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Conserved domains on  [gi|665407183|ref|NP_995660|]
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Aminoadipate-semialdehyde dehydrogenase, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

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
PQQ_2 super family cl38403
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.


The actual alignment was detected with superfamily member pfam13360:

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
PQQ super family cl34291
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];


The actual alignment was detected with superfamily member COG1520:

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
 
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
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
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
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
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
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
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
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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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