:cd05969 186 APTAIRMLMKEGDELARKYDLSSLRFIHSVGEPL--NPEAIRWGMEVFGVPIH--DTWWQTETGSIMIANYPCMPIKPGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 352 LGTPIEEDTVLRIESEDNET--SQQGELFLGS---VKRRCYIPEVDDQANASQDDsgicFRATGDLVTRQQDGTLFYSER 426
Cdd:cd05969 262 MGKPLPGVKAAVVDENGNELppGTKGILALKPgwpSMFRGIWNDEERYKNSFIDG----WYLTGDLAYRDEDGYFWFVGR 337
|
330
....*....|...
gi 665407183 427 SNDVVKRAGNRIS 439
Cdd:cd05969 338 ADDIIKTSGHRVG 350
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
177-432 |
4.55e-07 |
|
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: 53.76 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 177 TTGTTGKPK---LIHvpYECIAPN-IVGLSQKLNVSMADIIYLGTP---ITFDPFVVeffLALQNGATLLTSRhsmrdsp 249
Cdd:cd05911 154 SSGTTGLPKgvcLSH--RNLIANLsQVQTFLYGNDGSNDVILGFLPlyhIYGLFTTL---ASLLNGATVIIMP------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 250 sKVLSALFPDNLATPGITVLQMTPSLFRQFGASSIKDR-VLsgsSSLRVLLLGGEPFPSNV-ELVtwmhPSVLMQKHICN 327
Cdd:cd05911 222 -KFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKyDL---SSLRVILSGGAPLSKELqELL----AKRFPNATIKQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 328 IYGITE---ISCWSLLHIVQ--SLQSPVPLgtpieedTVLRIESEDNETS----QQGEL-FLGSVKRRCYIPevDDQANA 397
Cdd:cd05911 294 GYGMTEtggILTVNPDGDDKpgSVGRLLPN-------VEAKIVDDDGKDSlgpnEPGEIcVRGPQVMKGYYN--NPEATK 364
|
250 260 270
....*....|....*....|....*....|....*.
gi 665407183 398 -SQDDSGicFRATGDLVTRQQDGTLFYSERSNDVVK 432
Cdd:cd05911 365 eTFDEDG--WLHTGDIGYFDEDGYLYIVDRKKELIK 398
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
160-522 |
6.43e-07 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 53.10 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 160 TVQSKKPLPAnmCYTISTtGTTGKPKLI---HVPYECIA---PNIVGLSQklnvsmaDIIYL-GTPITFD-----PFVVE 227
Cdd:cd05920 133 ELAESIPEVA--LFLLSG-GTTGTPKLIprtHNDYAYNVrasAEVCGLDQ-------DTVYLaVLPAAHNfplacPGVLG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 228 FFLAlqNGATLLTSRhsmrDSPSKVLSALfpdnlATPGITVLQMTPSLFRQFGASSIKDRvlSGSSSLRVLLLGGEPFPS 307
Cdd:cd05920 203 TLLA--GGRVVLAPD----PSPDAAFPLI-----EREGVTVTALVPALVSLWLDAAASRR--ADLSSLRLLQVGGARLSP 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 308 nvELVTWMHPSV---LMQkhicnIYGITE-ISCWSLL----HIVQSLQspvplGTPIEEDTVLRIESEDNETSQQGE--- 376
Cdd:cd05920 270 --ALARRVPPVLgctLQQ-----VFGMAEgLLNYTRLddpdEVIIHTQ-----GRPMSPDDEIRVVDEEGNPVPPGEege 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 377 -LFLGSVKRRCYIPEVDDQANASQDDSgicFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKI------QK 449
Cdd:cd05920 338 lLTRGPYTIRGYYRAPEHNARAFTPDG---FYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLlrhpavHD 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 450 C----LPSSEL--TTCLW--LEDLQkliccIRTLESKTRVQQR-VQTFDIlskvsiaeqPDRFVYLQHFPCNVHGKLDKQ 520
Cdd:cd05920 415 AavvaMPDELLgeRSCAFvvLRDPP-----PSAAQLRRFLRERgLAAYKL---------PDRIEFVDSLPLTAVGKIDKK 480
|
..
gi 665407183 521 QL 522
Cdd:cd05920 481 AL 482
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
177-438 |
2.84e-06 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 50.94 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 177 TTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIyLGTPITFD--PFVVEFFLALQNGATLLTSRHSMRDspskvls 254
Cdd:cd05935 92 TSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI-LACLPLFHvtGFVGSLNTAVYVGGTYVLMARWDRE------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 255 aLFPDNLATPGITVLQMTPSLFRQFGAS-SIKDRVLsgsSSLRVLLLGGEPFPSNV-----ELVTWMHpsvlMQkhicnI 328
Cdd:cd05935 164 -TALELIEKYKVTFWTNIPTMLVDLLATpEFKTRDL---SSLKVLTGGGAPMPPAVaekllKLTGLRF----VE-----G 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 329 YGITEISCWSLL--HIVQSLQSpvpLGTPIEEDTVLRIESEDNET---SQQGELFL-GSVKRRCYIPEVDDQANASQDDS 402
Cdd:cd05935 231 YGLTETMSQTHTnpPLRPKLQC---LGIP*FGVDARVIDIETGRElppNEVGEIVVrGPQIFKGYWNRPEETEESFIEIK 307
|
250 260 270
....*....|....*....|....*....|....*.
gi 665407183 403 GICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRI 438
Cdd:cd05935 308 GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
137-451 |
6.24e-06 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 49.74 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 137 LGSILV-----FKEDCRLYRVKLKSADETVQSKKPLPAnmcYTISTTGTTGKPK---------LIHVPYECIAPNIVGLS 202
Cdd:cd05971 54 SGAIAVplfalFGPEALEYRLSNSGASALVTDGSDDPA---LIIYTSGTTGPPKgalhahrvlLGHLPGVQFPFNLFPRD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 203 QKLNVSMADIIYLGTpitfdpFVVEFFLALQNGATLLTSRhSMRDSPSKVLsalfpDNLATPGITVLQMTPS---LFRQF 279
Cdd:cd05971 131 GDLYWTPADWAWIGG------LLDVLLPSLYFGVPVLAHR-MTKFDPKAAL-----DLMSRYGVTTAFLPPTalkMMRQQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 280 GASSIKDRVlsgssSLRVLLLGGEPFPSnvELVTWMHPSvlMQKHICNIYGITEI-----SCWSLLHIvqslqSPVPLGT 354
Cdd:cd05971 199 GEQLKHAQV-----KLRAIATGGESLGE--ELLGWAREQ--FGVEVNEFYGQTECnlvigNCSALFPI-----KPGSMGK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 355 PIEEDTVLRIESEDNET--SQQGELflgSVKRRCYIP--EVDDQANASQDDSGICFRATGDLVTRQQDGTLFYSERSNDV 430
Cdd:cd05971 265 PIPGHRVAIVDDNGTPLppGEVGEI---AVELPDPVAflGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV 341
|
330 340
....*....|....*....|.
gi 665407183 431 VKRAGNRISLGlitrKIQKCL 451
Cdd:cd05971 342 ITSSGYRIGPA----EIEECL 358
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
177-439 |
8.32e-06 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 49.40 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 177 TTGTTGKPKLIHVPY-------ECIAPNIVGLSQklnvsmaDIIYLGTP---ITFDPFVVEFFLALQNGATLLTSRHsmr 246
Cdd:cd05958 105 TSGTTGAPKATMHFHrdplasaDRYAVNVLRLRE-------DDRFVGSPplaFTFGLGGVLLFPFGVGASGVLLEEA--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 247 dSPSKVLSAlfpdnLATPGITVLQMTPSLFRQFGASsiKDRVLSGSSSLRVLLLGGEPFPSNVElVTWmhpsvlmqKHIC 326
Cdd:cd05958 175 -TPDLLLSA-----IARYKPTVLFTAPTAYRAMLAH--PDAAGPDLSSLRKCVSAGEALPAALH-RAW--------KEAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 327 NIYGITEISCWSLLHIVQSLQS----PVPLGTPIEEDTvLRIESEDNETSQQGELFLGSVK--RRCYIPEVDDQANASQD 400
Cdd:cd05958 238 GIPIIDGIGSTEMFHIFISARPgdarPGATGKPVPGYE-AKVVDDEGNPVPDGTIGRLAVRgpTGCRYLADKRQRTYVQG 316
|
250 260 270
....*....|....*....|....*....|....*....
gi 665407183 401 DsgicFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRIS 439
Cdd:cd05958 317 G----WNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
175-519 |
9.46e-06 |
|
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: 48.80 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 175 ISTTGTTGKPK--LIHVPYECIAPNIVgLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHsmrdspSKV 252
Cdd:cd17635 7 IFTSGTTGEPKavLLANKTFFAVPDIL-QKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE------NTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 253 LSALFpDNLATPGITVLQMTPSLFRQFgASSIKDrVLSGSSSLRVLLLGGE-PFPSNVELVTWmHPSVlmqkHICNIYGI 331
Cdd:cd17635 80 YKSLF-KILTTNAVTTTCLVPTLLSKL-VSELKS-ANATVPSLRLIGYGGSrAIAADVRFIEA-TGLT----NTAQVYGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 332 TEISCWSLLHIVQSLQSPVPLGTPIE--EDTVLRIESEDNETSQQGELFLGSvkrrcyiPEVDDQANASQDDSGICFRA- 408
Cdd:cd17635 152 SETGTALCLPTDDDSIEINAVGRPYPgvDVYLAATDGIAGPSASFGTIWIKS-------PANMLGYWNNPERTAEVLIDg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 409 ---TGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKcLPSSELTTCLWLED-----LQKLICCIRTLESKTR 480
Cdd:cd17635 225 wvnTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEG-VSGVQECACYEISDeefgeLVGLAVVASAELDENA 303
|
330 340 350
....*....|....*....|....*....|....*....
gi 665407183 481 VQQRVQTfdILSKVSIAEQPDRFVYLQHFPCNVHGKLDK 519
Cdd:cd17635 304 IRALKHT--IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
293-443 |
9.57e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 49.02 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 293 SSLRVLLLGGEPFPsnVELVTWMHPSVLMQkhICNIYGITEISCWSLLHIVQSLQSPVPLGTPIEEDTVlRIESEDNETS 372
Cdd:cd05944 121 SSLRFAMSGAAPLP--VELRARFEDATGLP--VVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARV-RIKVLDGVGR 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665407183 373 QQ-----GELFLGSVKRRCYIPEVDDQANASQDDSGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLI 443
Cdd:cd05944 196 LLrdcapDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALI 271
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
156-438 |
1.30e-05 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 49.03 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 156 SADETVQSKKPLPANM-----CYTISTTGTTGKPK-LIHV----PYECIApnivGLSQKLNVSMADIIYLGTPITF--DP 223
Cdd:cd05968 218 SYDEEKETAGDGAERTesedpLMIIYTSGTTGKPKgTVHVhagfPLKAAQ----DMYFQFDLKPGDLLTWFTDLGWmmGP 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 224 FVVefFLALQNGATLLTSrHSMRDSPSkvlsalfPDNL----ATPGITVLQMTPSLFRQFGASSIKDRVLSGSSSLRVLL 299
Cdd:cd05968 294 WLI--FGGLILGATMVLY-DGAPDHPK-------ADRLwrmvEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 300 LGGEPFpsNVELVTWMHPSVLM-QKHICNIYGITEIS----CWSLLHIVQ--SLQSPVPlGTpieeDTVLRIESEDNETS 372
Cdd:cd05968 364 STGEPW--NPEPWNWLFETVGKgRNPIINYSGGTEISggilGNVLIKPIKpsSFNGPVP-GM----KADVLDESGKPARP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 373 QQGEL------------FLGSVKR--RCYIPEVDDqanasqddsgicFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRI 438
Cdd:cd05968 437 EVGELvllapwpgmtrgFWRDEDRylETYWSRFDN------------VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRV 504
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
175-524 |
1.43e-05 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 48.98 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 175 ISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFdpfVVEFFlalqNGAT---LLTSRHSMRD--SP 249
Cdd:PRK06087 193 LFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH---ATGFL----HGVTapfLIGARSVLLDifTP 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 250 SKVLSALFPDNL-----ATPGI----TVLQMTPSLFrqfgassikdrvlsgsSSLRVLLLGGEPFPSNVELVTWMHPSVL 320
Cdd:PRK06087 266 DACLALLEQQRCtcmlgATPFIydllNLLEKQPADL----------------SALRFFLCGGTTIPKKVARECQQRGIKL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 321 mqkhiCNIYGITEiscwSLLHIVQSLQSPVPL-----GTPIEEDTVlRIESEDNET---SQQGE-------LFLGsvkrr 385
Cdd:PRK06087 330 -----LSVYGSTE----SSPHAVVNLDDPLSRfmhtdGYAAAGVEI-KVVDEARKTlppGCEGEeasrgpnVFMG----- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 386 cYIPEVDDQANAsQDDSGICFraTGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKC-LPSSELTTCLWLED 464
Cdd:PRK06087 395 -YLDEPELTARA-LDEEGWYY--SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHpKIHDACVVAMPDER 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665407183 465 LQKLICCIRTLESKTRVQQRVQTFDILSKVSIAEQ--PDRFVYLQHFPCNVHGKLDKQQLLK 524
Cdd:PRK06087 471 LGERSCAYVVLKAPHHSLTLEEVVAFFSRKRVAKYkyPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
168-450 |
2.94e-05 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 47.59 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 168 PANMCYTistTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIylgtpITFDPF--VVE----FFLALQNGAtllTS 241
Cdd:cd05907 89 LATIIYT---SGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH-----LSFLPLahVFErragLYVPLLAGA---RI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 242 RHSmrdSPSKVLSalfpDNLATPGITVLQMTPSLFRQF-------GASSIKDRVL---SGsSSLRVLLLGGEPFPsnVEL 311
Cdd:cd05907 158 YFA---SSAETLL----DDLSEVRPTVFLAVPRVWEKVyaaikvkAVPGLKRKLFdlaVG-GRLRFAASGGAPLP--AEL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 312 VTWMHPSVLmqkHICNIYGITE----ISCWSLLHI-VQSLQSPVPlgtpieeDTVLRIeSEDNETSQQGE-LFLGSVKRr 385
Cdd:cd05907 228 LHFFRALGI---PVYEGYGLTEtsavVTLNPPGDNrIGTVGKPLP-------GVEVRI-ADDGEILVRGPnVMLGYYKN- 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665407183 386 cyiPEVDDQAnasQDDSGicFRATGDLVTRQQDGTLFYSERSNDVVKRAGNR-ISLGLITRKIQKC 450
Cdd:cd05907 296 ---PEATAEA---LDADG--WLHTGDLGEIDEDGFLHITGRKKDLIITSGGKnISPEPIENALKAS 353
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
45-438 |
1.95e-04 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 45.03 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 45 VSYADAADEIQVLMNFLRKNGVPDEAGIALrVTEHTPASSLMILAilnnkchffptdkmmlsqdlysqMSTAGVDYLVAN 124
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVAL-LSKNSIEMILLIHA-----------------------LWLLGAEAVLLN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 125 KHLTVAPLYFtflgsilvfkedcrlyrvKLKSADetvqSKKPLPANMCYTistTGTTGKPKLIHVPYE------------ 192
Cdd:cd05912 58 TRLTPNELAF------------------QLKDSD----VKLDDIATIMYT---SGTTGKPKGVQQTFGnhwwsaigsaln 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 193 ----------CIAP--NIVGLSqklnVSMADIIYlGTPITfdpfVVEFFlalqngatlltsrhsmrdSPSKVLSALfpdn 260
Cdd:cd05912 113 lglteddnwlCALPlfHISGLS----ILMRSVIY-GMTVY----LVDKF------------------DAEQVLHLI---- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 261 lATPGITVLQMTPSLFRQfgassIKDRVLSG-SSSLRVLLLGGEPFPsnvelvtwmhPSVLMQKHICNI-----YGITEI 334
Cdd:cd05912 162 -NSGKVTIISVVPTMLQR-----LLEILGEGyPNNLRCILLGGGPAP----------KPLLEQCKEKGIpvyqsYGMTET 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 335 SCWSL-LHIVQSLQSPVPLGTPIeEDTVLRIESEDNETSQQGELFL-GSVKRRCYIPEVDDQANASQDDsgicFRATGDL 412
Cdd:cd05912 226 CSQIVtLSPEDALNKIGSAGKPL-FPVELKIEDDGQPPYEVGEILLkGPNVTKGYLNRPDATEESFENG----WFKTGDI 300
|
410 420
....*....|....*....|....*.
gi 665407183 413 VTRQQDGTLFYSERSNDVVKRAGNRI 438
Cdd:cd05912 301 GYLDEEGFLYVLDRRSDLIISGGENI 326
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
170-519 |
3.30e-04 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 43.93 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 170 NMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRhsmRDSP 249
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 250 SKVLSALFPDNlATPGITVLQMTPSLFR-QFGASSIKDrVLSGSSSLrvlllggepFPSNVELVTWMHPsvlmQKHICNI 328
Cdd:cd17633 78 KSWIRKINQYN-ATVIYLVPTMLQALARtLEPESKIKS-IFSSGQKL---------FESTKKKLKNIFP----KANLIEF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 329 YGITEISCWSLLhIVQSLQSPVPLGTPIEEdtvLRIESEDNETSQQGELFLGSVKR-RCYIpevddQANASQDDSGIcfr 407
Cdd:cd17633 143 YGTSELSFITYN-FNQESRPPNSVGRPFPN---VEIEIRNADGGEIGKIFVKSEMVfSGYV-----RGGFSNPDGWM--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 408 ATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKClPSSELTTCLWLEDL---QKLICCIrtlESKTRVQQR 484
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAI-PGIEEAIVVGIPDArfgEIAVALY---SGDKLTYKQ 286
|
330 340 350
....*....|....*....|....*....|....*
gi 665407183 485 VQTFdILSKVSIAEQPDRFVYLQHFPCNVHGKLDK 519
Cdd:cd17633 287 LKRF-LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
731-981 |
7.44e-04 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 43.00 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 731 YDGCLYGFNPQTGNIVFRVGIGGLIKSQPmlTADGRRIIVCSYADDynVYCLSAERQEVLWCLRI-GEkpIFASPleLPR 809
Cdd:TIGR03300 73 ADGTVAALDAETGKRLWRVDLDERLSGGV--GADGGLVFVGTEKGE--VIALDAEDGKELWRAKLsSE--VLSPP--LVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 810 EQSLIVCTLDGSYSRVAITDGSVEWTQKFREPVF-----STPVLlesVSNIFLSAEVAGRVHACHVGNGKILAT----FS 880
Cdd:TIGR03300 145 NGLVVVRTNDGRLTALDAATGERLWTYSRVTPPLtlrgsASPVI---ADGGVLVGFAGGKLVALDLQTGQPLWEqrvaLP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 881 TEGNIFSSLV-VKTPPTFMGHS-FAI-----FGCIDQhlyclrcKTGpggksvelELHWKVDVGApiYATPtllTVQPNG 953
Cdd:TIGR03300 222 KGRTELERLVdVDGDPVVDGGQvYAVsyqgrVAALDL-------RSG--------RVLWKRDASS--YQGP---AVDDNR 281
|
250 260
....*....|....*....|....*....
gi 665407183 954 LLVwcAATDGRVMLINFRNGEIQWS-DKL 981
Cdd:TIGR03300 282 LYV--TDADGVVVALDRRSGSELWKnDEL 308
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
925-1010 |
8.31e-04 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 42.88 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 925 SVELELHWKVDVGAPIYATPTLLTVQPNGLLVWCAATDGRVMLINFRNGEIQWSDKLpGQVFSS---AcfieDLRRVFVG 1001
Cdd:COG1520 29 SVKVKQLWSASVGDGVGKGYSRLAPAVAGDRVYAADADGRVAALDAATGKELWRVDL-GEPLSGgvgA----DGGLVVVG 103
|
....*....
gi 665407183 1002 CRDNFLYCL 1010
Cdd:COG1520 104 TEDGEVIAL 112
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
279-432 |
2.13e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 42.01 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 279 FGASS-IKDRVlsgSSSLRVLLLGGEPFPSNV--ELvtwmhpSVLMQKHICNIYGITEiSCWSLLHIVQSLQSPVPLGTP 355
Cdd:PTZ00342 449 THISSkIKDKV---NPNLEVILNGGGKLSPKIaeEL------SVLLNVNYYQGYGLTE-TTGPIFVQHADDNNTESIGGP 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 356 IEEDTVLRIES----EDNETSQQGELFLGSVKRRC-YIPEVDDQANASQDDSgicFRATGDLVTRQQDGTLFYSERSNDV 430
Cdd:PTZ00342 519 ISPNTKYKVRTwetyKATDTLPKGELLIKSDSIFSgYFLEKEQTKNAFTEDG---YFKTGDIVQINKNGSLTFLDRSKGL 595
|
..
gi 665407183 431 VK 432
Cdd:PTZ00342 596 VK 597
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
694-791 |
3.48e-03 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 41.07 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 694 LRTLNPQTGSEYSVVKLPERIECKVTfLTEQLAMVGCYDGCLYGFNPQTGNIVFRVGIGGLIKSQPmLTADGRRIIVCSy 773
Cdd:TIGR03300 77 VAALDAETGKRLWRVDLDERLSGGVG-ADGGLVFVGTEKGEVIALDAEDGKELWRAKLSSEVLSPP-LVANGLVVVRTN- 153
|
90
....*....|....*...
gi 665407183 774 adDYNVYCLSAERQEVLW 791
Cdd:TIGR03300 154 --DGRLTALDAATGERLW 169
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
656-791 |
3.67e-03 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 40.95 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407183 656 QPVLKLQIYWKVNfekcIDSPVTEYEGRF--------ICVGAHSKILRTLNPQTGSEYSVVKLPERIECKVTfLTEQLAM 727
Cdd:COG1520 27 EPSVKVKQLWSAS----VGDGVGKGYSRLapavagdrVYAADADGRVAALDAATGKELWRVDLGEPLSGGVG-ADGGLVV 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665407183 728 VGCYDGCLYGFNPQTGNIVFRVGIGGLIKSQPmLTADGrRIIVcsYADDYNVYCLSAERQEVLW 791
Cdd:COG1520 102 VGTEDGEVIALDADDGEELWRARLSSEVLAAP-AVAGG-RVVV--RTGDGRVYALDAATGERLW 161
|
|
| PQQ_3 |
pfam13570 |
PQQ-like domain; |
973-1010 |
5.09e-03 |
|
PQQ-like domain;
Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 35.64 E-value: 5.09e-03
10 20 30
....*....|....*....|....*....|....*...
gi 665407183 973 GEIQWSDKLPGQVFSSACFIEDLrrVFVGCRDNFLYCL 1010
Cdd:pfam13570 1 GEVLWRFETGGPIVSSPAVAGGL--VYVGTGDGTLYAL 36
|
|
|